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.2019-05-092019-05-09201801418130https://scholars.lib.ntu.edu.tw/handle/123456789/406708Human £^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[SDGs]SDG3advanced 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; Ribosejournal article10.1016/j.ijbiomac.2018.06.1082-s2.0-85049078571https://www.scopus.com/inward/record.uri?eid=2-s2.0-85049078571&doi=10.1016%2fj.ijbiomac.2018.06.108&partnerID=40&md5=469d99e24c7c12546c1e03ea6e3a03c3