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Am J Physiol Regul Integr Comp Physiol 277: R11-R17, 1999;
0363-6119/99 $5.00
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Vol. 277, Issue 1, R11-R17, July 1999

Mitochondrial protein and HSP70 signaling after ischemia in hypothermic-adapted hearts augmented with glucose

Xue-Han Ning, Cheng-Su Xu, and Michael A. Portman

Cardiology Division, Department of Pediatrics, University of Washington, Seattle 98195; and Children's Hospital and Regional Medical Center, Seattle, Washington 98105

Hypothermia improves resistance to subsequent ischemia in the cardioplegic-arrested heart (CAH). This adaptive process produces mRNA elevation for heat shock protein (HSP) 70-1 and mitochondrial proteins, adenine nucleotide translocator (ANT1), and beta -F1-ATPase. Glucose in cardioplegia also enhances myocardial protection. These processes might be linked to reduced ATP depletion. To assess for synergism between these protective processes, isolated rabbit hearts (n = 91) were perfused at 37°C and exposed to ischemic cardioplegic arrest for 2 h. Hearts were in four groups: control (C), hypothermia adapted (H) perfused to 31°C 20 min before ischemia, 22 mM glucose (G) in cardioplegia, and hypothermic adaptation and glucose (HG). Developed pressure (DP), dP/dtmax, and pressure-rate product (PRP) improved (P < 0.05) in G, H, and HG compared with C during reperfusion. DP and PRP were elevated in HG over H and G. ATP was higher in G, H, and HG, although no additional increase in HG over H was found. Lactate and CO2 production were elevated in G only. The mRNA expression for HSP70-1, ANT1, and beta -F1-ATPase was elevated severalfold in H and HG, but not G over C during reperfusion. In conclusion, glucose provides additional functional improvement in H. Additionally, neither ATP levels nor anaerobic metabolism are linked to mRNA expression for HSP70, ANT1, or beta -F1-ATPase in CAH.

stress response; RNA; cardiac surgery


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