Biomineralización de tejidos calcificados

Este libro responde a la necesidad de presentar a los estudiantes de Odontología y de cursos básicos de posgrado en ciencias biomédicas u odontológicas los fundamentos y mecanismos del fenómeno de biomineralización de tejidos dentales. Se trata de un proceso dinámico y complejo llevado a cabo por cé...

Full description

Autores:: Mejía Naranjo, Wilson
Beltrán Zúñiga, Edgar O.

Tipo de recurso:: Book

Fecha de publicación:: 2022

Institución:: Universidad El Bosque

Repositorio:: Repositorio U. El Bosque

Idioma:

id	UNBOSQUE2_c2ca168d5dca9d89924687813c4b95e6
oai_identifier_str	oai:repositorio.unbosque.edu.co:20.500.12495/9051
network_acronym_str	UNBOSQUE2
network_name_str	Repositorio U. El Bosque
repository_id_str
dc.title.spa.fl_str_mv	Biomineralización de tejidos calcificados
title	Biomineralización de tejidos calcificados
spellingShingle	Biomineralización de tejidos calcificados Biomineralización Ciencia de los materiales Cristalización Biomateriales Calcificación Biomineralization Material science Crystallization Biomaterials Calcification
title_short	Biomineralización de tejidos calcificados
title_full	Biomineralización de tejidos calcificados
title_fullStr	Biomineralización de tejidos calcificados
title_full_unstemmed	Biomineralización de tejidos calcificados
title_sort	Biomineralización de tejidos calcificados
dc.creator.fl_str_mv	Mejía Naranjo, Wilson Beltrán Zúñiga, Edgar O.
dc.contributor.author.none.fl_str_mv	Mejía Naranjo, Wilson Beltrán Zúñiga, Edgar O.
dc.subject.spa.fl_str_mv	Biomineralización Ciencia de los materiales Cristalización Biomateriales Calcificación
topic	Biomineralización Ciencia de los materiales Cristalización Biomateriales Calcificación Biomineralization Material science Crystallization Biomaterials Calcification
dc.subject.keywords.spa.fl_str_mv	Biomineralization Material science Crystallization Biomaterials Calcification
description	Este libro responde a la necesidad de presentar a los estudiantes de Odontología y de cursos básicos de posgrado en ciencias biomédicas u odontológicas los fundamentos y mecanismos del fenómeno de biomineralización de tejidos dentales. Se trata de un proceso dinámico y complejo llevado a cabo por células especializadas, mediante el cual ocurren la secreción y deposición de minerales de calcio y fosfato inorgánicos, los cuales interactúan de forma organizada con proteínas nucleadoras en una matriz extracelular para generar tejidos mineralizados altamente funcionales. Las células especializadas son los ameloblastos, los odontoblastos, los cementoblastos y los osteoblastos, responsables respectivamente de la producción de esmalte, dentina, cemento y hueso. Comprender los procesos de biomineralización y las dinámicas de mineralización y remineralización es importante para prevenir y tratar las enfermedades causadas por una mineralización anormal y/o defectuosa de los tejidos calcificados.
publishDate	2022
dc.date.accessioned.none.fl_str_mv	2022-09-20T13:42:03Z
dc.date.available.none.fl_str_mv	2022-09-20T13:42:03Z
dc.date.issued.none.fl_str_mv	2022
dc.type.none.fl_str_mv	book
dc.type.local.spa.fl_str_mv	Libro completo
dc.type.hasversion.none.fl_str_mv	info:eu-repo/semantics/publishedVersion
dc.type.coar.none.fl_str_mv	http://purl.org/coar/resource_type/c_2f33
dc.type.driver.none.fl_str_mv	info:eu-repo/semantics/book
dc.type.coarversion.none.fl_str_mv	http://purl.org/coar/version/c_970fb48d4fbd8a85
format	http://purl.org/coar/resource_type/c_2f33
status_str	publishedVersion
dc.identifier.isbn.none.fl_str_mv	9789587392760 9789587392814 9789587392753
dc.identifier.uri.none.fl_str_mv	http://hdl.handle.net/20.500.12495/9051
dc.identifier.instname.spa.fl_str_mv	instname:Universidad El Bosque
dc.identifier.reponame.spa.fl_str_mv	reponame:Repositorio Institucional Universidad El Bosque
dc.identifier.repourl.none.fl_str_mv	repourl:https://repositorio.unbosque.edu.co
identifier_str_mv	9789587392760 9789587392814 9789587392753 instname:Universidad El Bosque reponame:Repositorio Institucional Universidad El Bosque repourl:https://repositorio.unbosque.edu.co
url	http://hdl.handle.net/20.500.12495/9051
dc.relation.references.spa.fl_str_mv	Bronckers, A. L. J. J., Lyaruu, D. M., & DenBesten, P. K. (2009). The impact of fluoride on ameloblasts and the mechanisms of enamel fluorosis. Journal of Dental Research, 88(10), 877-893. https://doi.org/10.1177/0022034509343280 Cameron, F. K., & Seidell, A. (1904). The action of water upon the phosphates of calcium. Journal of the American Chemical Society, 26(11), 1454-1463. https://doi.org/10.1021/ja02001a007 Castiblanco, G. A., Rutishauser, D., Ilag, L. L., Martignon, S., Castellanos, J. E., & Mejía, W. (2015). Identification of proteins from human permanent erupted enamel. European Journal of Oral Sciences, 123(6), 390-395. https://doi.org/10.1111/eos.12214 Dorozhkin, S. V. (2011). Calcium orthophosphates: Occurrence, properties, biomineralization, pathological calcification and biomimetic applications. Biomatter, 1(2), 121-164. https://doi.org/10.4161/biom.18790 Dreesmann, H. (1892). Ueber knochenplombierung. Beitr Klin Chir, 9, 804-810. Evans, J. S. (2017). Polymorphs, proteins, and nucleation theory: A critical analysis. Minerals (2075-163X), 7(4):62. https://doi.org/10.3390/min7040062 Evans, J. S. (2019). Composite materials design: Biomineralization proteins and the guided assembly and organization of biomineral nanoparticles. Materials (Basel, Switzerland), 12(4). https://doi.org/10.3390/ma12040581 Furtos, G., Lesci, I. G., Šiller, L., Marin, F., Brümmer, F., & Checa, A. (2015). Biomineralization: From fundamentals to biomaterials & environmental issues. Pfaffikon, Switzerland: Trans Tech Publications Ltd. Retrieved from http://ezproxy.javeriana.edu.co:2048/login?url=https://search.ebscohost.com/login.aspx?direct=true&db=e000xww&AN=1165291&lang=es&site=ehost-live Gower, L. B. (2008). Biomimetic model systems for investigating the amorphous precursor pathway and its role in biomineralization. Chemical Reviews, 108(11), 4551-4627. https://doi.org/10.1021/cr800443h Kay, M. I., Young, R. A., & Posner, A. S. (1964). Crystal structure of hydroxyapatite. Nature, 204(4963), 1050-1052. https://doi.org/10.1038/2041050a0 Lafisco, M., Delgado López, J., & Drouet, C. (2014). Nanocrystaline apatites: Synthesis, physical-cehmical and thermodynamic characterization. In M. Lafisco, & J. Delgado López (Eds.), Apatite (pp. 49-80) Nova Science Publishers, Inc. Lide, D. (2005). The CRC handbook of chemistry and physics. CRC Press, Boca Ratón, Florida, 86, 2544. Madupalli, H., Pavan, B., & Tecklenburg, M. (2017). Carbonate substitution in the mineral component of bone: Discriminating the structural changes, simultaneously imposed by carbonate in A and B sites of apatite. J Solid State Chem. 255:27-35. https://doi.org/10.1016/j.jssc.2017.07.025 Omelon, S. J., & Grynpas, M. D. (2008). Relationships between polyphosphate chemistry, biochemistry and apatite biomineralization. Chemical Reviews, 108(11), 4694-4715. https://doi.org/10.1021/cr0782527 Posner, A. S., & Betts, F. (1975). Synthetic amorphous calcium phosphate and its relation to bone mineral structure. Accounts of Chemical Research, 8(8), 273-281. https://doi.org/10.1021/ar50092a003 Ramirez-Rodríguez, G., Delgado-López, J., & Gomez-Morales, J. (2013). Evolution of calcium phosphate precipitatation in hanging drop vapor infussion by in situ raman microspectroscopy. CrystEngComm, 15, 2206. Rodríguez-Navarro, A. B., Marie, P., Nys, Y., Hincke, M. T., & Gautron, J. (2015). Amorphous calcium carbonate controls avian eggshell mineralization: A new paradigm for understanding rapid eggshell calcification. Journal of Structural Biology, 190(3), 291-303. https://doi.org/10.1016/j.jsb.2015.04.014 Sharma, R., Tsuchiya, M., Skobe, Z., Tannous, B. A., & Bartlett, J. D. (2010). The acid test of fluoride: How pH modulates toxicity. PLoS ONE, 5(-5), -e10895. https://doi.org/10.1371/journal.pone.0010895 Simmer, J. P., & Fincham, A. G. (1995). Molecular mechanisms of dental enamel formation. Critical Reviews in Oral Biology & Medicine, 6(2), 84-108. https://doi.org/10.1177/10454411950060020701 Yao, S., Jin, B., Liu, Z., Shao, C., Zhao, R., Tang, R., & Wang, X. (2017). Biomineralization: From material tactis to biological strategy. Adv Mater, 29(14). https://doi.org/10.1002/adma.201605903 Zahn, D. (2015). Thermodynamics and kinetics of prenucleation clusters, classical and non-classical nucleation. ChemPhysChem, 16(10), 2069-2075. https://doi.org/10.1002/cphc.201500231 Aoba, T., & Fejerskov, O. (2002). Dental fluorosis: Chemistry and biology. Crit Rev Oral Biol & Med., 13(2), 155-170. https://doi.org/10.1177/154411130201300206 Bansal, A., Shetty, D., Bindal, R., & Pathak, A. (2012). Amelogenin: Novel protein with diverse applications in genetic and molecular profiling. Oral Maxillofac Pathol J, 16, 395-399. https://doi.org/10.4103/0973-029X.102495 Bartlett, J. D., & Simmer, J. P. (2015). New perspectives on amelotin and amelogenesis. J Dent Res., 94(5), 642-644. https://doi.org/10.1177/0022034515572442 Bartlett, J. D., Ganss, B., Goldberg, M., Moradian-Oldak, J., Paine, M. L., Snead, M. L., . . . Zhou, Y. L. (2006). Protein–Protein interactions of the developing enamel matrix. Current Topics in Developmental Biology, 74, 57-115. https://doi.org/10.1016/S0070-2153(06)74003-0 Bouropoulos, N., & Moradian-Oldak, J. (2004). Induction of apatite by the cooperative effect of amelogenin and the 32-kDa enamelin. Journal of Dental Research, 83(4), 278-282. https://doi.org/10.1177/154405910408300402 Bromley, K. M., Kiss, A. S., Lokappa, S. B., Lakshminarayanan, R., Fan, D., Ndao, M., . . . Moradian-Oldak, J. (2011). Dissecting amelogenin protein nanospheres: Characterization of metastable oligomers. Journal of Biological Chemistry, 286(40), 34643-34653. https://doi.org/10.1074/jbc.M111.250928 Bronckers, A. L. J. J., Lyaruu, D. M., & DenBesten, P. K. (2009). The