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

Raju V S Rajala, Rakesh Kakkar, Rani Kanthan, Jasim M. Radhi, Xintao Wang, Rui Wang, Raju S S Datla, Rajendra K. Sharma

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Pages (from-to)509-519
Number of pages11
JournalJournal of Cellular Biochemistry
Volume86
Issue number3
DOIs
StatePublished - 2002
Externally publishedYes

Fingerprint

Reperfusion
Rats
Ischemia
Translational Protein Modification
leucylleucine
Calpain
Myristic Acid
glycylpeptide N-tetradecanoyltransferase
Glycine
Cytoplasm
Perfusion
Western Blotting
Peptides
Antibodies
Wounds and Injuries
Proteins

Keywords

  • c-Src
  • Calpain
  • Ischemic heart
  • N-myristoyltransferase
  • Tyrosine kinase

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology

Cite this

Altered expression and localization of N-myristoyltransferase in experimentally induced rat model of ischemia-reperfusion. / Rajala, Raju V S; Kakkar, Rakesh; Kanthan, Rani; Radhi, Jasim M.; Wang, Xintao; Wang, Rui; Datla, Raju S S; Sharma, Rajendra K.

In: Journal of Cellular Biochemistry, Vol. 86, No. 3, 2002, p. 509-519.

Research output: Contribution to journalArticle

Rajala, Raju V S ; Kakkar, Rakesh ; Kanthan, Rani ; Radhi, Jasim M. ; Wang, Xintao ; Wang, Rui ; Datla, Raju S S ; Sharma, Rajendra K. / Altered expression and localization of N-myristoyltransferase in experimentally induced rat model of ischemia-reperfusion. In: Journal of Cellular Biochemistry. 2002 ; Vol. 86, No. 3. pp. 509-519.
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AU - Kanthan, Rani

AU - Radhi, Jasim M.

AU - Wang, Xintao

AU - Wang, Rui

AU - Datla, Raju S S

AU - Sharma, Rajendra K.

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AB - 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.

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