منابع مشابه
Correction: In Vivo Substrates of the Lens Molecular Chaperones αA-Crystallin and αB-Crystallin
αA-crystallin and αB-crystallin are members of the small heat shock protein family and function as molecular chaperones and major lens structural proteins. Although numerous studies have examined their chaperone-like activities in vitro, little is known about the proteins they protect in vivo. To elucidate the relationships between chaperone function, substrate binding, and human cataract forma...
متن کاملαA-Crystallin–Derived Mini-Chaperone Modulates Stability and Function of Cataract Causing αAG98R-Crystallin
BACKGROUND A substitution mutation in human αA-crystallin (αAG98R) is associated with autosomal dominant cataract. The recombinant mutant αAG98R protein exhibits altered structure, substrate-dependent chaperone activity, impaired oligomer stability and aggregation on prolonged incubation at 37 °C. Our previous studies have shown that αA-crystallin-derived mini-chaperone (DFVIFLDVKHFSPEDLTVK) fu...
متن کاملIncreased expression of αA-crystallin in human diabetic eye.
We recently demonstrated that αA-crystallin, a molecular chaperone, protected photoreceptors from apoptotic signals in intraocular inflammation. Advanced glycation end product (AGE) plays an important role in the progression of diabetic retinopathy. The aim of this study was to examine the expression of α-crystallins and apoptosis in human diabetic retina, and to analyze α-crystallin up-regulat...
متن کاملαA-crystallin and αB-crystallin reside in separate subcellular compartments in the developing ocular lens.
αA-Crystallin (αA) and αB-crystallin (αB), the two prominent members of the small heat shock family of proteins are considered to be two subunits of one multimeric protein, α-crystallin, within the ocular lens. Outside of the ocular lens, however, αA and αB are known to be two independent proteins, with mutually exclusive expression in many tissues. This dichotomous view is buoyed by the high e...
متن کاملMutations in Human αA-Crystallin/sHSP Affect Subunit Exchange Interaction with αB-Crystallin
BACKGROUND Mutation in αA-crystallin contributes to the development of congenital cataract in humans. Heterooligomerization of αA-crystallin and αB-crystallin is essential for maintaining transparency in the eye lens. The effect of congenital cataract causing mutants of αA-crystallin on subunit exchange and interaction with αB-crystallin is unknown. In the present study, interaction of the muta...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1987
ISSN: 0014-5793
DOI: 10.1016/0014-5793(87)80935-3