Srinivas 6 α - Crystallins , small heat shock proteins with diverse functions in cell survival and stress tolerance
نویسندگان
چکیده
α-Crystallin, a multimeric protein, composed of αAand αB-crystallin subunits is abundantly present in the eye lens. Both the crystallin subunits have also been found in other tissues and exhibit sequence homology with small heat shock proteins. The expression of αB-crystallin is induced under heat and other stresses and in several neurodegenerative diseases. As a member of the small heat shock protein family, it confers thermo-tolerance to cells, exhibits molecular chaperone activity in preventing aggregation of proteins, prevents amyloid fibril formation, prevents Correspondence/Reprint request: Dr. Ch. Mohan Rao, Deputy Director (Director Grade Scientist), Centre for Cellular and Molecular Biology, Uppal Road, Hyderabad 500007, India. E-mail: [email protected] Ch. Mohan Rao et al. 94 thermal inactivation of enzymes and helps in refolding enzymes either alone or with the help of other heat shock proteins. Growing evidences show that it also involved in important cellular events such as cell differentiation, apoptosis, protein turn over and quality control indicating that α-crystallin plays a diverse functional role. Its involvement in several neurodegenerative diseases and cancer suggests that a complete understanding of its role may mark this small heat shock protein a potential therapeutic target.
منابع مشابه
Diabetes impairs the neuroprotective properties of retinal alpha-crystallins.
PURPOSE α-Crystallins are small heat shock proteins that regulate cellular damage and cell survival. Expression of the proteins of the crystallin superfamily in the retina and their role in neuronal cell survival were investigated in two animal models of diabetes and retinal neurons in culture. METHODS Crystallin expression was assessed in streptozotocin-induced and Ins2(Akita) diabetic mice ...
متن کاملDendrosomal Nanocurcumin Induces Changes in the Expression Levels of Heat Shock Proteins in the AGS Cell Line: Cellular Tolerance or Smart Apoptosis Induction
Objectives:The expression levels of heat shock proteins (HSPs) are elevated in many cancers, and this overexpression is often associated with both a poor survival and a therapeutic outcome. Curcumin is an anti-cancer agent that also induces a heat shock response. HSPs confer resistance to curcumin-induced apoptosis in cancerous cells. The aim of the current study was to analyze variations in th...
متن کاملATP-enhanced molecular chaperone functions of the small heat shock protein human alphaB crystallin.
We report direct experimental evidence that human alphaB-crystallin, a member of the small heat shock protein family, actively participates in the refolding of citrate synthase (CS) in vitro. In the presence of 3.5 mM ATP, CS reactivation by alphaB-crystallin was enhanced approximately twofold. Similarly, 3.5 mM ATP enhanced the chaperone activity of alphaB-crystallin on the unfolding and aggre...
متن کاملAnalysis of the Cytoprotective Role of α-Crystallins in Cell Survival and Implication of the αA-Crystallin C-Terminal Extension Domain in Preventing Bax-Induced Apoptosis
α-Crystallins, initially described as the major structural proteins of the lens, belong to the small heat shock protein family. Apart from their function as chaperones, α-crystallins are involved in the regulation of intracellular apoptotic signals. αA- and αB-crystallins have been shown to interfere with the mitochondrial apoptotic pathway triggering Bax pro-apoptotic activity and downstream a...
متن کاملGene sharing, lens crystallins and speculations on an eye/ear evolutionary relationship.
The crystallins comprise 80-90% of the water-soluble proteins of the transparent, cellular, refractive eye lens and are responsible for its optical properties. Comparative studies have established that the crystallins are surprisingly diverse and often differ among species in a taxon-specific fashion. In general, the crystallins are derived from or identical to metabolic enzymes or stress (smal...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
دوره شماره
صفحات -
تاریخ انتشار 2007