Associate Provost for Research Boston University Medical Campus
NIDDK - National Institute of Diabetes & Digestive & Kidney Diseases	Research Resources

Abstract

Abstract: The former specific aims were: 1) To test the hypothesis that the increase in malonyl-CoA caused by an excess of glucose is related to cytosolic citrate. 2) To explore the possibility that other kinases interact with AMPK in regulating ACC activity and fatty acid oxidation in muscle. 3) To extend preliminary observations suggesting that malonyl-CoA decarboxylase is regulated by phosphorylation and that its activity is increased in muscle contraction. The subcellular distribution of MCD and whether its activity is regulated by AMPK or other kinases activated by muscle contraction will be assessed. 4) To determine if the high concentration of malonyl-CoA that has been found in muscle mitochondria is due to transport from the cytosol or de novo synthesis. 5) To evaluate whether alterations in one or more of the mechanisms we have defined can explain elevated levels of malonyl-CoA in muscle in situations for which no definitive explanation currently exists such as the Dahl-salt-sensitive rat. The investigators have responded to the reviewer's

Thesaurus Terms:
bioenergetics, malonyl coA, muscle metabolism, obesity
acetyl coA carboxylase, adenosine triphosphate, biological signal transduction, citrate, enzyme activity, enzyme substrate, exercise, fatty acid metabolism, isoproterenol, muscle cell, muscle contraction, muscle pharmacology, protein kinase A, striated muscle
laboratory rat

Institution:	BOSTON MEDICAL CENTER
	ONE BOSTON MEDICAL CENTER PLACE
	BOSTON, MA 02118
Fiscal Year:	2005
Department:
Project Start:	01-JUN-1979
Project End:	15-FEB-2006
ICD:	NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES
IRG:	MET