impact of fluoride on ameloblasts and the mechanisms of enamel fluorosis. Journal of Dental Research, 88(10), 877-893. https://doi.org/10.1177/0022034509343280 Castiblanco, G. A., Rutishauser, D., Ilag, L. L., Martignon, S., Castellanos, J. E., & Mejía, W. (2015). Identification of proteins from human permanent erupted enamel. European Journal of Oral Sciences, 123(6), 390-395. https://doi.org/10.1111/eos.12214 Carey, C. M. (2014). Focus on fluorides: Update on the use of fluoride for the prevention of dental caries. Journal of Evidence Based Dental Practice, 14, 95-102. https://doi.org/10.1016/j.jebdp.2014.02.004 Fincham, A. G., Belcourt, A. B., Termine, J. D., Butler, W. T., & Cothran, W. C. (1981). Dental enamel matrix: Sequences of two amelogenin polypeptides. Bioscience Reports, 1(10), 771-778. https://doi.org/10.1007/BF01114799 Fincham, A. G., Moradian-Oldak, J., & Simmer, J. P. (1999). The structural biology of the developing dental enamel matrix. Journal of Structural Biology, 126(3), 270-299. https://doi.org/10.1006/jsbi.1999.4130 Gallon, V., Chen, L., Yang, X., & Moradian-Oldak, J. (2013). Localization and quantitative co-localization of enamelin with amelogenin. Journal of Structural Biology, 183(2), 239-249. https://doi.org/10.1016/j.jsb.2013.03.014 Hu, J. C. -., Zhang, C. H., Yang, Y., Kärrman-MÅrdh, C., Forsman-Semb, K., & Simmer, J. P. (2001). Cloning and characterization of the mouse and human enamelin genes. J Dent Res., 80(3), 898-902. https://doi.org/10.1177/00220345010800031001 Hu, J. C. -., Hu, Y., Lu, Y., Smith, C. E., Lertlam, R., Wright, J. T., . . . Simmer, J. P. (2014). Enamelin is critical for ameloblast integrity and enamel ultrastructure formation. PLoS ONE, 9(3), e89303. https://doi.org/10.1371/journal.pone.0089303 Hu, Y., Smith, C. E., Richardson, A. S., Bartlett, J. D., Hu, J. C. C., & Simmer, J. P. (2016). MMP20, KLK4, and MMP20/KLK4 double null mice define roles for matrix proteases during dental enamel formation. Molecular Genetics & Genomic Medicine, 4(2), 178-196. https://doi.org/10.1002/mgg3.194 Kidd, E., & Fejerskov, O. (2016). Essentials of dental caries. p. 6. Oxford: OUP Oxford. Lacruz, R. S., Smith, C. E., Kurtz, I., Hubbard, M. J., & Paine, M. L. (2012). New paradigms on the transport functions of maturation-stage ameloblasts. Journal of Dental Research, 92(2), 122-129. https://doi.org/10.1177/0022034512470954 Lacruz, R. S., Habelitz, S., Timothy Wright, J., & Paine, M. L. (2017). Dental enamel formation and implications for oral health and disease. Physiological Reviews, 97(3), 939-993. https://doi.org/10.1152/physrev.00030.2016 Le Norcy, E., Kwak, S., Wiedemann-Bidlack, F. B., Beniash, E., Yamakoshi, Y., Simmer, J. P., & Margolis, H. C. (2011). Leucine-rich amelogenin peptides regulate mineralization in vitro. Journal of Dental Research, 90(9), 1091-1097. https://doi.org/10.1177/0022034511411301 Lu, Y., Papagerakis, P., Yamakoshi, Y., Hu, J., Bartlett, J., & Simmer, J. (2008). Functions of KLK4 and MMP-20 in dental enamel formation. Biological Chemistry, 389(6), 695-700. https://doi.org/10.1515/BC.2008.080 Margolis, H. C., Beniash, E., & Fowler, C. E. (2006). Role of macromolecular assembly of enamel matrix proteins in enamel formation. Journal of Dental Research, 85(9), 775-793. https://doi.org/10.1177/154405910608500902 Moradian-Oldak, J. (2012). Protein- mediated enamel mineralization. Frontiers in Bioscience : A Journal and Virtual Library, 17, 1996-2023. Nagano, T., Kakegawa, A., Yamakoshi, Y., Tsuchiya, S., Hu, J. C. -., Gomi, K., . . . Simmer, J. P. (2009). Mmp-20 and Klk4 cleavage site preferences for amelogenin sequences. Journal of Dental Research, 88(9), 823-828. https://doi.org/10.1177/0022034509342694 Sharma, R., Tsuchiya, M., Skobe, Z., Tannous, B. A., & Bartlett, J. D. (2010). The acid test of fluoride: How pH modulates toxicity. - PLoS ONE, 5(- 5), -e10895. https://doi.org/10.1371/journal.pone.0010895 Simmer, J. P., & Fincham, A. G. (1995). Molecular mechanisms of dental enamel formation. Critical Reviews in Oral Biology & Medicine, 6(2), 84-108. https://doi.org/10.1177/10454411950060020701 Sire, J., Delgado, S., Frometin, D., & Girondot, M. (2005). Amelogenin: Lessons from evolution. Archives of Oral Biology, (- 2), 205-212. https://doi.org/10.1016/j.archoralbio.2004.09.004 Teepe, J. D., Schmitz, J. E., Hu, Y., Yamada, Y., Fajardo, R. J., Smith, C. E., & Chun, Y. P. (2014). Correlation of ameloblastin with enamel mineral content. Connect Tissue Res, 55, 38-42. https://doi.org/10.3109/03008207.2014.923871 Veis, A., & Dorvee, J. (2013). Biomineralization mechanisms: A new paradigm for crystal nucleation in organic matrices. Calcified Tissue International, 93(4), 307-315. https://doi.org/10.1007/s00223-012-9678-2 Weatherell, J., Deutsch, D., Robinson, C., & Hallsworth, A. (1975). Fluoride concentrations in developing enamel. Nature, 256(5514), 230-232. https://doi.org/10.1038/256230a0 Akiva, A., Kerschnitzki, M., Pinkas, I., Wagermaier, W., Yaniv, K., Fratzl, P., .Weiner, S. (2016). Mineral formation in the larval zebrafish tail bone occurs via an acidic disordered calcium phosphate phase. Journal of the American Chemical Society, 138(43), 14481-14487. https://doi.org/10.1021/jacs.6b09442 Alvares, K. (2014). The role of acidic phosphoproteins in biomineralization. Connective Tissue Research, 55(1), 34-40. https://doi.org/10.3109/03008207.2013.867336 Arana-Chavez, V. E., & Massa, L. F. (2004). Odontoblasts: The cells forming and maintaining dentine. Int J Biochem Cell Biol, 36(8), 1367-1373 https://doi.org/10.1016/j.biocel.2004.01.006 Beniash, E. (2011). Biominerals-hierarchical nanocomposites: The example of bone. Wiley Interdisciplinary Reviews: Nanomedicine and Nanobiotechnology, 3(1), 47-69 https://doi.org/10.1002/wnan.105 Bertassoni, L., & Swain, M. (2017). Removal of dentin non-collagen structures results in the unraveling of microfibril bundless in collagen type I. Connect Tissue Res, 58(5), 414-423. https://doi.org/10.1080/03008207.2016.1235566 Bertassoni, L. E., Orgel, J. P. R., Antipova, O., & Swain, M. V. (2012). The dentin organic matrix – limitations of restorative dentistry hidden on the nanometer scale. Acta Biomaterialia, 8(7), 2419-2433. https://doi.org/10.1016/j.actbio.2012.02.022 Bertassoni, L. E., Habelitz, S., Kinney, J. H., Marshall, S. J., & Marshall Jr., G. W. (2009). Biomechanical perspective on the remineralization of dentin. Caries Research, 43(1), 70-77. https://doi.org/0.1159/000201593 Bertassoni, L. E. (2017). Dentin on the nanoscale: Hierarchical organization, mechanical behavior and bioinspired engineering. Dental Materials, 33, 637-649. https://doi.org/10.1016/j.dental.2017.03.008 Bleicher, F. (2014). Odontoblast physiology. Exp Cell Res, 325(2), 65-71. https://doi.org/10.1016/j.yexcr.2013.12.012 Bonar, L. C., Lees, S., & Mook, H. A. (1985). Neutron diffraction studies of collagen in fully mineralized bone. J Mol Biol, 181(2), 265-270. http://doi.org/10.1016/0022-2836(85)90090-7 Bonucci, E. (2002). Crystal ghost and biological mineralization: Fancy spectres in an old castle, or negelcted structures worthy of belief. J. Bone. Miner. Metab, 20(5), 249-265. https://doi.org/10.1007/s007740200037 Boonrungsiman, S., Gentleman, E., Carzaniga, R., Evans, N. D., McComb, D. W., Porter, A. E., & Stevens, M. M. (2012). The role of intracellular calcium phosphate in osteoblast-mediated bone apatite formation. Proc Natl Acad Sci U S A., 109(35), 14170-14175. https://doi.org/10.1073/pnas.1208916109 Butler, W. T., Brunn, J. C., & Qin, C. (2003). Dentin extracellular matrix (ECM) proteins: Comparison to bone ECM and contribution to dynamics of dentinogenesis. Connective Tissue Research, 44(1), 171-178. https://doi.org/10.1080/03008200390152287 Cao, Y. C., Mei, L. M., Li, Q., Lo, C. E., & Chu, H. C. (2015). Methods for biomimetic remineralization of human dentine: A systematic review. Int. J. Mol. Sci, 16(3), 4615-4627. https://doi.org/10.3390/ijms16034615 Colfen, H. (2010). Biomineralization: A crystal-clear view. Nat Mater, 9(12), 960-961. https://doi.org/10.1038/nmat2911 Dorozhkin, S. V. (2017). Hydroxyapatite and other calcium orthophosphates: Nanodimensional, multiphasic and amorphous formulations. New York: Nova Science Publishers, Inc. Retrieved from http://ezproxy.javeriana.edu.co:2048/login?url=https://search.ebscohost.com/login.aspx?direct=true&db=e000xww&AN=1530704&lang=es&site=ehost-live Embery, G., Hall, R., Waddington, R., Septier, D., & Goldberg, M. (2001). Proteoglycans in dentinogenesis. Crit Rev Oral Biol & Med, 12(4), 331-349. https://doi.org/10.1177/10454411010120040401 Fisher, L. W., & Fedarko, N. S. (2003). Six genes expressed in bones and teeth encode the current members of the SIBLING family of proteins. Connect Tissue Res, 44(Suppl 1), 33-40. Gericke, A., Qin, C., Sun, Y., Redfern, R., Redfern, D., Fujimoto, Y., . . . Boskey, A. L. (2010). Different forms of DMP1 play distinct roles in mineralization. J Dent Res, 89(4), 355-359. https://doi.org/10.1177/0022034510363250 Goldberg, M., Kulkarni, A., Young, M., & Boskey, A. (2011). Dentin: Structure, composition and mineralization. Front Biosci, 3(2), 711-735. https://doi.org/10.2741/e281 Hao, J., Zou, B., Narayanan, K., & George, A. (2004). Differential expression patterns of the dentin matrix proteins during mineralized tissue formation. Bone, 34(6), 921-932 https://doi.org/10.1016/j.bone.2004.01.020 He, G., Dahl, T., Veis, A., & George, A. (2003). Nucleation of apatite crystals in vitro by self-assembled dentin matrix protein 1. Nat Mater, 2(8), 552-558. https://www.nature.com/articles/nmat945 He, G., & George, A. (2004). Dentin matrix protein 1 immobilized on type I collagen fibrils facilitates apatite deposition in vitro. J Biol Chem, 279(12), 11649-11656. https://doi.org/10.1074/jbc.M309296200 He, L., Hao, Y., Zhen, L., Liu, H., Shao, M., Xu, X., . . . van Loveren, C. (2019). Biomineralization of dentin. J Struct Biol, 