αB-Crystallin Modulates Protein Aggregation of Abnormal Desmin
نویسندگان
چکیده
منابع مشابه
Effect of αB-Crystallin on Protein Aggregation in Drosophila
Disorganisation and aggregation of proteins containing expanded polyglutamine (polyQ) repeats, or ectopic expression of α-synuclein, underlie neurodegenerative diseases including Alzheimer's, Parkinson, Huntington, Creutzfeldt diseases. Small heat-shock proteins, such as αB-crystallin, act as chaperones to prevent protein aggregation and play a key role in the prevention of such protein disorga...
متن کاملThe specificity of the interaction between αB-crystallin and desmin filaments and its impact on filament aggregation and cell viability
CRYAB (αB-crystallin) is expressed in many tissues and yet the R120G mutation in CRYAB causes tissue-specific pathologies, namely cardiomyopathy and cataract. Here, we present evidence to demonstrate that there is a specific functional interaction of CRYAB with desmin intermediate filaments that predisposes myocytes to disease caused by the R120G mutation. We use a variety of biochemical and bi...
متن کاملDesmin and αB-crystallin interplay in the maintenance of mitochondrial homeostasis and cardiomyocyte survival.
The association of desmin with the α-crystallin Β-chain (αΒ-crystallin; encoded by CRYAB), and the fact that mutations in either one of them leads to heart failure in humans and mice, suggests a potential compensatory interplay between the two in cardioprotection. To address this hypothesis, we investigated the consequences of αΒ-crystallin overexpression in the desmin-deficient (Des-/-) mouse ...
متن کاملRescue of αB Crystallin (HSPB5) Mutants Associated Protein Aggregation by Co-Expression of HSPB5 Partners
HSPB5 (also called αB-crystallin) is a ubiquitously expressed small heat shock protein. Mutations in HSPB5 have been found to cause cataract, but are also associated with a subgroup of myofibrillar myopathies. Cells expressing each of these HSPB5 mutants are characterized by the appearance of protein aggregates of primarily the mutant HSPB5. Like several members of the HSPB family, HSPB5 can fo...
متن کاملInhibition of Mutant αB Crystallin‐Induced Protein Aggregation by a Molecular Tweezer
BACKGROUND Compromised protein quality control causes the accumulation of misfolded proteins and intracellular aggregates, contributing to cardiac disease and heart failure. The development of therapeutics directed at proteotoxicity-based pathology in heart disease is just beginning. The molecular tweezer CLR01 is a broad-spectrum inhibitor of abnormal self-assembly of amyloidogenic proteins, i...
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ژورنال
عنوان ژورنال: Circulation Research
سال: 2003
ISSN: 0009-7330,1524-4571
DOI: 10.1161/01.res.0000102401.77712.ed