Altered expression and localization of N-myristoyltransferase in experimentally induced rat model of ischemia-reperfusion

N-myristoyltransferase (NMT) catalyzes the attachment of myristate onto the amino-terminal glycine residue of select polypeptides. In the present study, we investigated the expression and activity of NMT in rat heart after ischemia and reperfusion. Western blot analysis of rat heart samples indicated a prominent immunoreactive band of 66 kDa probed with human NMT antibody. Both the expression and activity of NMT were increased by ischemia-reperfusion. Immunohistochemical studies showed cytosolic localization of NMT in normal rat heart and predominant nuclear localization after ischemia followed by reperfusion. The pre-ischemic perfusion and post-ischemic reperfusion of hearts with a cell-permeable calpain inhibitor (N-Ac-Leu-Leu-methioninal) suppressed the increase in calpain expression and reversed the localization of NMT from nucleus to cytoplasm. This is the first study demonstrating the expression and alteration of NMT localization in cardiac ischemia and pertaining to a possible role of co-translational modification of proteins in cardiac functions and injury.