207(2), 115-122. https://doi.org/10.1016/j.jsb.2019.05.010 Kalamajski, S., & Oldberg, Å. (2010). The role of small leucine-rich proteoglycans in collagen fibrillogenesis. Matrix Biology, 29(4), 248-253. http://doi.org/10.1016/j.matbio.2010.01.001 Kawasaki, K., & Weiss, K. M. (2008). SCPP gene evolution and the dental mineralization continuum. J Dent Res, 87(6), 520-531. https://doi.org/10.1177/154405910808700608 Kinney, J. H., Pople, J. A., Driessen, C. H., Breunig, T. M., Marshall, G. W., & Marshall, S. J. (2001). Intrafibrillar mineral may be absent in dentinogenesis imperfecta type II (DI-II). J Dent Res, 80(6), 1555-1559. https://doi.org/10.1177/00220345010800061501 Li, C., Jing, Y., Wang, K., Ren, Y., Liu, X., Wang, X., . . . Feng, J. Q. (2018). Dentinal mineralization is not limited in the mineralization front but occurs along with the entire odontoblast process. Int J Biol Sci, 14(7), 693-704. https://doi.org/10.7150/ijbs.25712 Linde, A., & Robins, S. (1988). Quantitative assessment of collagen crosslinks in dissected predentin and dentin. Coll Relat Res, 8(5), 443-450. https://doi.org/10.1016/s0174-173x(88)80017-7 Linde, A. (1989). Dentin matrix proteins: Composition and possible functions in calcification. The Anatomical Record, 224(2), 154-166. https://doi.org/10.1002/ar.1092240206 Nijhuis, A. W. G., Nejadnik, M. R., Nudelman, F., Walboomers, X. F., te Riet, J., Habibovic, P., . . . Leeuwenburgh, S. C. G. (2014). Enzymatic pH control for biomimetic deposition of calcium phosphate coatings. Acta Biomaterialia, 10(2), 931-939. http://doi.org/10.1016/j.actbio.2013.09.036 Niu, L., Jee, S. E., Jiao, K., Tonggu, L., Li, M., Wang, L., . . . Tay, F. R. (2017). Collagen intrafibrillar mineralization as a result of the balance between osmotic equilibrium and electroneutrality. Nat Mater, 16(3), 370-378. https://doi.org/10.1038/nmat4789 Niu, L., Zhang, W., Pashley, D. H., Breschi, L., Mao, J., Chen, J., & Tay, F. R. (2013). Biomimetic remineralization of dentin. Dental Materials: Official Publication of the Academy of Dental Materials, 30(1), 77-96. https://doi.org/10.1016/j.dental.2013.07.013 Nudelman, F., Lausch, A. J., Sommerdijk, N. A. J. M., & Sone, E. D. (2013). In vitro models of collagen biomineralization. Journal of Structural Biology, 183(2), 258-269. http://doi.org/10.1016/j.jsb.2013.04.003 Orgel, J. P. R. O., Irving, T. C., Miller, A., & Wess, T. J. (2006). Microfibrillar structure of type I collagen in situ. Proceedings of the National Academy of Sciences, 103(24), 9001-9005. https://doi.org/10.1073/pnas.0502718103 Padovano, J. D., Ravindran, S., Snee, P. T., Ramachandran, A., Bedran-Russo, A., & George, A. (2015). DMP1-derived peptides promote remineralization of human dentin. J Dent Res., 94(4), 608-614. https://doi.org/10.1177/0022034515572441 Prasad, M., Butler, W. T., & Qin, C. (2010). Dentin sialophosphoprotein (DSPP) in biomineralization. Connect Tissue Res, 51(5), 404-417. https://doi.org/10.3109/03008200903329789 Qin, C., Baba, O., & Butler, W. T. (2004). Post-translational modifications of SIBLING proteins and their roles in osteogenesis and dentinogenesis. Crit Rev Oral Biol & Med, 15(3), 126-136. https://doi.org/10.1177/154411130401500302 Ruch, J., Lesot, H., & Bègue-Kirn, C. (1995). Odontoblast differentiation. Int. J. Dev. BioI., 39(1), 51-68. https://pubmed.ncbi.nlm.nih.gov/7626422/#:~:text=Odontoblasts%20are%20post%2Dmitotic%2C%20neural,and%20secrete%20predentin%2Ddentin%20components Scott, J. E. (1990). Proteoglycan:Collagen interactions and subfibrillar structure in collagen fibrils. implications in the development and ageing of connective tissues. Journal of Anatomy, 169, 23-35. https://pubmed.ncbi.nlm.nih.gov/2384335/ Tesch, W., Eidelman, N., Roschger, P., Goldenberg, F., Klaushofer, K., & Fratzl, P. (2001). Graded microstructure and mechanical properties of human crowm dentine. Calcif Tissue Int, 69(3), 147-157. https://doi.org/10.1007/s00223-001-2012-z Thesleff, I. (2003). Epithelial-mesenchymal signalling regulating tooth morphogenesis. J Cell Sci., 116(Pt 9), 1647-1648. https://doi.org/10.1242/jcs.00410 Toroian, D., Lim, J. E., & Price, P. A. (2007). The size exclusion characteristics of type I collagen: Implications for the role of noncollagenous bone constituents in mineralization. The Journal of Biological Chemistry, 282(31), 22437-22447. https://doi.org/10.1074/jbc.M700591200 Veis, A., & Dorvee, J. (2013). Biomineralization mechanisms: A new paradigm for crystal nucleation in organic matrices. Calcified Tissue International, 93(4), 307-315. https://doi.org/10.1007/s00223-012-9678-2 Yamakoshi, Y., & Simmer, J. P. (2018). Structural features, processing mechanism and gene splice variants of dentin sialophosphoprotein. Japanese Dental Science Review, 54(4), 183-196. https://doi.org/10.1016/j.jdsr.2018.03.006 Zhao, J., Liu, Y., Wei-bin Sun, & Yang, X. (2012). First detection, characterization, and application of amorphous calcium phosphate in dentistry. Journal of Dental Sciences, 7(4), 316-323. https://doi.org/10.1016/j.jds.2012.09.001 Ababneh, K. T., Hall, R. C., & Embery, G. (1999). The proteoglycans of human cementum: Immunohistochemical localization in healthy, periodontally involved and ageing teeth. J Periodont Res, 34(2), 87-96. https://doi.org/10.1111/j.1600-0765.1999.tb02227.x Abou Neel, E., Aljabo, A., Strange, A., Ibrahim, S. (2016). Coathup M, Young A & Mudera V. Demineralization-remineralization dynamics in teeth and bone. Int J Nanom 11, 4743-4763. https://doi.org/10.2147/IJN.S107624 Arzate, H., Zeichner-David, M., & Mercado-Celis, G. (2015). Cementum proteins: Role in cementogenesis, biomineralization, periodontium formation and regeneration. Periodontol 2000 67(1), 211-233. https://doi.org/10.1111/prd.12062 Beertsen, W., VandenBos, T., & Everts, V. (1999). Root development in mice lacking functional tissue non-specific alkaline phosphatase gene: Inhibition of acellular cementum formation. J. Dent. Res 78(6), 1221-1229. https://doi.org/10.1177/00220345990780060501 Berry, J. E., Zhao, M., Jin, Q., Foster, B. L., Viswanathan, H., & Somerman, M. J. (2003). Exploring the origins of cementoblasts and their trigger factors. Connect. Tissue Res 44(1), 97-102. https://pubmed.ncbi.nlm.nih.gov/12952181/ Choi, H., Kim, T., Yang, S., Lee, J., You, H., & Cho, E. (2017). A reciprocal interaction between β-catenin and osterix in cementogenesis. Sci Rep 7, 8160. https://www.nature.com/articles/s41598-017-08607-5 Foster, B., Ao, M., Willoughby, C., Soenjaya, Y., Holm, E., Lukashova, L., & Somerman, M. (2015). Mineralization defects in cementum and craniofacial bone from loss of bone sialoprotein. Bone 78, 150-164. https://doi.org/10.1016/j.bone.2015.05.007 Foster, B. L. (2017). On the discovery of cementum. J Periodontal Res, 52(2), 666-685. https://doi.org/10.1111/jre.12444 Gottlieb, B. (1942). Biology of the cementum. J Periodontol 13, 13-19. Hollis, A., Arundel, P., High, A., & Balmer, R. (2013). Current concepts in hypophosphatasia: Case report and literature review. Int J Paediatr Dent 23(3), 153-159. https://doi.org/10.1111/j.1365-263X.2012.01239.x Ikezawa, K., Hart, C. E., Williams, D. C., & Narayanan, A. S. (1997). Characterization of cementum derived growth factor as an insulin-like growth factor-I like molecule. Connect Tissue Res 36(4), 309-319. https://doi.org/10.3109/03008209709160230 Kaipatur, N. R., Murshed, M., & McKee, M. D. (2008). Matrix Gla protein inhibition of tooth mineralization. J Dent Res 87(9), 839-844. https://doi.org/10.1177/154405910808700907 Listik, E., Azevedo Marques Gaschler, J., Matias, M., Neuppmann Feres, M. F., Toma, L., & Raphaelli Nahás-Scocate, A. C. (2019). Proteoglycans and dental biology: The first review. Carbohydr Polym 1;225:115199. https://doi.org/10.1016/j.carbpol.2019.115199 Montoya, G., Arenas, J., Romo, E., Zeichner-David, M., Alvarez, M., Narayanan, A. S., & Arzate, H. (2014). Human recombinant cementum attachment protein (hrPTPLa/CAP) promotes hydroxyapatite crystal formation in vitro and bone healing in vivo. Bone 69, 154-164. https://doi.org/10.1016/j.bone.2014.09.014 Montoya, G., Correa, R., Arenas, J., Hoz, L., Romo, E., Arroyo, R., & Arzate, H. (2019). Cementum protein 1-derived peptide (CEMP 1-p1) modulates hydroxyapatite crystal formation in vitro. J Pept Sci 25, e3211. https://doi.org/10.1002/psc.3211 Nanci, A., & Bosshardt, D. D. (2006). Structure of periodontal tissues in health and disease*. Periodontol 2000, 40, 11-28. https://doi.org/10.1111/j.1600-0757.2005.00141.x Orimo, H. (2010). The mechanism of mineralization and the role of alkaline phosphatase in health and disease. J Nippon Med Sch 77, 4-12. https://doi.org/10.1272/jnms.77.4 Popowics, T., Foster, B., Swanson, E., Fong, H., & Somerman, M. (2005). Defining the roots of cementum formation. Cells Tissues Organs 181, 248-257. https://www.karger.com/Article/Pdf/91386 Tenório, D. M. H., Santos, M. F., & Zorn, T. M. T. (2003). Distribution of biglycan and decorin in rat dental tissue. Braz J Med Biol Res 36, 1061-1065. https://doi.org/10.1590/s0100-879x2003000800012 van den Bos, T., & Beertsen, W. (1999). Alkaline phosphatase activity in human periodontal ligament: Age effect and relation to cementum growth rate. J Periodontal Res 34, 1-6. https://doi.org/10.1111/j.1600-0765.1999.tb02215.x Watanabe, H., Umeda, M., Seki, T., & Ishikawa, I. (1993). Clinical and laboratory studies of severe periodontal disease in an adolescent associated with hypophosphatasia. A case report. J. Periodontol 64, https://doi.org/174-180. 