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Expression and Immunohistochemical Localization of Heat‐Shock Protein‐70 in Preconditioned Porcine Myocardium
Author(s) -
SHARMA HARI S.,
SNOECKX LUC H.,
SASSEN LOES M. A.,
KNöLL RALPH,
ANDRES JANUSZ,
VERDOUW PIETER D.,
SCHAPER WOLFGANG
Publication year - 1994
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.1994.tb36787.x
Subject(s) - erasmus+ , classics , humanities , art history , philosophy , art , the renaissance
Brief periods of ischemia not only cause a long lasting (hours to days) myocardial contractile dysfunction (stunning) but also increase the tolerance for irreversible damage during a subsequent ischemic episode, a phenomenon called ischemic preconditioning.1J Heat-shock proteins, in particular HSP-70, have been postulated in myocardial protection against irreversible damage due to i~chemia .~ It is known that in vivo as well as in vim, metabolic stressors (e.g., ischemia) and heat lead to the rapid synthesis of 70 kD heat-shock protein (HSP-70) family.3.4 However, the cellular distribution and its potential role in ischemic preconditioning have not yet been well established. Brief periods of myocardial ischemia in rabbits also cause a rapid expression of HSP-70, which is detectable at the protein level within 2 h.4 Recently, we have shown that porcine myocardium responds to ischemia and repehsion by inducing a battery of genes.5-7 In this study, we examined the expression pattern and cellular distribution of HSP-70 in a porcine model of myocardial stunning and preconditioning achieved by two cycles of 10 min of ischemia and 30 min of reperfusion followed by additional 90 and 180 min of reperfusion.