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J Biol Chem, Vol. 274, Issue 51, 36592-36600, December 17, 1999

Identification and Characterization of cvHsp
A NOVEL HUMAN SMALL STRESS PROTEIN SELECTIVELY EXPRESSED IN CARDIOVASCULAR AND INSULIN-SENSITIVE TISSUES^*

Stéphane Krief^§, Jean-François Faivre, Philippe Robert, Bertrand Le Douarin^¶, Nicole Brument-Larignon, Isabelle Lefrère, Mark M. Bouzyk^**, Karen M. Anderson, Larry D. Greller, Frank L. Tobin, Michel Souchet, and Antoine Bril

From  SmithKline Beecham Laboratoires Pharmaceutiques, 4 rue du Chesnay-Beauregard, BP 58, 35762 Saint-Grégoire, France, the  CNRS Unité Propre 041, Rennes, France, ^** SmithKline Beecham Pharmaceuticals, New Frontiers Science Park, CM19 5AD Harlow, United Kingdom, and  SmithKline Beecham Pharmaceuticals, King of Prussia, Pennsylvania 19406-0939

Starting with computational tools that search for tissue-selective expression of assembled expressed sequenced tags, we have identified by focusing on heart libraries a novel small stress protein of 170 amino acids that we named cvHsp. cvHsp was found as being computationally selectively and highly (0.3% of the total RNA) expressed in human heart. The cvHsp gene mapped to 1p36.23-p34.3 between markers D1S434 and D1S507. The expression of cvHsp was analyzed with RNA dot, Northern blots, or reverse transcription-polymerase chain reaction: expression was high in heart, medium in skeletal muscle, and low in aorta or adipose tissues. In the heart of rat models of cardiac pathologies, cvHsp mRNA expression was either unchanged (spontaneous hypertension), up-regulated (right ventricular hypertrophy induced by monocrotaline treatment), or down-regulated (left ventricular hypertrophy following aortic banding). In obese Zucker rats, cvHsp mRNA was increased in skeletal muscle, brown, and white adipose tissues but remained unchanged in the heart. Western blot analysis using antipeptide polyclonal antibodies revealed two specific bands at 23 and 25 kDa for cvHsp in human heart. cvHsp interacted in both yeast two-hybrid and immunoprecipitation experiments with -filamin or actin-binding protein 280. Within cvHsp, amino acid residues 56-119 were shown to be important for its specific interaction with the C-terminal tail of -filamin.

This article is dedicated to the memory of Dr. Bertrand Le Douarin.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EMBL Data Bank with accession number(s) AF155908 (human), AF155909 (mouse), and AF155910 (rat).

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