10.1902/jop.1993.64.3.174 Watanabe, K. (1990). Prepubertal periodontitis: A review of diagnostic criteria, pathogenesis, and differential diagnosis. J Periodontal Res 25, 31-48. https://doi.org/10.1111/j.1600-0765.1990.tb01205.x Yamamoto, T., Domon, T., Takahashi, S., Arambawatta, A. K. S., & Wakita, M. (2004). Immunolocation of proteoglycans and bone-related noncollagenous glycoproteins in developing acellular cementum of rat molars. Cell Tissue Res 317, 299-312. https://doi.org/10.1007/s00441-004-0896-4 Zeichner-David, M. (2006). Regeneration of periodontal tissues: Cementogenesis revisited. Periodontol 2000 41, 196-217. https://doi.org/10.1111/j.1600-0757.2006.00162.x Alam, I., Padgett, L. R., Ichikawa, S., Alkhouli, M., Koller, D. L., Lai, D. & Econs, M. J. (2014). SIBLING family genes and bone mineral density: Association and allele-specific expression in humans. Bone, 64, 166-172. https://doi.org/10.1016/j.bone.2014.04.013 Aubin, J. E. (1998). Advances in the osteoblast lineage. Biochem Cell Biol, 76, 899-910. https://pubmed.ncbi.nlm.nih.gov/10392704/ Babaji, P., Devanna, R., Jagtap, K., Chaurasia, V. R., Jerry, J. J., Choudhury, B. K., & Duhan, D. (2017). The cell biology and role of resorptive cells in diseases: A review. Ann Afr Med, 16(2), 39-45. https://doi.org/10.4103/aam.aam_97_16 Bellido, T. (2013). Osteocytes and Their Role in Bone Remodeling. Actualizaciones En Osteología, 9(1), 56-64. http://osteologia.org.ar/files/pdf/rid32_Bellido.pdf Bellido, T. (2014). Osteocyte-driven bone remodeling. Calcif Tissue Int, 94, 25-34. https://doi.org/10.1007/s00223-013-9774-y Beniash, E. (2011), Biominerals—hierarchical nanocomposites: the example of bone. WIREs Nanomed Nanobiotechnol, 3(1), 47-69. https://doi.org/10.1002/wnan.105 Bini, F., Pica, A., Marinozzi, A., & Marinozzi, F. (2017). 3D diffusion model within the collagen apatite porosity: An insight to the nanostructure of human trabecular bone. Plos One. 12(12): e0189041. https://doi.org/10.1371/journal.pone.0189041 Bouleftour, W., Juignet, L., Bouet, G., Granito, R. N., Vanden-Bossche, A., Laroche, N. & Malaval, L. (2016). The role of the SIBLING, bone sialoprotein in skeletal biology — contribution of mouse experimental genetics. Matrix Biol 52-54, 60-77. https://doi.org/10.1016/j.matbio.2015.12.011 Boyle, W. J., Simonet, W. S., & Lacey, D. L. (2003). Osteoclast differentiation and activation. Nature 423, 337-342. https://doi.org/10.1038/nature01658 Compston, J. (2006). Bone quality: What is it and how is it measured? Arq Bras Endocrinol Metabol. 50(4), 579-585. https://doi.org/10.1590/s0004-27302006000400003 D'Amico, L., & Roato, I. (2012). Osteoclasts, the major actors in bone resorption. In J. S. Walker, & A. J. Brown (Eds.), Osteoclasts: Morphology, functions & clinical implications (pp. 95-112). Hauppauge, [New York]: Nova Science Publishers, Inc. Deshpande, A. S., & Beniash, E. (2008). Bioinspired synthesis of mineralized collagen fibrils. Cryst Growth & Des, 8, 3084-3090. https://doi.org/10.1021/cg800252f Dorozhkin, S. (2016). Calcium orthophosphates (CaPO4): Ocurrence and properties. Prog Biomater, 5, 9-70. https://doi.org/10.1007/s40204-015-0045-z Ducy, P., & Karsenty, G. (1998). Genetic control of cell differentiation in the skeleton. Curr Opin Cell Biol, 10, 614-619. https://doi.org/10.1016/s0955-0674(98)80037-9 Ducy, P., Schinke, T., & Karsenty, G. (2000). The osteoblast: A sophisticated fibroblast under central surveillance. Science, 289, 1501-1504. https://doi.org/10.1126/science.289.5484.1501 Foster, B. L., Ao, M., Willoughby, C., Soenjaya, Y., Holm, E., Lukashova, L., Tran, A. B., Wimer, H. F., Zerfas, P. M., Nociti, F. H., Kantovitz, K. R., Quan, B. D., Sone, E. D., Goldberg, H. A., & Somerman, M. J. (2015). Mineralization defects in cementum and craniofacial bone from loss of bone sialoprotein. Bone, 78, 150-164. https://doi.org/10.1016/j.bone.2015.05.007 George, A., & Veis, A. (2008). Phosphorylated proteins and control over apatite nucleation, crystal growth, and inhibition. Chem Rev, 108, 4670-4693. https://doi.org/10.1021/cr0782729 Gorski, J. P. (2011). Biomineralization of bone: A fresh view of the roles of non-collagenous proteins. Front Biosci (Landmark Ed), 16, 2598-2621. https://doi.org/10.2741/3875 Ikeda, F., Nishimura, R., Matsubara, T., Tanaka, S., Inoue, J., Reddy, S. V., & Yoneda, T. (2004). Critical roles of c-jun signaling in regulation of NFAT family and RANKL-regulated osteoclast differentiation. J Clin Invest, 114, 475-484. https://doi.org/10.1172/JCI19657 Kagiya, T. (2016). Role of microRNAs in osteoclast differentiation and function. In C. Reeves (Ed.), Osteoclasts: Cell biology, functions and related diseases (pp. 1-18). New York: Nova Science Publishers, Inc. Kanakamedala , A. K., Mahendra, J., Kareem, N., & Mahendra, L. (2019). Osteoclasts: Multifaceted molecule in vesicular trafficking. Journal of Clinical & Diagnostic Research 13(8), 1-5. https://doi.org/10.7860/JCDR/2019/40307.13064 Kanazawa, I. (2015). Osteocalcin as a hormone regulating glucose metabolism. World J Diabetes, 6(18), 1345-1354. https://doi.org/10.4239/wjd.v6.i18.1345 Staines, K. A., MacRae, V. E., & Farquharson, C. (2012). The importance of the SIBLING family of proteins on skeletal mineralisation and bone remodelling. The Journal of endocrinology, 214(3), 241–255. https://doi.org/10.1530/JOE-12-0143 Landis, W. J., & Silver, F. H. (2009). Mineral deposition in the extracellular matrices of vertebrate tissues: Identification of possible apatite nucleation sites on type I collagen. Cells Tissues Organs, 189, 20-24. https://doi.org/10.1159/000151454 Lerner, U. H., Kindstedt, E., & Lundberg, P. (2019). The critical interplay between bone resorbing and bone forming cells. J Clin Periodontol, 46, 33-51. https://doi.org/10.1111/jcpe.13051 Margolis, H. C., Kwak, S., & Yamazaki, H. (2014). Role of mineralization inhibitors in the regulation of hard tissue biomineralization: Relevance to initial enamel formation and maturation. Front Physiol, 5, 339-452. https://doi.org/10.3389/fphys.2014.00339 Moser, S. C., & van der Eerden, B. C. J. (2019). Osteocalcin-A: Versatile bone-derived hormone. Front Endocrinol (Lausanne), 9, 794. https://doi.org/10.3389/fendo.2018.00794 Neve, A., Corrado, A., & Cantatore, F. P. (2013). Osteocalcin: Skeletal and extra-skeletal effects. J Cell Physiol, 228(6), 1149-1153. https://doi.org/10.1002/jcp.24278 Nudelman, F., Lausch, A. J., Sommerdijk, N. A. J. M., & Sone, E. D. (2013). In vitro models of collagen biomineralization. J Struct Biol, 183(2), 258-269. https://doi.org/ 10.1016/j.jsb.2013.04.003 Orgel, J. P. R. O., Irving, T. C., Miller, A., & Wess, T. J. (2006). Microfibrillar structure of type I collagen in situ. Proc Natl Acad Sci U S A, 103(24), 9001-5. https://doi.org/10.1073/pnas.0502718103 Ou-Yang, H., Paschalis, E. P., Mayo, W. E., Boskey, A. L., & Mendelsohn, R. (2001). Infrared microscopic imaging of bone: Spatial distribution of CO3(2-). J Bone Miner Res, 16(5), 893-900. https://doi.org/10.1359/jbmr.2001.16.5.893 Price, P. A., Toroian, D., & Lim, J. E. (2009). Mineralization by inhibitor exclusion: the calcification of collagen with fetuin. The Journal of biological chemistry, 284(25), 17092-17101. https://doi.org/10.1074/jbc.M109.007013 Qin, C., Baba, O., & Butler, W. T. (2004). Postranslational modifications of sibling proteins and their roles in osteogenesis and dentinogenesis. Crit Rev Oral Biol & Med, 15(3), 126-136. https://doi.org/10.1177/154411130401500302 Qin, C., D’Souza, R., & Feng, J. Q. (2007). Dentin matrix protein 1 (DMP1): New and important roles for biomineralization and phosphate homeostasis. J Dent Res, 86, 1134-1141. https://doi.org/10.1177/154405910708601202 Ritchie, H. (2018). The functional significance of dentin sialoprotein-phosphophoryn and dentin sialoprotein. Int J Oral Sci, 10, 31. https://doi.org/10.1038/s41368-018-0035-9 Saito, T., Arsenault, A. L., Yamauchi, M., Kuboki, Y., & Crenshaw, M. A. (1999). Mineral induction by immobilized phosphoproteins. Bone, 21(4), 305-311. https://doi.org/10.1016/S8756-3282(97)00149-X Scheurer, H. (2013). Osteoblasts: Morphology, functions and clinical implications. New York: Nova Science Publishers, Inc. Singh, A., Gill, G., Kaur, H., Amhmed, M., & Jakhu, H. (2018). Role of osteopontin in bone remodeling and orthodontic tooth movement: A review. Prog Orthod 19(1), 18. https://doi.org/10.1186/s40510-018-0216-2 Stewart, S., Shea, D. A., Tarnowski, C. P., Morris, M. D., Wang, D., Franceschi, R. & Keller, E. (2002). Trends in early mineralization of murine calvarial osteoblastic cultures: A raman microscopic study. J Raman Spectrosc, 33(7), 536-543. https://doi.org/10.1002/jrs.892 Tavafoghi, M., & Cerruti, M. (2016). The role of amino acids in hydroxyapatite mineralization. J R Soc Interface, 13, 123. https://doi.org/10.1098/rsif.2016.0462 Tresguerres, F. G. F., Torres, J., López-Quiles, J., Hernández, G., Vega, J. A., & Tresguerres, I. F. (2020). The osteocyte: A multifunctional cell within the bone. Ann Anat, 227, 151422. https://doi.org/10.1016/j.aanat.2019.151422 Tsao, Y., Huang, Y., Wu, H., Liu, Y., Liu, Y., & Lee, K. O. (2017). Osteocalcin mediates biomineralization during osteogenic maturation in human mesenchymal stromal cells. Int J Mol Sci, 18, 159. https://doi.org/10.3390/ijms18010159 Veis, A., & Perry, A. (1967). The phosphoprotein of the dentin matrix. Biochemistry, 6(8), 2409-2416. https://doi.org/10.1021/bi00860a017 Veschi, E. A., Bolean, M., Strzelecka-Kiliszek, A., Bandorowicz-Pikula, J., Pikula, S., Granjon, T., & Ciancaglini, P. (2020). Localization of annexin A6 in matrix vesicles during physiological mineralization. Int J Mol Sci, 21(4), 1367. https://doi.org/ 10.3390/ijms21041367 Zofkova, I. (2008). Involvement of bone in systemic endocrine regulation. Physiol Res, 67, 669-677. https://doi.org/10.33549/physiolres.933843
dc.rights.uri.*.fl_str_mv	http://creativecommons.org/licenses/by-nc-nd/4.0/
dc.rights.local.spa.fl_str_mv	Acceso abierto
dc.rights.accessrights.none.fl_str_mv	info:eu-repo/semantics/openAccess
dc.rights.creativecommons.*.fl_str_mv	Atribución-Nocomercial-SinDerivar 4.0 International
dc.rights.coar.none.fl_str_mv	http://purl.org/coar/access_right/c_abf2
rights_invalid_str_mv	http://creativecommons.org/licenses/by-nc-nd/4.0/ Acceso abierto Atribución-Nocomercial-SinDerivar 4.0 International http://purl.org/coar/access_right/c_abf2
