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(Circulation Research. 2003;92:130.)
© 2003 American Heart Association, Inc.

Editorials

Serine Phosphorylation and Suppression of Apoptosis by the Small Heat Shock Protein B-Crystallin

Keith A. Webster

From the Department of Molecular and Cellular Pharmacology, University of Miami Medical Center, Miami, Fla.

Correspondence to Keith A. Webster, Dept of Molecular and Cellular Pharmacology, University of Miami Medical Center, 1600 NW 10th Ave, RMSB 6038, Miami, FL 33136. E-mail kwebster@chroma.med.miami.edu

Key Words: apoptosis • p38 • mitogen-activated protein kinase • crystallin • small heat shock protein

An extract of the first 250 words of the full text is provided, because this article has no abstract.

A poptotic death of cardiac myocytes is a central feature of ischemic heart disease and a prime target for therapeutic intervention. Multiple stress factors are associated with ischemic stress and a battery of intrinsic pathways work to attenuate damage. These include antioxidants, antiapoptotic factors such as Bcl-2 proteins, and endogenous caspase inhibitors such as ARC (see review¹). B-crystallin is a relative newcomer to this defensive arsenal; it has strong antiapoptotic properties and, when fully induced, may constitute as much as 5% of total cardiac myocyte protein. As such, B-crystallin may have critical structural as well as protective functions in the heart. The signaling pathways that regulate B-crystallin activity and the molecular mechanism of protection are not understood and some aspects of these are presently controversial. In this issue of Circulation Research, Morrison et al² describe the involvement of a critical serine residue at position 59 of the B-crystallin protein that is targeted by the p38ß-MAPKAP-K2 pathway during ischemic stress. They show that phosphorylation of this serine may be the key step for the activation and regulation of the antiapoptotic function(s) of B-crystallin during ischemia.

Crystallin Family Proteins

The crystallins are a family of dual function proteins responsible for the transparent and refractive properties of the eye lens. At least 11 vertebrate crystallins have been described and several of these have secondary chaperoning and antioxidant activities that serve to protect the lens from light-induced oxidative stress (see reviews^3,4). B-crystallin is also a small heat shock protein (smHSP) structurally related to other . . . [Full Text of this Article]

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