Abnormal N-Glycosylation of Human Lens Epithelial Cells in Type-2 Diabetes May Contribute to Cataract Progression

Ivan Ramos-Martínez,1– 3 Oscar Vivanco-Rojas,2 Brenda Juárez-Domínguez,2 Luis Hernández-Zimbrón,1,2 Lenin Ochoa-de la Paz,1,2 Hugo Quiroz-Mercado,2 Eleazar Ramírez-Hernández,1 Rosario Gulias-Cañizo,4 Ed...

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Autores principales: Ramos-Martínez I, Vivanco-Rojas O, Juárez-Domínguez B, Hernández-Zimbrón L, Ochoa-de la Paz L, Quiroz-Mercado H, Ramírez-Hernández E, Gulias-Cañizo R, Zenteno E
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Publicado: Dove Medical Press 2021
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spelling oai:doaj.org-article:48d9e7f4e5194413b14baefcc0529eb02021-12-02T13:56:03ZAbnormal N-Glycosylation of Human Lens Epithelial Cells in Type-2 Diabetes May Contribute to Cataract Progression1177-5483https://doaj.org/article/48d9e7f4e5194413b14baefcc0529eb02021-03-01T00:00:00Zhttps://www.dovepress.com/abnormal-n-glycosylation-of-human-lens-epithelial-cells-in-type-2-diab-peer-reviewed-article-OPTHhttps://doaj.org/toc/1177-5483Ivan Ramos-Martínez,1– 3 Oscar Vivanco-Rojas,2 Brenda Juárez-Domínguez,2 Luis Hernández-Zimbrón,1,2 Lenin Ochoa-de la Paz,1,2 Hugo Quiroz-Mercado,2 Eleazar Ramírez-Hernández,1 Rosario Gulias-Cañizo,4 Edgar Zenteno1,2 1Departamento de Bioquímica, Facultad de Medicina UNAM, Ciudad de Mexico, 04510, Mexico; 2Departamento de Investigación, Asociación para Evitar la Ceguera en Mexico I.A.P. Hospital Dr. Luis Sánchez Bulnes, Mexico City, Mexico; 3Glycobiology, Cell Growth and Tissue Repair Research Unit (Gly-CRRET), Université Paris Est Créteil (UPEC), Créteil, France; 4Centro de Investigación en Ciencias de la Salud (CICSA), Universidad Anáhuac Mexico, Huixquilucan, Estado de Mexico, MexicoCorrespondence: Rosario Gulias-Cañizo; Edgar Zenteno Email rosariogulias@yahoo.com.mx; ezenteno@servidor.unam.mxPurpose: In order to better understand cataract development, we analyzed the glycosylation profile of human lens epithelial cells (HLECs) from anterior lens capsules of type 2 diabetes mellitus (T2DM) and non-diabetic (ND) patients undergoing routine cataract surgery.Setting: Research Department of the Asociación para Evitar la Ceguera, Hospital “Dr. Luis Sánchez Bulnes”, Mexico.Design: Experimental study.Methods: Evaluation of anterior lens capsules from T2DM and ND patients undergoing phacoemulsification and free from other ocular diseases.Results: Hematoxylin-eosin staining revealed HLECs alterations in T2DM samples. From lectins with different sugar specificities used, concanavalin A showed significant differences, labeling homogeneously both in the cytoplasm and in cell membranes in ND capsules, while in T2DM capsules, in addition to membrane and cytoplasm labeling, there were perinuclear vesicles with high concanavalin A labeling. Two-dimensional gel electrophoresis showed that T2DM patients have a ∼ 65-kDa spot with an isoelectric point of 5.5 with a higher density compared to ND capsules, and liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis showed 62% homology with type-1 cytokeratin. Immunohistochemistry using anti-pan cytokeratin antibody revealed co-localization with concanavalin A, and a lectin blot revealed with concanavalin A showed a band of ∼ 65 kDa, a molecular weight that corresponds to human type 1 cytokeratin.Conclusion: These results suggest that over-expression of N-glycosidically linked human type 1 cytokeratin may induce capsule disruption and affect selective permeability, allowing the entry of different molecules to the lens that facilitate cataract progression.Keywords: glycosylation, human epithelial lens cells, diabetes mellitus, cataractRamos-Martínez IVivanco-Rojas OJuárez-Domínguez BHernández-Zimbrón LOchoa-de la Paz LQuiroz-Mercado HRamírez-Hernández EGulias-Cañizo RZenteno EDove Medical Pressarticleglycosylationhuman epithelial lens cellsdiabetes mellituscataractOphthalmologyRE1-994ENClinical Ophthalmology, Vol Volume 15, Pp 1365-1373 (2021)
institution DOAJ
collection DOAJ
language EN
topic glycosylation
human epithelial lens cells
diabetes mellitus
cataract
Ophthalmology
RE1-994
spellingShingle glycosylation
