The major objective of this research is to determine how renal glycogen synthase is regulated and to apply any new insights gained to the regulation of glycogen synthase in other mammalian tissues. While much is known about the regulation of glycogen synthase in tissues with relatively high concentrations of glycogen, little is known about the regulation of glycogen synthase in tissues which contain relatively low concentrations of glycogen. Of particular interest is the kidney since there is a large difference in the synthesis of glycogen in the cortex and medulla even though glycogen levels are low in both portions of the kidney. The specific goals of this project are: 1) To purify and characterize renal glycogen synthase kinases and to establish the physiological significance and regulation of these enzymes in the medulla and cortex. Special emphasis will be placed on the role of cyclic AMP-independent glycogen synthase kinases as well as cyclic AMP-dependent protein kinase. 2) To purify and characterize renal glycogen synthase I and D and to establish how they are regulated in the cortex and medulla. 3) To purify and characterize renal glycogen synthase phosphatases and to establish their physiological significance and regulation in the cortex and medulla.

Agency
National Institute of Health (NIH)
Institute
National Institute of Arthritis, Diabetes, Digestive and Kidney Diseases (NIADDK)
Type
Research Project (R01)
Project #
5R01AM014723-14
Application #
3150926
Study Section
Physiological Chemistry Study Section (PC)
Project Start
1977-05-01
Project End
1988-04-30
Budget Start
1985-05-01
Budget End
1986-04-30
Support Year
14
Fiscal Year
1985
Total Cost
Indirect Cost
Name
University of Toledo
Department
Type
Schools of Medicine
DUNS #
807418939
City
Toledo
State
OH
Country
United States
Zip Code
43614
Hegazy, M G; Schlender, K K; Reimann, E M et al. (1988) Modulation of glycogen synthase kinase activity of skeletal and smooth muscle casein kinase I by spermine. Biochem Biophys Res Commun 156:653-9
Schlender, K K; Hegazy, M G; Thysseril, T J (1987) Dephosphorylation of cardiac myofibril C-protein by protein phosphatase 1 and protein phosphatase 2A. Biochim Biophys Acta 928:312-9
Jakes, S; Mellgren, R L; Schlender, K K (1986) Isolation and characterization of an inhibitor-sensitive and a polycation-stimulated protein phosphatase from rat liver nuclei. Biochim Biophys Acta 888:135-42
Schlender, K K; Wilson, S E; Mellgren, R L (1986) Purification and characterization of the polycation-stimulated protein phosphatase catalytic subunit from porcine renal cortex. Biochim Biophys Acta 872:1-10
Schlender, K K; Wilson, S E; Mellgren, R L (1986) Catalytic subunit of the polycation-stimulated protein phosphatase. Effect of proteolysis on polycation stimulation. Biochim Biophys Acta 889:200-7