The role of glycosyltransferases in colorectal cancer
Colorectal cancer (CRC) is one of the main causes of cancer death in the world. Post-translational modifications (PTMs) have been extensively studied in malignancies due to its relevance in tumor pathogenesis and therapy. This review is focused on the dysregulation of glycosyltransferase expression...
- Autores:
-
Fernández-Ponce, Cecilia
Geribaldi-Doldán, Noelia
Sánchez-Gomar, Ismael
Navarro Quiroz, Roberto
Atencio Ibarra, Linda
Gomez Escorcia, Lorena
Fernández-Cisnal, Ricardo
Aroca Martinez, Gustavo
García-Cózar, Francisco
Navarro Quiroz, Elkin
- Tipo de recurso:
- Fecha de publicación:
- 2021
- Institución:
- Universidad Simón Bolívar
- Repositorio:
- Repositorio Digital USB
- Idioma:
- eng
- OAI Identifier:
- oai:bonga.unisimon.edu.co:20.500.12442/7846
- Acceso en línea:
- https://hdl.handle.net/20.500.12442/7846
https://doi.org/10.3390/ijms22115822
https://www.mdpi.com/1422-0067/22/11/5822/pdf
- Palabra clave:
- Colorectal cancer
Glycosyl transferase
Glycosylation
Post-translational modification
- Rights
- openAccess
- License
- Attribution-NonCommercial-NoDerivatives 4.0 Internacional
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The role of glycosyltransferases in colorectal cancer |
| title |
The role of glycosyltransferases in colorectal cancer |
| spellingShingle |
The role of glycosyltransferases in colorectal cancer Colorectal cancer Glycosyl transferase Glycosylation Post-translational modification |
| title_short |
The role of glycosyltransferases in colorectal cancer |
| title_full |
The role of glycosyltransferases in colorectal cancer |
| title_fullStr |
The role of glycosyltransferases in colorectal cancer |
| title_full_unstemmed |
The role of glycosyltransferases in colorectal cancer |
| title_sort |
The role of glycosyltransferases in colorectal cancer |
| dc.creator.fl_str_mv |
Fernández-Ponce, Cecilia Geribaldi-Doldán, Noelia Sánchez-Gomar, Ismael Navarro Quiroz, Roberto Atencio Ibarra, Linda Gomez Escorcia, Lorena Fernández-Cisnal, Ricardo Aroca Martinez, Gustavo García-Cózar, Francisco Navarro Quiroz, Elkin |
| dc.contributor.author.none.fl_str_mv |
Fernández-Ponce, Cecilia Geribaldi-Doldán, Noelia Sánchez-Gomar, Ismael Navarro Quiroz, Roberto Atencio Ibarra, Linda Gomez Escorcia, Lorena Fernández-Cisnal, Ricardo Aroca Martinez, Gustavo García-Cózar, Francisco Navarro Quiroz, Elkin |
| dc.subject.eng.fl_str_mv |
Colorectal cancer Glycosyl transferase Glycosylation Post-translational modification |
| topic |
Colorectal cancer Glycosyl transferase Glycosylation Post-translational modification |
| description |
Colorectal cancer (CRC) is one of the main causes of cancer death in the world. Post-translational modifications (PTMs) have been extensively studied in malignancies due to its relevance in tumor pathogenesis and therapy. This review is focused on the dysregulation of glycosyltransferase expression in CRC and its impact in cell function and in several biological pathways associated with CRC pathogenesis, prognosis and therapeutic approaches. Glycan structures act as interface molecules between cells and their environment and in several cases facilitate molecule function. CRC tissue shows alterations in glycan structures decorating molecules, such as annexin-1, mucins, heat shock protein 90 (Hsp90), β1 integrin, carcinoembryonic antigen (CEA), epidermal growth factor receptor (EGFR), insulin-like growth factor-binding protein 3 (IGFBP3), transforming growth factor beta (TGF-β) receptors, Fas (CD95), PD-L1, decorin, sorbin and SH3 domain-containing protein 1 (SORBS1), CD147 and glycosphingolipids. All of these are described as key