Title:Regulation of Angiogenesis by the Small Heat Shock Protein αB-Crystallin
Volume: 1
Issue: 1
Author(s): Lothar C. Dieterich and Anna Dimberg
Affiliation:
Keywords:
αB-crystallin, angiogenesis, apoptosis, chaperone, endothelial, heat shock protein, stress, VEGF
Abstract: 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.