eu_rights_str_mv	openAccess
dc.publisher.grantor.spa.fl_str_mv	Universidad El Bosque
institution	Universidad El Bosque
bitstream.url.fl_str_mv	https://repositorio.unbosque.edu.co/bitstreams/64c53565-0fdf-4ca2-8ebb-a4b9eb343bb3/download https://repositorio.unbosque.edu.co/bitstreams/611f78aa-ed2f-4212-8a1b-e4ea5403d815/download https://repositorio.unbosque.edu.co/bitstreams/bdb7033d-28aa-4a2b-bff1-9b78d2a42190/download https://repositorio.unbosque.edu.co/bitstreams/9b76fc95-772b-48f6-b148-314c769d351c/download
bitstream.checksum.fl_str_mv	eabd03aa747e1c3ebfbcf826852057fd 17cc15b951e7cc6b3728a574117320f9 13258e9ea2c0665da5f8423e735e4acf 75630c28f3aa50329b9ab622cfd271b2
bitstream.checksumAlgorithm.fl_str_mv	MD5 MD5 MD5 MD5
repository.name.fl_str_mv	Repositorio Institucional Universidad El Bosque
repository.mail.fl_str_mv	bibliotecas@biteca.com
_version_	1814100802162130944
spelling	Mejía Naranjo, WilsonBeltrán Zúñiga, Edgar O.2022-09-20T13:42:03Z2022-09-20T13:42:03Z2022978958739276097895873928149789587392753http://hdl.handle.net/20.500.12495/9051instname:Universidad El Bosquereponame:Repositorio Institucional Universidad El Bosquerepourl:https://repositorio.unbosque.edu.coEste libro responde a la necesidad de presentar a los estudiantes de Odontología y de cursos básicos de posgrado en ciencias biomédicas u odontológicas los fundamentos y mecanismos del fenómeno de biomineralización de tejidos dentales. Se trata de un proceso dinámico y complejo llevado a cabo por células especializadas, mediante el cual ocurren la secreción y deposición de minerales de calcio y fosfato inorgánicos, los cuales interactúan de forma organizada con proteínas nucleadoras en una matriz extracelular para generar tejidos mineralizados altamente funcionales. Las células especializadas son los ameloblastos, los odontoblastos, los cementoblastos y los osteoblastos, responsables respectivamente de la producción de esmalte, dentina, cemento y hueso. Comprender los procesos de biomineralización y las dinámicas de mineralización y remineralización es importante para prevenir y tratar las enfermedades causadas por una mineralización anormal y/o defectuosa de los tejidos calcificados.This book responds to the need to present to students of Dentistry and basic postgraduate courses in biomedical or dental sciences the fundamentals and mechanisms of the phenomenon of biomineralization of dental tissues. It is a dynamic and complex process carried out by specialized cells, through which the secretion and deposition of inorganic calcium and phosphate minerals occur. These interact in an organized way with nucleating proteins in an extracellular matrix to generate highly functional mineralized tissues. The specialized cells are the ameloblasts, the odontoblasts, the cementoblasts and the osteoblasts, responsible respectively for the production of enamel, dentin, cementum and bone. Understanding biomineralization processes and the dynamics of mineralization and remineralization is important to prevent and treat diseases caused by abnormal and/or defective mineralization of calcified tissues.http://creativecommons.org/licenses/by-nc-nd/4.0/Acceso abiertoinfo:eu-repo/semantics/openAccessAtribución-Nocomercial-SinDerivar 4.0 Internationalhttp://purl.org/coar/access_right/c_abf2BiomineralizaciónCiencia de los materialesCristalizaciónBiomaterialesCalcificaciónBiomineralizationMaterial scienceCrystallizationBiomaterialsCalcificationBiomineralización de tejidos calcificadosbookLibro completoinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_2f33info:eu-repo/semantics/bookhttp://purl.org/coar/version/c_970fb48d4fbd8a85Universidad El BosqueBronckers, A. L. J. J., Lyaruu, D. M., & DenBesten, P. K. (2009). The impact of fluoride on ameloblasts and the mechanisms of enamel fluorosis. Journal of Dental Research, 88(10), 877-893. https://doi.org/10.1177/0022034509343280Cameron, F. K., & Seidell, A. (1904). The action of water upon the phosphates of calcium. Journal of the American Chemical Society, 26(11), 1454-1463. https://doi.org/10.1021/ja02001a007Castiblanco, G. A., Rutishauser, D., Ilag, L. L., Martignon, S., Castellanos, J. E., & Mejía, W. (2015). Identification of proteins from human permanent erupted enamel. European Journal of Oral Sciences, 123(6), 390-395. https://doi.org/10.1111/eos.12214Dorozhkin, S. V. (2011). Calcium orthophosphates: Occurrence, properties, biomineralization, pathological calcification and biomimetic applications. Biomatter, 1(2), 121-164. https://doi.org/10.4161/biom.18790Dreesmann, H. (1892). Ueber knochenplombierung. Beitr Klin Chir, 9, 804-810.Evans, J. S. (2017). Polymorphs, proteins, and nucleation theory: A critical analysis. Minerals (2075-163X), 7(4):62. https://doi.org/10.3390/min7040062Evans, J. S. (2019). Composite materials design: Biomineralization proteins and the guided assembly and organization of biomineral nanoparticles. Materials (Basel, Switzerland), 12(4). https://doi.org/10.3390/ma12040581Furtos, G., Lesci, I. G., Šiller, L., Marin, F., Brümmer, F., & Checa, A. (2015). Biomineralization: From fundamentals to biomaterials & environmental issues. Pfaffikon, Switzerland: Trans Tech Publications Ltd. Retrieved from http://ezproxy.javeriana.edu.co:2048/login?url=https://search.ebscohost.com/login.aspx?direct=true&db=e000xww&AN=1165291&lang=es&site=ehost-liveGower, L. B. (2008). Biomimetic model systems for investigating the amorphous precursor pathway and its role in biomineralization. Chemical Reviews, 108(11), 4551-4627. https://doi.org/10.1021/cr800443hKay, M. I., Young, R. A., & Posner, A. S. (1964). Crystal structure of hydroxyapatite. Nature, 204(4963), 1050-1052. https://doi.org/10.1038/2041050a0Lafisco, M., Delgado López, J., & Drouet, C. (2014). Nanocrystaline apatites: Synthesis, physical-cehmical and thermodynamic characterization. In M. Lafisco, & J. Delgado López (Eds.), Apatite (pp. 49-80) Nova Science Publishers, Inc.Lide, D. (2005). The CRC handbook of chemistry and physics. CRC Press, Boca Ratón, Florida, 86, 2544.Madupalli, H., Pavan, B., & Tecklenburg, M. (2017). Carbonate substitution in the mineral component of bone: Discriminating the structural changes, simultaneously imposed by carbonate in A and B sites of apatite. J Solid State Chem. 255:27-35. https://doi.org/10.1016/j.jssc.2017.07.025Omelon, S. J., & Grynpas, M. D. (2008). Relationships between polyphosphate chemistry, biochemistry and apatite biomineralization. Chemical Reviews, 108(11), 4694-4715. https://doi.org/10.1021/cr0782527Posner, A. S., & Betts, F. (1975). Synthetic amorphous calcium phosphate and its relation to bone mineral structure. Accounts of Chemical Research, 8(8), 273-281. https://doi.org/10.1021/ar50092a003Ramirez-Rodríguez, G., Delgado-López, J., & Gomez-Morales, J. (2013). Evolution of calcium phosphate precipitatation in hanging drop vapor infussion by in situ raman microspectroscopy. CrystEngComm, 15, 2206.Rodríguez-Navarro, A. B., Marie, P., Nys, Y., Hincke, M. T., & Gautron, J. (2015). Amorphous calcium carbonate controls avian eggshell mineralization: A new paradigm for understanding rapid eggshell calcification. Journal of Structural Biology, 190(3), 291-303. https://doi.org/10.1016/j.jsb.2015.04.014Sharma, R., Tsuchiya, M., Skobe, Z., Tannous, B. A., & Bartlett, J. D. (2010). The acid test of fluoride: How pH modulates toxicity. PLoS ONE, 5(-5), -e10895. https://doi.org/10.1371/journal.pone.0010895Simmer, J. P., & Fincham, A. G. (1995). Molecular mechanisms of dental enamel formation. Critical Reviews in Oral Biology & Medicine, 6(2), 84-108. https://doi.org/10.1177/10454411950060020701Yao, S., Jin, B., Liu, Z., Shao, C., Zhao, R., Tang, R., & Wang, X. (2017). Biomineralization: From material tactis to biological strategy. Adv Mater, 29(14). https://doi.org/10.1002/adma.201605903Zahn, D. (2015). Thermodynamics and kinetics of prenucleation clusters, classical and non-classical nucleation. ChemPhysChem, 16(10), 2069-2075. https://doi.org/10.1002/cphc.201500231Aoba, T., & Fejerskov, O. (2002). Dental fluorosis: Chemistry and biology. Crit Rev Oral Biol & Med., 13(2), 155-170. https://doi.org/10.1177/154411130201300206Bansal, A., Shetty, D., Bindal, R., & Pathak, A. (2012). Amelogenin: Novel protein with diverse applications in genetic and molecular profiling. Oral Maxillofac Pathol J, 16, 395-399. https://doi.org/10.4103/0973-029X.102495Bartlett, J. D., & Simmer, J. P. (2015). New perspectives on amelotin and amelogenesis. J Dent Res., 94(5), 642-644. https://doi.org/10.1177/0022034515572442Bartlett, J. D., Ganss, B., Goldberg, M., Moradian-Oldak, J., Paine, M. L., Snead, M. L., . . . Zhou, Y. L. (2006). Protein–Protein interactions of the developing enamel matrix. Current Topics in Developmental Biology, 74, 57-115. https://doi.org/10.1016/S0070-2153(06)74003-0Bouropoulos, N., & Moradian-Oldak, J. (2004). Induction of apatite by the cooperative effect of amelogenin and the 32-kDa enamelin. Journal of Dental Research, 83(4), 278-282. https://doi.org/10.1177/154405910408300402Bromley, K. M., Kiss, A. S., Lokappa, S. B., Lakshminarayanan, R., Fan, D., Ndao, M., . . . Moradian-Oldak, J. (2011). Dissecting amelogenin protein nanospheres: Characterization of metastable oligomers. Journal of Biological Chemistry, 286(40), 34643-34653. https://doi.org/10.1074/jbc.M111.250928Bronckers, A. L. J. J., Lyaruu, D. M., & DenBesten, P. K. (2009). The impact of fluoride on ameloblasts and the mechanisms of enamel fluorosis. Journal of Dental Research, 88(10), 877-893. https://doi.org/10.1177/0022034509343280Castiblanco, G. A., Rutishauser, D., Ilag, L. L., Martignon, S., Castellanos, J. E., & Mejía, W. (2015). Identification of proteins from human permanent erupted enamel. European Journal of Oral Sciences, 123(6), 390-395. https://doi.org/10.1111/eos.12214Carey, C. M. (2014). Focus on fluorides: Update on the use of fluoride for the prevention of dental caries. Journal