title: Non-enzymatic glycation of α-crystallin as an in vitro model for aging, diabetes and degenerative diseases.
abstract: Alpha crystallin, a small heat-shock protein, has been studied extensively for its chaperone function. Alpha crystallin subunits are expressed in stress conditions and have been found to prevent apoptosis by inhibiting the activation of caspase pathway. Non-enzymatic glycation of protein leads to the formation of advanced glycation end-products (AGEs). These AGEs bind to receptors and lead to blocking the signaling pathways or cause protein precipitation as observed in aggregation-related diseases. Methylglyoxal (MGO) is one of the major glycating agents expressed in pathological conditions due to defective glycolysis pathway. MGO reacts rapidly with proteins, forms AGEs and finally leads to aggregation. The goal of this study was to understand the non-enzymatic glycation-induced structural damage in alpha crystallin using biophysical and spectroscopic characterization. This will help to develop better disease models for understanding the biochemical pathways and also in drug discovery.
authors.affiliation: Department of Chemistry and Biochemistry, Northern Illinois University, DeKalb, USA.
authors.forename: Devi Kalyan
authors.initials: DK
authors.lastname: Karumanchi
authors.affiliation: Department of Physics, Northern Illinois University, DeKalb, USA.
authors.forename: Nuwan
authors.initials: N
authors.lastname: Karunaratne
authors.affiliation: Department of Physics, Northern Illinois University, DeKalb, USA.
authors.forename: Laurence
authors.initials: L
authors.lastname: Lurio
authors.affiliation: Department of Physics, Northern Illinois University, DeKalb, USA.
authors.forename: James P
authors.initials: JP
authors.lastname: Dillon
authors.affiliation: Department of Chemistry and Biochemistry, Northern Illinois University, DeKalb, USA. gaillard@niu.edu.|Department of Biological Sciences, Northern Illinois University, 1425 W Lincoln Hwy, DeKalb, IL, 60115, USA. gaillard@niu.edu.
authors.forename: Elizabeth R
authors.initials: ER
authors.lastname: Gaillard
mesh_terms: D000375:Aging; D000818:Animals; D017209:Apoptosis; D002386:Cataract / Q000473:pathology; D002417:Cattle; D003920:Diabetes Mellitus / Q000473:pathology*; D004195:Disease Models, Animal; D055808:Drug Discovery; D017127:Glycation End Products, Advanced / Q000378:metabolism; D006019:Glycolysis; D006031:Glycosylation; D006360:Heat-Shock Proteins / Q000378:metabolism; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D007908:Lens, Crystalline / Q000473:pathology; D008027:Light; D018832:Molecular Chaperones / Q000378:metabolism; D019636:Neurodegenerative Diseases / Q000473:pathology*; D011305:Presbyopia / Q000473:pathology; D011485:Protein Binding; D011765:Pyruvaldehyde / Q000737:chemistry; D012542:Scattering, Radiation; D015398:Signal Transduction; D013050:Spectrometry, Fluorescence; D013696:Temperature; D038201:alpha-Crystallins / Q000737:chemistry*
chemical_list: D017127:Glycation End Products, Advanced; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D038201:alpha-Crystallins; D011765:Pyruvaldehyde
keywords: Aging; Alpha crystallin; Cataract; Degenerative diseases; Diabetes; Lens; Presbyopia