作者: Wilbert C. Boelens
DOI: 10.1016/J.PBIOMOLBIO.2014.02.005
关键词:
摘要: αB-crystallin, also called HspB5, is a molecular chaperone able to interact with unfolding proteins. By interacting, it inhibits further unfolding, thereby preventing protein aggregation and allowing ATP-dependent chaperones refold the αB-crystallin belongs family of small heat-shock proteins (sHsps), which in humans consists 10 different members. The forms large oligomeric complexes, containing up 40 or more subunits, vivo consist heterooligomeric complexes formed by mixture other sHsps. highly expressed lens lesser extent several tissues, among heart, skeletal muscle brain. plays role cellular processes, such as signal transduction, degradation, stabilization cytoskeletal structures apoptosis. Mutations gene can have detrimental effects, leading pathologies cataract cardiomyopathy. This review describes biological roles special focus on its function eye lens, heart In addition therapeutic potential discussed.