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In vivo modulation of N-myristoyltransferase activity by orthovanadate

  • Martin J. King
  • Subbiah Pugazhenthi
  • Ramji L. Khandelwal
  • Rajendra K. Sharma
Chapter
Part of the Developments in Molecular and Cellular Biochemistry book series (DMCB, volume 16)

Abstract

N-Myristoytransferase (NMT) catalyses the transfer of myristate from myristoyl-CoA to the NH2-terminal glycine residue of several proteins and are important in signal transduction. STZ-induced diabetes (an animal model for insulin-dependent diabetes mellitus, IDDM) resulted in a 2-fold increase in rat liver NMT activity as compared with control animals. In obese Zucker (fa/fa) rats (an animal model for non-insulin dependent diabetes mellitus, NIDDM) there was a ~4.7-fold lower liver particulate NMT activity as compared with the control lean rat livers. Administration of sodium orthovanadate to the diabetic rats normalised liver NMT activity. These results would indicate that the rat liver particulate N-myristoyltransferase activity appears to be inversely proportional to the level of plasma insulin, implicating insulin in the control of N-myristoylation.

Key words

sodium orthovanadate diabetes N-myristoyltransferase Liver membrane-associated vanadate obese Zucker rat 

Abbreviations

NMT

N-myristoyl-CoA:protein N-myristoyltransferase

IDDM

insulin-dependent diabetes mellitus

NIDDM

non-insulin-dependent diabetes mellitus

NIP71

71 kDa N-myristoyltransferase inhibitor protein

NAF45

45 kDa N-myristoyltransferase activating factor

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Copyright information

© Kluwer Academic Publishers 1995

Authors and Affiliations

  • Martin J. King
    • 1
  • Subbiah Pugazhenthi
    • 2
  • Ramji L. Khandelwal
    • 2
  • Rajendra K. Sharma
    • 3
  1. 1.Saskatoon Cancer CentreSaskatoonCanada
  2. 2.Department of BiochemistryUniversity of SaskatchewanSaskatoonCanada
  3. 3.Department of Pathology and Saskatoon Cancer Centre, Royal University HospitalUniversity of SaskatchewanSaskatoonCanada

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