https://scholars.lib.ntu.edu.tw/handle/123456789/406708
Title: | Effects of glycation on human £^D-crystallin proteins by different glycation-inducing agents | Authors: | Li C.-T. How S.-C. Chen M.-E. Lo C.-H. Chun M.-C. Chang C.-K. Chen W.-A. Wu J.W. Wang S.S.-S. |
Issue Date: | 2018 | Journal Volume: | 118 | Start page/Pages: | 442-451 | Source: | International Journal of Biological Macromolecules | Abstract: | Human £^D-crystallin (H£^D-crystallin), a major protein component of the human eye lens, is associated with the development of juvenile- and mature-onset cataracts. Evidence suggests that nonenzymatic protein glycation plays an important role in the aetiology of cataract and diabetic sequelae. This research compared the effects of various glycation modifiers on H£^D-crystallin aggregation, by treating samples of H£^D-crystallin with ribose, galactose, or methylglyoxal using several biophysical techniques. To measure advanced glycation end products, an N£`-(carboxyethyl)lysine enzyme-linked immunosorbent assay was performed on the glycating agent-treated H£^D-crystallin samples. Fructosamine production detection was performed for both ribose-treated and galactose-treated samples. Methylglyoxal-treated samples had the highest level of aggregation and the greatest extent of unfolding, and upon incubation for a minimum of 12 days, exhibited a marked enhancement in the amount of N£`-(carboxyethyl)lysine. The molecular profiles and morphological features of the glycated samples were highly correlated to the type of glycation agent used. These findings highlight a close connection between the type of glycation modifier and the various aggregation species that form. Thus, these results may facilitate deciphering of the molecular mechanism of diabetic cataractogenesis. ? 2018 |
URI: | https://scholars.lib.ntu.edu.tw/handle/123456789/406708 | ISSN: | 01418130 | DOI: | 10.1016/j.ijbiomac.2018.06.108 | SDG/Keyword: | advanced glycation end product receptor affecting agent; fructosamine; galactose; gamma crystallin; gamma D crystallin; methylglyoxal; n epsilon(carboxyethyl)lysine; ribose; unclassified drug; advanced glycation end product; CRYGD protein, human; galactose; gamma crystallin; lysine; N(6)-carboxyethyllysine; ribose; absorption spectroscopy; Article; circular dichroism; controlled study; enzyme linked immunosorbent assay; human; hydrophobicity; incubation time; limit of quantitation; molecular weight; polyacrylamide gel electrophoresis; protein aggregation; protein expression; protein function; protein glycosylation; protein secondary structure; protein unfolding; spectrofluorometry; transmission electron microscopy; ultraviolet spectrophotometry; analogs and derivatives; biosynthesis; cataract; chemistry; complication; diabetic complication; drug effect; genetics; glycosylation; lens; metabolism; pathology; protein denaturation; proteinosis; Cataract; Diabetes Complications; Fructosamine; Galactose; gamma-Crystallins; Glycation End Products, Advanced; Glycosylation; Humans; Lens, Crystalline; Lysine; Protein Aggregation, Pathological; Protein Denaturation; Pyruvaldehyde; Ribose |
Appears in Collections: | 化學工程學系 |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.