α-Crystallin is a lens protein that contains two homologous subunits: αA- and αB-crystallins. α-Crystallin displays chaperone-like activity and plays an important role in maintaining lens transparency. It has been noted that in diabetic conditions of rats there is a decline in the chaperone activity of α-Crystallin. Research has shown that a dietary antioxidant, curcumin, can prevent this loss of chaperone activity.
Biochem/physiol Actions
α-Crystallin is a small heat-shock protein that has chaperone-like activity, preventing protein aggregation in vitro. Point mutations in α-crystallin genes are believed to be responsible for hereditary cataract development.
Purpose/Aim: The amount of membrane-bound α-crystallin increases significantly with age and cataract formation, accompanied by a corresponding decline in the level of α-crystallin in the lens cytoplasm. The purpose of this research is to evaluate the binding affinity of α-crystallin
Binding of Alpha-Crystallin to Cortical and Nuclear Lens Lipid Membranes Derived from a Single Lens.
Timsina, et al.
International Journal of Molecular Sciences, 23 (2023)
Protein science : a publication of the Protein Society, 31(8), e4378-e4378 (2022-07-29)
Molecular chaperones are essential to maintain proteostasis. While the functions of intracellular molecular chaperones that oversee protein synthesis, folding and aggregation, are established, those specialized to work in the extracellular environment are less understood. Extracellular proteins reside in a considerably
It is well-studied that the significant factor in cataract formation is the association of α-crystallin, a major eye lens protein, with the fiber cell plasma membrane of the eye lens. The fiber cell plasma membrane of the eye lens consists
Delay of diabetic cataract in rats by the antiglycating potential of cumin through modulation of α-crystallin chaperone activity.
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