Department of Biochemistry, School of Biology, Moscow State University, Moscow, Russian Federation.
Physiol Rev. 2011 Oct;91(4):1123-59. doi: 10.1152/physrev.00023.2010.
Modern classification of the family of human small heat shock proteins (the so-called HSPB) is presented, and the structure and properties of three members of this family are analyzed in detail. Ubiquitously expressed HSPB1 (HSP27) is involved in the control of protein folding and, when mutated, plays a significant role in the development of certain neurodegenerative disorders. HSPB1 directly or indirectly participates in the regulation of apoptosis, protects the cell against oxidative stress, and is involved in the regulation of the cytoskeleton. HSPB6 (HSP20) also possesses chaperone-like activity, is involved in regulation of smooth muscle contraction, has pronounced cardioprotective activity, and seems to participate in insulin-dependent regulation of muscle metabolism. HSPB8 (HSP22) prevents accumulation of aggregated proteins in the cell and participates in the regulation of proteolysis of unfolded proteins. HSPB8 also seems to be directly or indirectly involved in regulation of apoptosis and carcinogenesis, contributes to cardiac cell hypertrophy and survival and, when mutated, might be involved in development of neurodegenerative diseases. All small heat shock proteins play important "housekeeping" roles and regulate many vital processes; therefore, they are considered as attractive therapeutic targets.
本文介绍了人类小热休克蛋白家族（所谓的 HSPB）的现代分类，并详细分析了该家族的三个成员的结构和特性。普遍表达的 HSPB1（HSP27）参与蛋白质折叠的控制，当发生突变时，在某些神经退行性疾病的发展中起着重要作用。HSPB1 直接或间接参与细胞凋亡的调节，保护细胞免受氧化应激，并参与细胞骨架的调节。HSPB6（HSP20）也具有分子伴侣样活性，参与调节平滑肌收缩，具有明显的心脏保护活性，并且似乎参与胰岛素依赖性肌肉代谢的调节。HSPB8（HSP22）防止细胞中聚集蛋白的积累，并参与未折叠蛋白的蛋白酶解调节。HSPB8 似乎还直接或间接地参与细胞凋亡和癌变的调节，有助于心肌细胞肥大和存活，并且当发生突变时，可能参与神经退行性疾病的发展。所有小热休克蛋白都发挥着重要的“管家”作用，并调节许多重要的生命过程；因此，它们被认为是有吸引力的治疗靶点。