of Evidence Based Dental Practice, 14, 95-102. https://doi.org/10.1016/j.jebdp.2014.02.004Fincham, A. G., Belcourt, A. B., Termine, J. D., Butler, W. T., & Cothran, W. C. (1981). Dental enamel matrix: Sequences of two amelogenin polypeptides. Bioscience Reports, 1(10), 771-778. https://doi.org/10.1007/BF01114799Fincham, A. G., Moradian-Oldak, J., & Simmer, J. P. (1999). The structural biology of the developing dental enamel matrix. Journal of Structural Biology, 126(3), 270-299. https://doi.org/10.1006/jsbi.1999.4130Gallon, V., Chen, L., Yang, X., & Moradian-Oldak, J. (2013). Localization and quantitative co-localization of enamelin with amelogenin. Journal of Structural Biology, 183(2), 239-249. https://doi.org/10.1016/j.jsb.2013.03.014Hu, J. C. -., Zhang, C. H., Yang, Y., Kärrman-MÅrdh, C., Forsman-Semb, K., & Simmer, J. P. (2001). Cloning and characterization of the mouse and human enamelin genes. J Dent Res., 80(3), 898-902. https://doi.org/10.1177/00220345010800031001Hu, J. C. -., Hu, Y., Lu, Y., Smith, C. E., Lertlam, R., Wright, J. T., . . . Simmer, J. P. (2014). Enamelin is critical for ameloblast integrity and enamel ultrastructure formation. PLoS ONE, 9(3), e89303. https://doi.org/10.1371/journal.pone.0089303Hu, Y., Smith, C. E., Richardson, A. S., Bartlett, J. D., Hu, J. C. C., & Simmer, J. P. (2016). MMP20, KLK4, and MMP20/KLK4 double null mice define roles for matrix proteases during dental enamel formation. Molecular Genetics & Genomic Medicine, 4(2), 178-196. https://doi.org/10.1002/mgg3.194Kidd, E., & Fejerskov, O. (2016). Essentials of dental caries. p. 6. Oxford: OUP Oxford.Lacruz, R. S., Smith, C. E., Kurtz, I., Hubbard, M. J., & Paine, M. L. (2012). New paradigms on the transport functions of maturation-stage ameloblasts. Journal of Dental Research, 92(2), 122-129. https://doi.org/10.1177/0022034512470954Lacruz, R. S., Habelitz, S., Timothy Wright, J., & Paine, M. L. (2017). Dental enamel formation and implications for oral health and disease. Physiological Reviews, 97(3), 939-993. https://doi.org/10.1152/physrev.00030.2016Le Norcy, E., Kwak, S., Wiedemann-Bidlack, F. B., Beniash, E., Yamakoshi, Y., Simmer, J. P., & Margolis, H. C. (2011). Leucine-rich amelogenin peptides regulate mineralization in vitro. Journal of Dental Research, 90(9), 1091-1097. https://doi.org/10.1177/0022034511411301Lu, Y., Papagerakis, P., Yamakoshi, Y., Hu, J., Bartlett, J., & Simmer, J. (2008). Functions of KLK4 and MMP-20 in dental enamel formation. Biological Chemistry, 389(6), 695-700. https://doi.org/10.1515/BC.2008.080Margolis, H. C., Beniash, E., & Fowler, C. E. (2006). Role of macromolecular assembly of enamel matrix proteins in enamel formation. Journal of Dental Research, 85(9), 775-793. https://doi.org/10.1177/154405910608500902Moradian-Oldak, J. (2012). Protein- mediated enamel mineralization. Frontiers in Bioscience : A Journal and Virtual Library, 17, 1996-2023.Nagano, T., Kakegawa, A., Yamakoshi, Y., Tsuchiya, S., Hu, J. C. -., Gomi, K., . . . Simmer, J. P. (2009). Mmp-20 and Klk4 cleavage site preferences for amelogenin sequences. Journal of Dental Research, 88(9), 823-828. https://doi.org/10.1177/0022034509342694Sharma, R., Tsuchiya, M., Skobe, Z., Tannous, B. A., & Bartlett, J. D. (2010). The acid test of fluoride: How pH modulates toxicity. - PLoS ONE, 5(- 5), -e10895. https://doi.org/10.1371/journal.pone.0010895Simmer, J. P., & Fincham, A. G. (1995). Molecular mechanisms of dental enamel formation. Critical Reviews in Oral Biology & Medicine, 6(2), 84-108. https://doi.org/10.1177/10454411950060020701Sire, J., Delgado, S., Frometin, D., & Girondot, M. (2005). Amelogenin: Lessons from evolution. Archives of Oral Biology, (- 2), 205-212. https://doi.org/10.1016/j.archoralbio.2004.09.004Teepe, J. D., Schmitz, J. E., Hu, Y., Yamada, Y., Fajardo, R. J., Smith, C. E., & Chun, Y. P. (2014). Correlation of ameloblastin with enamel mineral content. Connect Tissue Res, 55, 38-42. https://doi.org/10.3109/03008207.2014.923871Veis, A., & Dorvee, J. (2013). Biomineralization mechanisms: A new paradigm for crystal nucleation in organic matrices. Calcified Tissue International, 93(4), 307-315. https://doi.org/10.1007/s00223-012-9678-2Weatherell, J., Deutsch, D., Robinson, C., & Hallsworth, A. (1975). Fluoride concentrations in developing enamel. Nature, 256(5514), 230-232. https://doi.org/10.1038/256230a0Akiva, A., Kerschnitzki, M., Pinkas, I., Wagermaier, W., Yaniv, K., Fratzl, P., .Weiner, S. (2016). Mineral formation in the larval zebrafish tail bone occurs via an acidic disordered calcium phosphate phase. Journal of the American Chemical Society, 138(43), 14481-14487. https://doi.org/10.1021/jacs.6b09442Alvares, K. (2014). The role of acidic phosphoproteins in biomineralization. Connective Tissue Research, 55(1), 34-40. https://doi.org/10.3109/03008207.2013.867336Arana-Chavez, V. E., & Massa, L. F. (2004). Odontoblasts: The cells forming and maintaining dentine. Int J Biochem Cell Biol, 36(8), 1367-1373 https://doi.org/10.1016/j.biocel.2004.01.006Beniash, E. (2011). Biominerals-hierarchical nanocomposites: The example of bone. Wiley Interdisciplinary Reviews: Nanomedicine and Nanobiotechnology, 3(1), 47-69 https://doi.org/10.1002/wnan.105Bertassoni, L., & Swain, M. (2017). Removal of dentin non-collagen structures results in the unraveling of microfibril bundless in collagen type I. Connect Tissue Res, 58(5), 414-423. https://doi.org/10.1080/03008207.2016.1235566Bertassoni, L. E., Orgel, J. P. R., Antipova, O., & Swain, M. V. (2012). The dentin organic matrix – limitations of restorative dentistry hidden on the nanometer scale. Acta Biomaterialia, 8(7), 2419-2433. https://doi.org/10.1016/j.actbio.2012.02.022Bertassoni, L. E., Habelitz, S., Kinney, J. H., Marshall, S. J., & Marshall Jr., G. W. (2009). Biomechanical perspective on the remineralization of dentin. Caries Research, 43(1), 70-77. https://doi.org/0.1159/000201593Bertassoni, L. E. (2017). Dentin on the nanoscale: Hierarchical organization, mechanical behavior and bioinspired engineering. Dental Materials, 33, 637-649. https://doi.org/10.1016/j.dental.2017.03.008Bleicher, F. (2014). Odontoblast physiology. Exp Cell Res, 325(2), 65-71. https://doi.org/10.1016/j.yexcr.2013.12.012Bonar, L. C., Lees, S., & Mook, H. A. (1985). Neutron diffraction studies of collagen in fully mineralized bone. J Mol Biol, 181(2), 265-270. http://doi.org/10.1016/0022-2836(85)90090-7Bonucci, E. (2002). Crystal ghost and biological mineralization: Fancy spectres in an old castle, or negelcted structures worthy of belief. J. Bone. Miner. Metab, 20(5), 249-265. https://doi.org/10.1007/s007740200037Boonrungsiman, S., Gentleman, E., Carzaniga, R., Evans, N. D., McComb, D. W., Porter, A. E., & Stevens, M. M. (2012). The role of intracellular calcium phosphate in osteoblast-mediated bone apatite formation. Proc Natl Acad Sci U S A., 109(35), 14170-14175. https://doi.org/10.1073/pnas.1208916109Butler, W. T., Brunn, J. C., & Qin, C. (2003). Dentin extracellular matrix (ECM) proteins: Comparison to bone ECM and contribution to dynamics of dentinogenesis. Connective Tissue Research, 44(1), 171-178. https://doi.org/10.1080/03008200390152287Cao, Y. C., Mei, L. M., Li, Q., Lo, C. E., & Chu, H. C. (2015). Methods for biomimetic remineralization of human dentine: A systematic review. Int. J. Mol. Sci, 16(3), 4615-4627. https://doi.org/10.3390/ijms16034615Colfen, H. (2010). Biomineralization: A crystal-clear view. Nat Mater, 9(12), 960-961. https://doi.org/10.1038/nmat2911Dorozhkin, S. V. (2017). Hydroxyapatite and other calcium orthophosphates: Nanodimensional, multiphasic and amorphous formulations. New York: Nova Science Publishers, Inc. Retrieved from http://ezproxy.javeriana.edu.co:2048/login?url=https://search.ebscohost.com/login.aspx?direct=true&db=e000xww&AN=1530704&lang=es&site=ehost-liveEmbery, G., Hall, R., Waddington, R., Septier, D., & Goldberg, M. (2001). Proteoglycans in dentinogenesis. Crit Rev Oral Biol & Med, 12(4), 331-349. https://doi.org/10.1177/10454411010120040401Fisher, L. W., & Fedarko, N. S. (2003). Six genes expressed in bones and teeth encode the current members of the SIBLING family of proteins. Connect Tissue Res, 44(Suppl 1), 33-40.Gericke, A., Qin, C., Sun, Y., Redfern, R., Redfern, D., Fujimoto, Y., . . . Boskey, A. L. (2010). Different forms of DMP1 play distinct roles in mineralization. J Dent Res, 89(4), 355-359. https://doi.org/10.1177/0022034510363250Goldberg, M., Kulkarni, A., Young, M., & Boskey, A. (2011). Dentin: Structure, composition and mineralization. Front Biosci, 3(2), 711-735. https://doi.org/10.2741/e281Hao, J., Zou, B., Narayanan, K., & George, A. (2004). Differential expression patterns of the dentin matrix proteins during mineralized tissue formation. Bone, 34(6), 921-932 https://doi.org/10.1016/j.bone.2004.01.020He, G., Dahl, T., Veis, A., & George, A. (2003). Nucleation of apatite crystals in vitro by self-assembled dentin matrix protein 1. Nat Mater, 2(8), 552-558. https://www.nature.com/articles/nmat945He, G., & George, A. (2004). Dentin matrix protein 1 immobilized on type I collagen fibrils facilitates apatite deposition in vitro. J Biol Chem, 279(12), 11649-11656. https://doi.org/10.1074/jbc.M309296200He, L., Hao, Y., Zhen, L., Liu, H., Shao, M., Xu, X., . . . van Loveren, C. (2019). Biomineralization of dentin. J Struct Biol, 207(2), 115-122. https://doi.org/10.1016/j.jsb.2019.05.010Kalamajski, S., & Oldberg, Å. (2010). The role of small leucine-rich proteoglycans in collagen fibrillogenesis. Matrix Biology, 29(4), 248-253. http://doi.org/10.1016/j.matbio.2010.01.001Kawasaki, K., & Weiss, K. M. (2008). SCPP gene evolution and the dental mineralization continuum. J Dent Res, 87(6), 520-531. https://doi.org/10.1177/154405910808700608Kinney, J. H., Pople, J. A., Driessen, C. H., Breunig, T. M., Marshall, G. W., & Marshall, S. J. (2001). Intrafibrillar mineral may be absent in dentinogenesis imperfecta type