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 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.
King
M J
MJ
Department of Pathology, University of Saskatchewan, Saskatoon, Canada.
Pugazhenthi
S
S
Khandelwal
R L
RL
Sharma
R K
RK
D000217:Acyltransferases / Q000378:metabolism*; D000818:Animals; D001786:Blood Glucose / Q000032:analysis; D001835:Body Weight; D003921:Diabetes Mellitus, Experimental / Q000201:enzymology*; D003922:Diabetes Mellitus, Type 1 / Q000378:metabolism; D004789:Enzyme Activation / Q000187:drug effects; D007328:Insulin / Q000097:blood; D008099:Liver / Q000201:enzymology*; D008297:Male; D051381:Rats; D017207:Rats, Sprague-Dawley; D014638:Vanadates / Q000494:pharmacology*
D001786:Blood Glucose; D007328:Insulin; D014638:Vanadates; D000217:Acyltransferases; C050480:glycylpeptide N-tetradecanoyltransferase