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Ann Thorac Surg 1996;61:1411-1412
© 1996 The Society of Thoracic Surgeons

Invited Commentary

Invited Commentary

Rakesh C. Kukreja, PhD, Michael L. Hess, MD

Eric Lipman Laboratories of Molecular and Cellular Cardiology, Division of Cardiology, Medical College of Virginia, Richmond, VA 23298

The first 20% of the full text of this article appears below.

See also page 1407.

When living cells are subjected to a short elevation in temperature, certain proteins, known as heat-stress or heat-shock proteins (HSPs), are synthesized. These proteins have been shown to subsequently protect the myocyte from not only further heat stress, but other metabolic insults, including ischemia/reperfusion injury [1, 2]. The induction of these HSPs has been shown to protect the myocardium from ischemic damage in a number of different models and species. The effects have included a reduction in infarct size as demonstrated by tetrazolium staining, reduced release of creatine kinase, and improvement in contractile functions. Increased levels of HSP have been associated with preservation of tissue adenosine triphosphate after ischemia-reperfusion and decreased production of oxygen-derived . . . [Full Text of this Article]


Related Article

Kinetics of Induction and Protective Effect of Heat-Shock Proteins After Cardioplegic Arrest
Mohamed Amrani, Joseph Corbett, Samuel Y. Boateng, Michael J. Dunn, and Magdi H. Yacoub
Ann. Thorac. Surg. 1996 61: 1407-1411. [Abstract] [Full Text]





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