II (DI-II). J Dent Res, 80(6), 1555-1559. https://doi.org/10.1177/00220345010800061501Li, C., Jing, Y., Wang, K., Ren, Y., Liu, X., Wang, X., . . . Feng, J. Q. (2018). Dentinal mineralization is not limited in the mineralization front but occurs along with the entire odontoblast process. Int J Biol Sci, 14(7), 693-704. https://doi.org/10.7150/ijbs.25712Linde, A., & Robins, S. (1988). Quantitative assessment of collagen crosslinks in dissected predentin and dentin. Coll Relat Res, 8(5), 443-450. https://doi.org/10.1016/s0174-173x(88)80017-7Linde, A. (1989). Dentin matrix proteins: Composition and possible functions in calcification. The Anatomical Record, 224(2), 154-166. https://doi.org/10.1002/ar.1092240206Nijhuis, A. W. G., Nejadnik, M. R., Nudelman, F., Walboomers, X. F., te Riet, J., Habibovic, P., . . . Leeuwenburgh, S. C. G. (2014). Enzymatic pH control for biomimetic deposition of calcium phosphate coatings. Acta Biomaterialia, 10(2), 931-939. http://doi.org/10.1016/j.actbio.2013.09.036Niu, L., Jee, S. E., Jiao, K., Tonggu, L., Li, M., Wang, L., . . . Tay, F. R. (2017). Collagen intrafibrillar mineralization as a result of the balance between osmotic equilibrium and electroneutrality. Nat Mater, 16(3), 370-378. https://doi.org/10.1038/nmat4789Niu, L., Zhang, W., Pashley, D. H., Breschi, L., Mao, J., Chen, J., & Tay, F. R. (2013). Biomimetic remineralization of dentin. Dental Materials: Official Publication of the Academy of Dental Materials, 30(1), 77-96. https://doi.org/10.1016/j.dental.2013.07.013Nudelman, F., Lausch, A. J., Sommerdijk, N. A. J. M., & Sone, E. D. (2013). In vitro models of collagen biomineralization. Journal of Structural Biology, 183(2), 258-269. http://doi.org/10.1016/j.jsb.2013.04.003Orgel, J. P. R. O., Irving, T. C., Miller, A., & Wess, T. J. (2006). Microfibrillar structure of type I collagen in situ. Proceedings of the National Academy of Sciences, 103(24), 9001-9005. https://doi.org/10.1073/pnas.0502718103Padovano, J. D., Ravindran, S., Snee, P. T., Ramachandran, A., Bedran-Russo, A., & George, A. (2015). DMP1-derived peptides promote remineralization of human dentin. J Dent Res., 94(4), 608-614. https://doi.org/10.1177/0022034515572441Prasad, M., Butler, W. T., & Qin, C. (2010). Dentin sialophosphoprotein (DSPP) in biomineralization. Connect Tissue Res, 51(5), 404-417. https://doi.org/10.3109/03008200903329789Qin, C., Baba, O., & Butler, W. T. (2004). Post-translational modifications of SIBLING proteins and their roles in osteogenesis and dentinogenesis. Crit Rev Oral Biol & Med, 15(3), 126-136. https://doi.org/10.1177/154411130401500302Ruch, J., Lesot, H., & Bègue-Kirn, C. (1995). Odontoblast differentiation. Int. J. Dev. BioI., 39(1), 51-68. https://pubmed.ncbi.nlm.nih.gov/7626422/#:~:text=Odontoblasts%20are%20post%2Dmitotic%2C%20neural,and%20secrete%20predentin%2Ddentin%20componentsScott, J. E. (1990). Proteoglycan:Collagen interactions and subfibrillar structure in collagen fibrils. implications in the development and ageing of connective tissues. Journal of Anatomy, 169, 23-35. https://pubmed.ncbi.nlm.nih.gov/2384335/Tesch, W., Eidelman, N., Roschger, P., Goldenberg, F., Klaushofer, K., & Fratzl, P. (2001). Graded microstructure and mechanical properties of human crowm dentine. Calcif Tissue Int, 69(3), 147-157. https://doi.org/10.1007/s00223-001-2012-zThesleff, I. (2003). Epithelial-mesenchymal signalling regulating tooth morphogenesis. J Cell Sci., 116(Pt 9), 1647-1648. https://doi.org/10.1242/jcs.00410Toroian, D., Lim, J. E., & Price, P. A. (2007). The size exclusion characteristics of type I collagen: Implications for the role of noncollagenous bone constituents in mineralization. The Journal of Biological Chemistry, 282(31), 22437-22447. https://doi.org/10.1074/jbc.M700591200Veis, A., & Dorvee, J. (2013). Biomineralization mechanisms: A new paradigm for crystal nucleation in organic matrices. Calcified Tissue International, 93(4), 307-315. https://doi.org/10.1007/s00223-012-9678-2Yamakoshi, Y., & Simmer, J. P. (2018). Structural features, processing mechanism and gene splice variants of dentin sialophosphoprotein. Japanese Dental Science Review, 54(4), 183-196. https://doi.org/10.1016/j.jdsr.2018.03.006Zhao, J., Liu, Y., Wei-bin Sun, & Yang, X. (2012). First detection, characterization, and application of amorphous calcium phosphate in dentistry. Journal of Dental Sciences, 7(4), 316-323. https://doi.org/10.1016/j.jds.2012.09.001Ababneh, K. T., Hall, R. C., & Embery, G. (1999). The proteoglycans of human cementum: Immunohistochemical localization in healthy, periodontally involved and ageing teeth. J Periodont Res, 34(2), 87-96. https://doi.org/10.1111/j.1600-0765.1999.tb02227.xAbou Neel, E., Aljabo, A., Strange, A., Ibrahim, S. (2016). Coathup M, Young A & Mudera V. Demineralization-remineralization dynamics in teeth and bone. Int J Nanom 11, 4743-4763. https://doi.org/10.2147/IJN.S107624Arzate, H., Zeichner-David, M., & Mercado-Celis, G. (2015). Cementum proteins: Role in cementogenesis, biomineralization, periodontium formation and regeneration. Periodontol 2000 67(1), 211-233. https://doi.org/10.1111/prd.12062Beertsen, W., VandenBos, T., & Everts, V. (1999). Root development in mice lacking functional tissue non-specific alkaline phosphatase gene: Inhibition of acellular cementum formation. J. Dent. Res 78(6), 1221-1229. https://doi.org/10.1177/00220345990780060501Berry, J. E., Zhao, M., Jin, Q., Foster, B. L., Viswanathan, H., & Somerman, M. J. (2003). Exploring the origins of cementoblasts and their trigger factors. Connect. Tissue Res 44(1), 97-102. https://pubmed.ncbi.nlm.nih.gov/12952181/Choi, H., Kim, T., Yang, S., Lee, J., You, H., & Cho, E. (2017). A reciprocal interaction between β-catenin and osterix in cementogenesis. Sci Rep 7, 8160. https://www.nature.com/articles/s41598-017-08607-5Foster, B., Ao, M., Willoughby, C., Soenjaya, Y., Holm, E., Lukashova, L., & Somerman, M. (2015). Mineralization defects in cementum and craniofacial bone from loss of bone sialoprotein. Bone 78, 150-164. https://doi.org/10.1016/j.bone.2015.05.007Foster, B. L. (2017). On the discovery of cementum. J Periodontal Res, 52(2), 666-685. https://doi.org/10.1111/jre.12444Gottlieb, B. (1942). Biology of the cementum. J Periodontol 13, 13-19.Hollis, A., Arundel, P., High, A., & Balmer, R. (2013). Current concepts in hypophosphatasia: Case report and literature review. Int J Paediatr Dent 23(3), 153-159. https://doi.org/10.1111/j.1365-263X.2012.01239.xIkezawa, K., Hart, C. E., Williams, D. C., & Narayanan, A. S. (1997). Characterization of cementum derived growth factor as an insulin-like growth factor-I like molecule. Connect Tissue Res 36(4), 309-319. https://doi.org/10.3109/03008209709160230Kaipatur, N. R., Murshed, M., & McKee, M. D. (2008). Matrix Gla protein inhibition of tooth mineralization. J Dent Res 87(9), 839-844. https://doi.org/10.1177/154405910808700907Listik, E., Azevedo Marques Gaschler, J., Matias, M., Neuppmann Feres, M. F., Toma, L., & Raphaelli Nahás-Scocate, A. C. (2019). Proteoglycans and dental biology: The first review. Carbohydr Polym 1;225:115199. https://doi.org/10.1016/j.carbpol.2019.115199Montoya, G., Arenas, J., Romo, E., Zeichner-David, M., Alvarez, M., Narayanan, A. S., & Arzate, H. (2014). Human recombinant cementum attachment protein (hrPTPLa/CAP) promotes hydroxyapatite crystal formation in vitro and bone healing in vivo. Bone 69, 154-164. https://doi.org/10.1016/j.bone.2014.09.014Montoya, G., Correa, R., Arenas, J., Hoz, L., Romo, E., Arroyo, R., & Arzate, H. (2019). Cementum protein 1-derived peptide (CEMP 1-p1) modulates hydroxyapatite crystal formation in vitro. J Pept Sci 25, e3211. https://doi.org/10.1002/psc.3211Nanci, A., & Bosshardt, D. D. (2006). Structure of periodontal tissues in health and disease*. Periodontol 2000, 40, 11-28. https://doi.org/10.1111/j.1600-0757.2005.00141.xOrimo, H. (2010). The mechanism of mineralization and the role of alkaline phosphatase in health and disease. J Nippon Med Sch 77, 4-12. https://doi.org/10.1272/jnms.77.4Popowics, T., Foster, B., Swanson, E., Fong, H., & Somerman, M. (2005). Defining the roots of cementum formation. Cells Tissues Organs 181, 248-257. https://www.karger.com/Article/Pdf/91386Tenório, D. M. H., Santos, M. F., & Zorn, T. M. T. (2003). Distribution of biglycan and decorin in rat dental tissue. Braz J Med Biol Res 36, 1061-1065. https://doi.org/10.1590/s0100-879x2003000800012van den Bos, T., & Beertsen, W. (1999). Alkaline phosphatase activity in human periodontal ligament: Age effect and relation to cementum growth rate. J Periodontal Res 34, 1-6. https://doi.org/10.1111/j.1600-0765.1999.tb02215.xWatanabe, H., Umeda, M., Seki, T., & Ishikawa, I. (1993). Clinical and laboratory studies of severe periodontal disease in an adolescent associated with hypophosphatasia. A case report. J. Periodontol 64, https://doi.org/174-180. 10.1902/jop.1993.64.3.174Watanabe, K. (1990). Prepubertal periodontitis: A review of diagnostic criteria, pathogenesis, and differential diagnosis. J Periodontal Res 25, 31-48. https://doi.org/10.1111/j.1600-0765.1990.tb01205.xYamamoto, T., Domon, T., Takahashi, S., Arambawatta, A. K. S., & Wakita, M. (2004). Immunolocation of proteoglycans and bone-related noncollagenous glycoproteins in developing acellular cementum of rat molars. Cell Tissue Res 317, 299-312. https://doi.org/10.1007/s00441-004-0896-4Zeichner-David, M. (2006). Regeneration of periodontal tissues: Cementogenesis revisited. Periodontol 2000 41, 196-217. https://doi.org/10.1111/j.1600-0757.2006.00162.xAlam, I., Padgett, L. R., Ichikawa, S., Alkhouli, M., Koller, D. L., Lai, D. & Econs, M. J. (2014). SIBLING family genes and bone mineral density: Association and allele-specific expression in humans. Bone, 64, 166-172. https://doi.org/10.1016/j.bone.2014.04.013Aubin, J. E. (1998). Advances in the osteoblast lineage. Biochem Cell Biol, 76, 899-910. https://pubmed.ncbi.nlm.nih.gov/10392704/Babaji, P., Devanna, R., Jagtap, K., Chaurasia, V. R., Jerry, J. J., Choudhury, B. K., & Duhan, D. (2017). The cell biology and role of resorptive cells in diseases: A review. Ann Afr Med, 16(2), 39-45. https://doi.org/10.4103/aam.aam_97_16Bellido, T. (2013). Osteocytes and Their Role in Bone Remodeling. Actualizaciones En Osteología, 9(1), 56-64. http://osteologia.org.ar/files/pdf/rid32_Bellido.pdfBellido, T. (2014). Osteocyte-driven bone remodeling. Calcif Tissue Int, 94, 25-34. https://doi.org/10.1007/s00223-013-9774-yBeniash, E. (2011), Biominerals—hierarchical nanocomposites: the example of bone. WIREs Nanomed Nanobiotechnol, 3(1), 47-69. https://doi.org/10.1002/wnan.105Bini, F., Pica, A., Marinozzi, A., & Marinozzi, F. (2017). 