The aims of the proposd work are to investigate the roles of covalent enzyme phosphorylation of hepatic lipogenesis and the activity of the key rate-limiting enzyme of fatty acid synthesis, acetyl-CoA carboxylase. Particular emphasis is being placed on the characterization of site-specific phosphorylation changes in the enzyme indued by hormones in the intact cell and the characterization in vitro of the major site-specific protein kinases and phosphatases responsible for these alterations. In addition, the regulation of hepatic lipogenesis by insulin is being employed as a model system for the further elucidation of the molecular mechanism of insulin action..

Agency
National Institute of Health (NIH)
Institute
National Institute of Arthritis, Diabetes, Digestive and Kidney Diseases (NIADDK)
Type
Research Project (R01)
Project #
7R01AM035712-01
Application #
3154151
Study Section
Metabolism Study Section (MET)
Project Start
1985-01-01
Project End
1988-12-31
Budget Start
1985-01-01
Budget End
1985-12-31
Support Year
1
Fiscal Year
1985
Total Cost
Indirect Cost
Name
Dartmouth College
Department
Type
Schools of Medicine
DUNS #
041027822
City
Hanover
State
NH
Country
United States
Zip Code
Glynn, B P; Colliton, J W; McDermott, J M et al. (1986) Phorbol esters, but not insulin, promote depletion of cytosolic protein kinase C in rat adipocytes. Biochem Biophys Res Commun 135:1119-25
Witters, L A; McDermott, J M (1986) Regulation of acetyl-CoA carboxylase by ADP-ribosylation. Biochemistry 25:7216-20
Blackshear, P J; Wen, L; Nemenoff, R A et al. (1986) Growth factor activation of protein kinase C-dependent and -independent pathways of protein phosphorylation in fibroblasts: relevance to activation of protein kinase C in neuronal tissues. Prog Brain Res 69:183-95
Glynn, B; Colliton, J; McDermott, J et al. (1985) Assay of protein kinase C with an N-bromosuccinimide-cleavage fragment of histone H1. Biochem J 231:489-92