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J Thorac Cardiovasc Surg 1998;115:200-204
© 1998 Mosby, Inc.

CARDIOPULMONARY SUPPORT AND PHYSIOLOGY

Relative induction of heat shock protein in coronary endothelial cells and cardiomyocytes: Implications for myocardial protection

From the Department of Cardiothoracic Surgery, Heart Science Centre,National Heart and Lung Institute at Harefield Hospital, Harefield, Middlesex,United Kingdom.

Received for publication April 7, 1997; revisions requested May 14,1997; revisions received July 9, 1997; accepted for publication August 13,1997. Address for reprints: Professor Sir Magdi Yacoub, FRCS, Departmentof Cardiothoracic Surgery Heart Science Centre, National Heart and Lung Instituteat Harefield Hospital, Harefield, Middlesex. UB9 6JH, United Kingdom.

Abstract

Objectives: Induction of the 70 kdheat shock protein in the heart is known to exert a protective effect againstpostischemic mechanical and endothelial dysfunction. However, the exact siteof induction and the mechanisms involved remain unknown. The aim of this studywas to investigate the relative capacity of endothelial and myocardial cellsto express the 70 kd heat shock protein in response to heat stress, as wellas their significance.

Methods: (1) Postischemic recoveryof cardiac mechanical and endothelial function was studied in isolated rathearts with and without endothelial denudation with saponin. (2) Semiquantitativedetermination of induction of 70 kd heat shock protein by Western immunoblottingwas performed in the whole cardiac homogenate, in isolated cardiac myocytes,and in coronary endothelial cells. (3) Immunocytochemistry was used to visualizethe distribution of induction of 70 kd heat shock protein in both cell types.

Results: Postischemic recovery (percentpreischemic value ± standard error of the mean) of cardiac outputin hearts from heat-stressed animals was significantly improved (66.7 ±6.9 vs 44.5 ± 4.5 in the control group, p < 0.01). In heat-stressed hearts treated with saponinno improvement in the recovery of cardiac output was noted (44.7 ±6.9 in heat-stressed hearts vs 38.0 ± 4.0 in heat-stressed, saponin-treatedhearts, p = not significant). Endothelialfunction (as assessed by the vasodilatory response to the endothelium-dependentvasodilator 5-hydroxytryptamine) improved from 31.0 ± 5.2 in thecontrol group to 65.8 ± 7.1 in heat-stressed hearts (p < 0.02 vs control) and dropped to –1.9 ±3.8 in heat-stressed hearts treated with saponin. Immunocytochemistry showedthat only sections of hearts from heat-treated rats showed a strong specificreaction with heat shock protein antibody. The positive staining was seenin endothelial cells. Induction of 70 kd heat shock protein content in thewhole cardiac homogenate from heat-stressed rats as measured by Western immunoblottingwas 5.2 ± 1.9 (vs 0.0 in non-heat–stressed rats, p < 0.0001) and dropped to 0.0 in heat-stressedhearts treated with saponin. The tentative amount of 70 kd heat shock proteinwas 18.1 ± 7.8 in isolated endothelial cells from heat-stressedhearts and 2.3 ± 2.3 in isolated cardiac myocytes (p < 0.01 vs endothelial cells).

Conclusions: Coronary endothelial cellsare the main site of induction of 70 kd heat shock protein in the heart andappear to contribute to the protective effects of heat stress on the recoveryof mechanical and endothelial function.

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