Heat shock protein beta-6

Definition:

Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state. Seems to have versatile functions in various biological processes. Plays a role in regulating muscle function such as smooth muscle vasorelaxation and cardiac myocyte contractility. May regulate myocardial angiogenesis implicating KDR. Overexpression mediates cardioprotection and angiogenesis after induced damage. Stabilizes monomeric YWHAZ thereby supporting YWHAZ chaperone-like activity.

References:

[1]. Olesya V Bukach, et al. Some properties of human small heat shock protein Hsp20 (HspB6). Eur J Biochem. 2004 Jan;271(2):291-302. [Content Brief]

[2]. Xiaowei Zhang, et al. Hsp20 functions as a novel cardiokine in promoting angiogenesis via activation of VEGFR2. PLoS One. 2012;7(3):e32765. [Content Brief]

[3]. Margit Fuchs, et al. Identification of the key structural motifs involved in HspB8/HspB6-Bag3 interaction. Biochem J. 2009 Dec 14;425(1):245-55. [Content Brief]

[4]. Nikolai N Sluchanko, et al. Monomeric 14-3-3ζ has a chaperone-like activity and is stabilized by phosphorylated HspB6. Biochemistry. 2012 Aug 7;51(31):6127-38. [Content Brief]

[5]. Michel J Vos, et al. HSPB7 is the most potent polyQ aggregation suppressor within the HSPB family of molecular chaperones. Hum Mol Genet. 2010 Dec 1;19(23):4677-93. [Content Brief]

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