3D diffusion model within the collagen apatite porosity: An insight to the nanostructure of human trabecular bone. Plos One. 12(12): e0189041. https://doi.org/10.1371/journal.pone.0189041Bouleftour, W., Juignet, L., Bouet, G., Granito, R. N., Vanden-Bossche, A., Laroche, N. & Malaval, L. (2016). The role of the SIBLING, bone sialoprotein in skeletal biology — contribution of mouse experimental genetics. Matrix Biol 52-54, 60-77. https://doi.org/10.1016/j.matbio.2015.12.011Boyle, W. J., Simonet, W. S., & Lacey, D. L. (2003). Osteoclast differentiation and activation. Nature 423, 337-342. https://doi.org/10.1038/nature01658Compston, J. (2006). Bone quality: What is it and how is it measured? Arq Bras Endocrinol Metabol. 50(4), 579-585. https://doi.org/10.1590/s0004-27302006000400003D'Amico, L., & Roato, I. (2012). Osteoclasts, the major actors in bone resorption. In J. S. Walker, & A. J. Brown (Eds.), Osteoclasts: Morphology, functions & clinical implications (pp. 95-112). Hauppauge, [New York]: Nova Science Publishers, Inc.Deshpande, A. S., & Beniash, E. (2008). Bioinspired synthesis of mineralized collagen fibrils. Cryst Growth & Des, 8, 3084-3090. https://doi.org/10.1021/cg800252fDorozhkin, S. (2016). Calcium orthophosphates (CaPO4): Ocurrence and properties. Prog Biomater, 5, 9-70. https://doi.org/10.1007/s40204-015-0045-zDucy, P., & Karsenty, G. (1998). Genetic control of cell differentiation in the skeleton. Curr Opin Cell Biol, 10, 614-619. https://doi.org/10.1016/s0955-0674(98)80037-9Ducy, P., Schinke, T., & Karsenty, G. (2000). The osteoblast: A sophisticated fibroblast under central surveillance. Science, 289, 1501-1504. https://doi.org/10.1126/science.289.5484.1501Foster, B. L., Ao, M., Willoughby, C., Soenjaya, Y., Holm, E., Lukashova, L., Tran, A. B., Wimer, H. F., Zerfas, P. M., Nociti, F. H., Kantovitz, K. R., Quan, B. D., Sone, E. D., Goldberg, H. A., & Somerman, M. J. (2015). Mineralization defects in cementum and craniofacial bone from loss of bone sialoprotein. Bone, 78, 150-164. https://doi.org/10.1016/j.bone.2015.05.007George, A., & Veis, A. (2008). Phosphorylated proteins and control over apatite nucleation, crystal growth, and inhibition. Chem Rev, 108, 4670-4693. https://doi.org/10.1021/cr0782729Gorski, J. P. (2011). Biomineralization of bone: A fresh view of the roles of non-collagenous proteins. Front Biosci (Landmark Ed), 16, 2598-2621. https://doi.org/10.2741/3875Ikeda, F., Nishimura, R., Matsubara, T., Tanaka, S., Inoue, J., Reddy, S. V., & Yoneda, T. (2004). Critical roles of c-jun signaling in regulation of NFAT family and RANKL-regulated osteoclast differentiation. J Clin Invest, 114, 475-484. https://doi.org/10.1172/JCI19657Kagiya, T. (2016). Role of microRNAs in osteoclast differentiation and function. In C. Reeves (Ed.), Osteoclasts: Cell biology, functions and related diseases (pp. 1-18). New York: Nova Science Publishers, Inc.Kanakamedala , A. K., Mahendra, J., Kareem, N., & Mahendra, L. (2019). Osteoclasts: Multifaceted molecule in vesicular trafficking. Journal of Clinical & Diagnostic Research 13(8), 1-5. https://doi.org/10.7860/JCDR/2019/40307.13064Kanazawa, I. (2015). Osteocalcin as a hormone regulating glucose metabolism. World J Diabetes, 6(18), 1345-1354. https://doi.org/10.4239/wjd.v6.i18.1345Staines, K. A., MacRae, V. E., & Farquharson, C. (2012). The importance of the SIBLING family of proteins on skeletal mineralisation and bone remodelling. The Journal of endocrinology, 214(3), 241–255. https://doi.org/10.1530/JOE-12-0143Landis, W. J., & Silver, F. H. (2009). Mineral deposition in the extracellular matrices of vertebrate tissues: Identification of possible apatite nucleation sites on type I collagen. Cells Tissues Organs, 189, 20-24. https://doi.org/10.1159/000151454Lerner, U. H., Kindstedt, E., & Lundberg, P. (2019). The critical interplay between bone resorbing and bone forming cells. J Clin Periodontol, 46, 33-51. https://doi.org/10.1111/jcpe.13051Margolis, H. C., Kwak, S., & Yamazaki, H. (2014). Role of mineralization inhibitors in the regulation of hard tissue biomineralization: Relevance to initial enamel formation and maturation. Front Physiol, 5, 339-452. https://doi.org/10.3389/fphys.2014.00339Moser, S. C., & van der Eerden, B. C. J. (2019). Osteocalcin-A: Versatile bone-derived hormone. Front Endocrinol (Lausanne), 9, 794. https://doi.org/10.3389/fendo.2018.00794Neve, A., Corrado, A., & Cantatore, F. P. (2013). Osteocalcin: Skeletal and extra-skeletal effects. J Cell Physiol, 228(6), 1149-1153. https://doi.org/10.1002/jcp.24278Nudelman, F., Lausch, A. J., Sommerdijk, N. A. J. M., & Sone, E. D. (2013). In vitro models of collagen biomineralization. J Struct Biol, 183(2), 258-269. https://doi.org/ 10.1016/j.jsb.2013.04.003Orgel, J. P. R. O., Irving, T. C., Miller, A., & Wess, T. J. (2006). Microfibrillar structure of type I collagen in situ. Proc Natl Acad Sci U S A, 103(24), 9001-5. https://doi.org/10.1073/pnas.0502718103Ou-Yang, H., Paschalis, E. P., Mayo, W. E., Boskey, A. L., & Mendelsohn, R. (2001). Infrared microscopic imaging of bone: Spatial distribution of CO3(2-). J Bone Miner Res, 16(5), 893-900. https://doi.org/10.1359/jbmr.2001.16.5.893Price, P. A., Toroian, D., & Lim, J. E. (2009). Mineralization by inhibitor exclusion: the calcification of collagen with fetuin. The Journal of biological chemistry, 284(25), 17092-17101. https://doi.org/10.1074/jbc.M109.007013Qin, C., Baba, O., & Butler, W. T. (2004). Postranslational modifications of sibling proteins and their roles in osteogenesis and dentinogenesis. Crit Rev Oral Biol & Med, 15(3), 126-136. https://doi.org/10.1177/154411130401500302Qin, C., D’Souza, R., & Feng, J. Q. (2007). Dentin matrix protein 1 (DMP1): New and important roles for biomineralization and phosphate homeostasis. J Dent Res, 86, 1134-1141. https://doi.org/10.1177/154405910708601202Ritchie, H. (2018). The functional significance of dentin sialoprotein-phosphophoryn and dentin sialoprotein. Int J Oral Sci, 10, 31. https://doi.org/10.1038/s41368-018-0035-9Saito, T., Arsenault, A. L., Yamauchi, M., Kuboki, Y., & Crenshaw, M. A. (1999). Mineral induction by immobilized phosphoproteins. Bone, 21(4), 305-311. https://doi.org/10.1016/S8756-3282(97)00149-XScheurer, H. (2013). Osteoblasts: Morphology, functions and clinical implications. New York: Nova Science Publishers, Inc.Singh, A., Gill, G., Kaur, H., Amhmed, M., & Jakhu, H. (2018). Role of osteopontin in bone remodeling and orthodontic tooth movement: A review. Prog Orthod 19(1), 18. https://doi.org/10.1186/s40510-018-0216-2Stewart, S., Shea, D. A., Tarnowski, C. P., Morris, M. D., Wang, D., Franceschi, R. & Keller, E. (2002). Trends in early mineralization of murine calvarial osteoblastic cultures: A raman microscopic study. J Raman Spectrosc, 33(7), 536-543. https://doi.org/10.1002/jrs.892Tavafoghi, M., & Cerruti, M. (2016). The role of amino acids in hydroxyapatite mineralization. J R Soc Interface, 13, 123. https://doi.org/10.1098/rsif.2016.0462Tresguerres, F. G. F., Torres, J., López-Quiles, J., Hernández, G., Vega, J. A., & Tresguerres, I. F. (2020). The osteocyte: A multifunctional cell within the bone. Ann Anat, 227, 151422. https://doi.org/10.1016/j.aanat.2019.151422Tsao, Y., Huang, Y., Wu, H., Liu, Y., Liu, Y., & Lee, K. O. (2017). Osteocalcin mediates biomineralization during osteogenic maturation in human mesenchymal stromal cells. Int J Mol Sci, 18, 159. https://doi.org/10.3390/ijms18010159Veis, A., & Perry, A. (1967). The phosphoprotein of the dentin matrix. Biochemistry, 6(8), 2409-2416. https://doi.org/10.1021/bi00860a017Veschi, E. A., Bolean, M., Strzelecka-Kiliszek, A., Bandorowicz-Pikula, J., Pikula, S., Granjon, T., & Ciancaglini, P. (2020). Localization of annexin A6 in matrix vesicles during physiological mineralization. Int J Mol Sci, 21(4), 1367. https://doi.org/ 10.3390/ijms21041367Zofkova, I. (2008). Involvement of bone in systemic endocrine regulation. Physiol Res, 67, 669-677. https://doi.org/10.33549/physiolres.933843ORIGINAL9789587392760.pdf9789587392760.pdfBiomineralización de tejidos calcificadosapplication/pdf2530456https://repositorio.unbosque.edu.co/bitstreams/64c53565-0fdf-4ca2-8ebb-a4b9eb343bb3/downloadeabd03aa747e1c3ebfbcf826852057fdMD51LICENSElicense.txtlicense.txttext/plain; charset=utf-82000https://repositorio.unbosque.edu.co/bitstreams/611f78aa-ed2f-4212-8a1b-e4ea5403d815/download17cc15b951e7cc6b3728a574117320f9MD52THUMBNAIL9789587392760.pdf.jpg9789587392760.pdf.jpgimage/jpeg258351https://repositorio.unbosque.edu.co/bitstreams/bdb7033d-28aa-4a2b-bff1-9b78d2a42190/download13258e9ea2c0665da5f8423e735e4acfMD53TEXT9789587392760.pdf.txt9789587392760.pdf.txtExtracted texttext/plain55201https://repositorio.unbosque.edu.co/bitstreams/9b76fc95-772b-48f6-b148-314c769d351c/download75630c28f3aa50329b9ab622cfd271b2MD5420.500.12495/9051oai:repositorio.unbosque.edu.co:20.500.12495/90512024-02-07 07:40:11.221http://creativecommons.org/licenses/by-nc-nd/4.0/restrictedhttps://repositorio.unbosque.edu.coRepositorio Institucional Universidad El Bosquebibliotecas@biteca.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

Biomineralización de tejidos calcificados

Publicaciones similares