molecules in oncogenesis and metastasis. Therefore, glycosylation in CRC can affect cell migration, cell–cell adhesion, actin polymerization, mitosis, cell membrane repair, apoptosis, cell differentiation, stemness regulation, intestinal mucosal barrier integrity, immune system regulation, T cell polarization and gut microbiota composition; all such functions are associated with the prognosis and evolution of the disease. According to these findings, multiple strategies have been evaluated to alter oligosaccharide processing and to modify glycoconjugate structures in order to control CRC progression and prevent metastasis. Additionally, immunotherapy approaches have contemplated the use of neoantigens, generated by altered glycosylation, as targets for tumor-specific T cells or engineered CAR (Chimeric antigen receptors) T cells. |
| publishDate |
2021 |
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2021-05-31T18:52:24Z |
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2021-05-31T18:52:24Z |
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2021 |
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14220067 |
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https://hdl.handle.net/20.500.12442/7846 |
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https://doi.org/10.3390/ijms22115822 |
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https://www.mdpi.com/1422-0067/22/11/5822/pdf |
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14220067 |
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https://hdl.handle.net/20.500.12442/7846 https://doi.org/10.3390/ijms22115822 https://www.mdpi.com/1422-0067/22/11/5822/pdf |
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eng |
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eng |
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Attribution-NonCommercial-NoDerivatives 4.0 Internacional |
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Fernández-Ponce, Cecilia3ea042ce-c868-4666-918b-baddf44673f4Geribaldi-Doldán, Noelia3d1da8a1-d3f9-487e-8853-6527fadbc918Sánchez-Gomar, Ismael88c76ad8-928e-47e3-af93-58fb04c9e688Navarro Quiroz, Roberto1246844f-5707-438a-808b-1f8c2761977eAtencio Ibarra, Linda5a20f00d-a98e-4ecf-8235-9c4aaf7033b5Gomez Escorcia, Lorena0eda4380-18c9-49b2-b09c-a02809a7d505Fernández-Cisnal, Ricardod4124d08-800f-40e8-8bd5-f570d4ec40c7Aroca Martinez, Gustavo85796035-bace-4923-8931-ac7730cbd5e7García-Cózar, Franciscoa272b47f-fab5-418d-9cb9-b288bf264ce8Navarro Quiroz, Elkind586f4e1-e86b-4364-8aa2-1b1dc7c1bb5e2021-05-31T18:52:24Z2021-05-31T18:52:24Z202114220067https://hdl.handle.net/20.500.12442/7846https://doi.org/10.3390/ijms22115822https://www.mdpi.com/1422-0067/22/11/5822/pdfColorectal cancer (CRC) is one of the main causes of cancer death in the world. Post-translational modifications (PTMs) have been extensively studied in malignancies due to its relevance in tumor pathogenesis and therapy. This review is focused on the dysregulation of glycosyltransferase expression in CRC and its impact in cell function and in several biological pathways associated with CRC pathogenesis, prognosis and therapeutic approaches. Glycan structures act as interface molecules between cells and their environment and in several cases facilitate molecule function. CRC tissue shows alterations in glycan structures decorating molecules, such as annexin-1, mucins, heat shock protein 90 (Hsp90), β1 integrin, carcinoembryonic antigen (CEA), epidermal growth factor receptor (EGFR), insulin-like growth factor-binding protein 3 (IGFBP3), transforming growth factor beta (TGF-β) receptors, Fas (CD95), PD-L1, decorin, sorbin and SH3 domain-containing protein 