human epithelial lens cells
diabetes mellitus
cataract
Ophthalmology
RE1-994
Ramos-Martínez I
Vivanco-Rojas O
Juárez-Domínguez B
Hernández-Zimbrón L
Ochoa-de la Paz L
Quiroz-Mercado H
Ramírez-Hernández E
Gulias-Cañizo R
Zenteno E
Abnormal N-Glycosylation of Human Lens Epithelial Cells in Type-2 Diabetes May Contribute to Cataract Progression
description Ivan Ramos-Martínez,1– 3 Oscar Vivanco-Rojas,2 Brenda Juárez-Domínguez,2 Luis Hernández-Zimbrón,1,2 Lenin Ochoa-de la Paz,1,2 Hugo Quiroz-Mercado,2 Eleazar Ramírez-Hernández,1 Rosario Gulias-Cañizo,4 Edgar Zenteno1,2 1Departamento de Bioquímica, Facultad de Medicina UNAM, Ciudad de Mexico, 04510, Mexico; 2Departamento de Investigación, Asociación para Evitar la Ceguera en Mexico I.A.P. Hospital Dr. Luis Sánchez Bulnes, Mexico City, Mexico; 3Glycobiology, Cell Growth and Tissue Repair Research Unit (Gly-CRRET), Université Paris Est Créteil (UPEC), Créteil, France; 4Centro de Investigación en Ciencias de la Salud (CICSA), Universidad Anáhuac Mexico, Huixquilucan, Estado de Mexico, MexicoCorrespondence: Rosario Gulias-Cañizo; Edgar Zenteno Email rosariogulias@yahoo.com.mx; ezenteno@servidor.unam.mxPurpose: In order to better understand cataract development, we analyzed the glycosylation profile of human lens epithelial cells (HLECs) from anterior lens capsules of type 2 diabetes mellitus (T2DM) and non-diabetic (ND) patients undergoing routine cataract surgery.Setting: Research Department of the Asociación para Evitar la Ceguera, Hospital “Dr. Luis Sánchez Bulnes”, Mexico.Design: Experimental study.Methods: Evaluation of anterior lens capsules from T2DM and ND patients undergoing phacoemulsification and free from other ocular diseases.Results: Hematoxylin-eosin staining revealed HLECs alterations in T2DM samples. From lectins with different sugar specificities used, concanavalin A showed significant differences, labeling homogeneously both in the cytoplasm and in cell membranes in ND capsules, while in T2DM capsules, in addition to membrane and cytoplasm labeling, there were perinuclear vesicles with high concanavalin A labeling. Two-dimensional gel electrophoresis showed that T2DM patients have a ∼ 65-kDa spot with an isoelectric point of 5.5 with a higher density compared to ND capsules, and liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis showed 62% homology with type-1 cytokeratin. Immunohistochemistry using anti-pan cytokeratin antibody revealed co-localization with concanavalin A, and a lectin blot revealed with concanavalin A showed a band of ∼ 65 kDa, a molecular weight that corresponds to human type 1 cytokeratin.Conclusion: These results suggest that over-expression of N-glycosidically linked human type 1 cytokeratin may induce capsule disruption and affect selective permeability, allowing the entry of different molecules to the lens that facilitate cataract progression.Keywords: glycosylation, human epithelial lens cells, diabetes mellitus, cataract
format article
author Ramos-Martínez I
Vivanco-Rojas O
Juárez-Domínguez B
Hernández-Zimbrón L
Ochoa-de la Paz L
Quiroz-Mercado H
Ramírez-Hernández E
Gulias-Cañizo R
Zenteno E
author_facet Ramos-Martínez I
Vivanco-Rojas O
Juárez-Domínguez B
Hernández-Zimbrón L
Ochoa-de la Paz L
Quiroz-Mercado H
Ramírez-Hernández E
Gulias-Cañizo R
Zenteno E
author_sort Ramos-Martínez I
title Abnormal N-Glycosylation of Human Lens Epithelial Cells in Type-2 Diabetes May Contribute to Cataract Progression
title_short Abnormal N-Glycosylation of Human Lens Epithelial Cells in Type-2 Diabetes May Contribute to Cataract Progression
title_full Abnormal N-Glycosylation of Human Lens Epithelial Cells in Type-2 Diabetes May Contribute to Cataract Progression
title_fullStr Abnormal N-Glycosylation of Human Lens Epithelial Cells in Type-2 Diabetes May Contribute to Cataract Progression
title_full_unstemmed Abnormal N-Glycosylation of Human Lens Epithelial Cells in Type-2 Diabetes May Contribute to Cataract Progression
title_sort abnormal n-glycosylation of human lens epithelial cells in type-2 diabetes may contribute to cataract progression
publisher Dove Medical Press
publishDate 2021
url https://doaj.org/article/48d9e7f4e5194413b14baefcc0529eb0
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