Effect of aging on the chaperone-like function of human α-crystallin assessed by three methods
نویسندگان
چکیده
α-Crystallin can function as a molecular chaperone by preventing unwanted interactions. This paper presents the effects of aging and cataract on the chaperone-like properties of α-crystallin from soluble fractions from the cortex and nucleus of human lenses by using three assays : enzyme inactivation and two turbidity experiments. The three methods complemented each other. There was no decrease with age of chaperone-like function
منابع مشابه
Effect of Mild Heating on Human Lens Epithelial Cells: A Possible Model of Lens Aging
This study aims to investigate the effect of mild heating on lens epithelial cells and to explore its possibility as an in vitro model for lens aging. Human lens epithelial cells (LECs) were heated at 50 °C for a cellular lens aging study. Analysis of the head group order of lens membranes was performed using Laurdan labeling. Immunofluorescence was performed to detect changes in α-crystallin e...
متن کاملEffect of glycation on α-crystallin structure and chaperone-like function
The chaperone-like activity of α-crystallin is considered to play an important role in the maintenance of the transparency of the eye lens. However, in the case of aging and in diabetes, the chaperone function of α-crystallin is compromized, resulting in cataract formation. Several post-translational modifications, including non-enzymatic glycation, have been shown to affect the chaperone funct...
متن کاملαA-Crystallin Peptide 66SDRDKFVIFLDVKHF80 Accumulating in Aging Lens Impairs the Function of α-Crystallin and Induces Lens Protein Aggregation
BACKGROUND The eye lens is composed of fiber cells that are filled with α-, β- and γ-crystallins. The primary function of crystallins is to maintain the clarity of the lens through ordered interactions as well as through the chaperone-like function of α-crystallin. With aging, the chaperone function of α-crystallin decreases, with the concomitant accumulation of water-insoluble, light-scatterin...
متن کاملHydroimidazolone Modification of the Conserved Arg12 in Small Heat Shock Proteins: Studies on the Structure and Chaperone Function Using Mutant Mimics
Methylglyoxal (MGO) is an α-dicarbonyl compound present ubiquitously in the human body. MGO reacts with arginine residues in proteins and forms adducts such as hydroimidazolone and argpyrimidine in vivo. Previously, we showed that MGO-mediated modification of αA-crystallin increased its chaperone function. We identified MGO-modified arginine residues in αA-crystallin and found that replacing su...
متن کاملModulation of α-crystallin chaperone activity in diabetic rat lens by curcumin
α-Crystallin, a small heat shock protein (sHSP), constitutes the major portion of eye lens cytoplasm and its concentration in the lens can reach up to 50% of the total protein. Like other sHSP, α-crystallin displays chaperone-like activity in suppressing the aggregation of various proteins and in preventing inactivation of enzymes due to heat and other stress conditions [1-6]. Hence, in additio...
متن کامل