1 (SORBS1), CD147 and glycosphingolipids. All of these are described as key molecules in oncogenesis and metastasis. Therefore, glycosylation in CRC can affect cell migration, cell–cell adhesion, actin polymerization, mitosis, cell membrane repair, apoptosis, cell differentiation, stemness regulation, intestinal mucosal barrier integrity, immune system regulation, T cell polarization and gut microbiota composition; all such functions are associated with the prognosis and evolution of the disease. According to these findings, multiple strategies have been evaluated to alter oligosaccharide processing and to modify glycoconjugate structures in order to control CRC progression and prevent metastasis. Additionally, immunotherapy approaches have contemplated the use of neoantigens, generated by altered glycosylation, as targets for tumor-specific T cells or engineered CAR (Chimeric antigen receptors) T cells.pdfengMDPIAttribution-NonCommercial-NoDerivatives 4.0 Internacionalhttp://creativecommons.org/licenses/by-nc-nd/4.0/info:eu-repo/semantics/openAccesshttp://purl.org/coar/access_right/c_abf2International Journal of Molecular ScienciesVol. 22 Nº 11, (2021)Colorectal cancerGlycosyl transferaseGlycosylationPost-translational modificationThe role of glycosyltransferases in colorectal cancerinfo:eu-repo/semantics/articleArtículo científicohttp://purl.org/coar/version/c_970fb48d4fbd8a85http://purl.org/coar/resource_type/c_2df8fbb1Araghi, M.; Soerjomataram, I.; Jenkins, M.; Brierley, J.; Morris, E.; Bray, F.; Arnold, M. Global trends in colorectal cancer mortality: Projections to the year 2035. Int. J. Cancer 2019, 144, 2992–3000.Keum, N.; Giovannucci, E. Global burden of colorectal cancer: Emerging trends, risk factors and prevention strategies. Nat. Rev. Gastroenterol. Hepatol. 2019, 16, 713–732.Rawla, P.; Sunkara, T.; Barsouk, A. Epidemiology of colorectal cancer: Incidence, mortality, survival, and risk factors. Prz. Gastroenterol. 2019, 14, 89–103.De Freitas, J.C.M., Jr.; Morgado-Díaz, J.A. The role of N-glycans in colorectal cancer progression: Potential biomarkers and therapeutic applications. Oncotarget 2016, 7, 19395–19413.Hoja-Łukowicz, D.; Link-Lenczowski, P.; Carpentieri, A.; Amoresano, A.; Pocheć, E.; Artemenko, K.A.; Bergquist, J.; Lityńska, A. L1CAM from human melanoma carries a novel type of N-glycan with Galβ1-4Galβ1- motif. Involvement of N-linked glycans in migratory and invasive behaviour of melanoma cells. Glycoconj. J. 2013, 30, 205–225.Julien, S.; Ivetic, A.; Grigoriadis, A.; QiZe, D.; Burford, B.; Sproviero, D.; Picco, G.; Gillett, C.; Papp, S.L.; Schaffer, L.; et al. Selectin ligand sialyl-Lewis x antigen drives metastasis of hormone-dependent breast cancers. Cancer Res. 2011, 71, 7683–7693.Kim, Y.-S.; Ahn, Y.H.; Song, K.J.; Kang, J.G.; Lee, J.H.; Jeon, S.K.; Kim, H.-C.; Yoo, J.S.; Ko, J.-H. Overexpression and β-1,6-Nacetylglucosaminylation- initiated aberrant glycosylation of TIMP-1: A “double whammy” strategy in colon cancer progression. J. Biol. Chem. 2012, 287, 32467–32478.Wei, T.; Liu, Q.; He, F.; Zhu, W.; Hu, L.; Guo, L.; Zhang, J. The role of N-acetylglucosaminyltransferases V in the malignancy of human hepatocellular carcinoma. Exp. Mol. Pathol. 2012, 93, 8–17.Cumin, C.; Huang, Y.L.; Everest-Dass, A.; Jacob, F. Deciphering the Importance of Glycosphingolipids on Cellular and Molecular Mechanisms Associated with Epithelial-to-Mesenchymal Transition in Cancer. Biomolecules 2021, 11, 62.Holst, S.; Stavenhagen, K.; Balog, C.I.; Koeleman, C.A.; McDonnell, L.M.; Mayboroda, O.A.; Verhoeven, A.; Mesker, W.E.; Tollenaar, R.A.; Deelder, A.M.; et al. 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