Elevated N-myristoyl transferase activity is reversed by sodium orthovanadate in streptozotocin-induced diabetic rat

N-Myristoyl transferase (NMT) is the enzyme that covalently modifies several proteins important in signal transduction. Streptozotocin-induced diabetes resulted in a 2-fold increase in NMT activity from rat liver as compared to control animals. Administration of sodium orthovanadate to the diabetic...

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Bibliographic Details
Published in:	Biochimica et biophysica acta Vol. 1165; no. 3; p. 259
Main Authors:	King, M J, Pugazhenthi, S, Khandelwal, R L, Sharma, R K
Format:	Journal Article
Language:	English
Published:	Netherlands 10-01-1993
Subjects:	Acyltransferases - metabolism Animals Blood Glucose - analysis Body Weight Diabetes Mellitus, Experimental - enzymology Diabetes Mellitus, Type 1 - metabolism Enzyme Activation - drug effects Insulin - blood Liver - enzymology Male Rats Rats, Sprague-Dawley Vanadates - pharmacology
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Summary:	N-Myristoyl transferase (NMT) is the enzyme that covalently modifies several proteins important in signal transduction. Streptozotocin-induced diabetes resulted in a 2-fold increase in NMT activity from rat liver as compared to control animals. Administration of sodium orthovanadate to the diabetic rats reduced the activity of the NMT to 75-120% of the control values. Elevated NMT activity was observed with both cAMP-dependent protein kinase-derived and pp60src-derived peptide substrates. No significant change in the apparent Km was observed with the cAMP-dependent protein kinase-derived peptide substrate. Unlike in rat brain, in all conditions highest NMT activity was observed in the particulate fraction of rat liver.
ISSN:	0006-3002
DOI:	10.1016/0005-2760(93)90134-U