Regulation of Angiogenesis by the Small Heat Shock Protein αB-Crystallin

Author(s): Lothar C. Dieterich, Anna Dimberg

Journal Name: Current Angiogenesis (Discontinued)

Volume 1 , Issue 1 , 2012


αB-crystallin is a member of the small heat shock protein family, primarily known for their ability to bind to and stabilize un- or misfolded proteins and protect cells from protein denaturation-induced damage. Besides its general chaperone function, αB-crystallin has been assigned additional activities, such as inhibition of apoptosis, cytoskeletal stabilization and turnover, and ubiquitination and degradation of specific target proteins. αB-crystallin is frequently expressed in endothelial cells and perivascular cells, and can be further induced by pro-angiogenic growth factors and different types of cellular stress. Recently, αB-crystallin has been implicated in the regulation of angiogenesis and blood vessel function by endothelial cell intrinsic and extrinsic mechanisms. The aim of this review is to summarize some of the recent findings concerning the various functions of αB-crystallin, with a specific focus on endothelial cell biology and regulation of angiogenesis.

Keywords: αB-crystallin, angiogenesis, apoptosis, chaperone, endothelial, heat shock protein, stress, VEGF

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Article Details

Year: 2012
Published on: 28 March, 2012
Page: [39 - 45]
Pages: 7
DOI: 10.2174/2211552811201010039

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