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J. Biol. Chem., Vol. 278, Issue 44, 43636-43644, October 31, 2003

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Cellular Redistribution of Inducible Hsp70 Protein in the Human and Rabbit Heart in Response to the Stress of Chronic Hypoxia

ROLE OF PROTEIN KINASES^*

Parvaneh Rafiee, Yang Shi, Kirkwood A. Pritchard, Jr., Hitoshi Ogawa, Annie L. W. Eis¶, Richard A. Komorowski||, Colleen M. Fitzpatrick, James S. Tweddell**, S. Bert Litwin**, Kathleen Mussatto, Robert D. Jaquiss**, and John E. Baker¶¶

From the Division of Pediatric Surgery, the Division of Gastroenterology, the ^¶Department of Pediatrics, the ^||Department of Pathology, the ^**Division of Cardiothoracic Surgery, and the Department of Biochemistry, Medical College of Wisconsin and the Section of Cardiothoracic Surgery, Children's Hospital of Wisconsin, Milwaukee, Wisconsin 53226

Many infants who undergo cardiac surgery have a congenital cyanotic defect where the heart is chronically perfused with hypoxemic blood. Infant hearts adapt to chronic hypoxemia by activation of intracellular protein kinase signal transduction pathways. However, the involvement of heat shock protein 70 in adaptation to chronic hypoxemia and its role in protein kinase signaling pathways is unknown. We determined expression of message and subcellular protein distribution for inducible (Hsp70i) and constitutive heat shock protein 70 (Hsc70) in chronically hypoxic and normoxic infant human and rabbit hearts and their relationship to protein kinases. In chronically hypoxic human and rabbit hearts message levels for Hsp70i were elevated 4- to 5-fold compared with normoxic hearts, Hsp70i protein was redistributed from the particulate to the cytosolic fraction. In normoxic infants Hsp70i protein was distributed almost equally between the cytosolic and particulate fractions. Hsc70 message and subcellular distribution of Hsc70 protein were unaffected by chronic hypoxia. We then determined if protein kinases influence Hsp70i protein subcellular distribution. In rabbit hearts SB203580 and chelerythrine reduced Hsp70i message levels, whereas SB203580, chelerythrine, and curcumin reversed the subcellular redistribution of Hsp70i protein caused by chronic hypoxia, with no effect in normoxic hearts, indicating regulation of Hsp70i message and subcellular distribution of Hsp70i protein in chronically hypoxic rabbit hearts is influenced by protein kinase C and mitogen-activated protein kinases, specifically p38 MAPK and JNK. We conclude the Hsp70 signal transduction pathway plays an important role in adaptation of infant human and rabbit hearts to chronic hypoxemia.

Received for publication, December 19, 2002 , and in revised form, August 11, 2003.

^* This work was supported by NHLBI, National Institutes of Health Grants HL54075 (to J. E. B.), HL65203 (to J. E. B.), and HL61414 (to K. A. P.), by Ronald McDonald's Children's Charities (to J. E. B.), by the Children's Hospital of Wisconsin Foundation (to J. S. T. and J. E. B.), and by the Digestive Disease Center, Medical College of Wisconsin (to P. R.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶¶ To whom correspondence should be addressed: Division of Pediatric Surgery, Medical College of Wisconsin, 8701 Watertown Plank Rd., Milwaukee, WI 53226. Tel.: 414-456-8706; Fax: 414-453-9700; E-mail: jbaker{at}mcw.edu.

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