Abstract

The purpose of this research is to determine the size, detergent binding and subunit composition of the insulin receptor from rat adipocytes, rat hepatocytes, and turkey erythrocytes before and after purification. The mechanism of coupling between the insulin receptor and the (Na ion, K ion) ATPase will be studied by examination of the coupling system in normal and in fused cells, and by reconstitution of the components in artificial lipid vesicles.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Arthritis, Diabetes, Digestive and Kidney Diseases (NIADDK)
Type
Research Project (R01)
Project #
5R01AM027626-05
Application #
3151771
Study Section
Physical Biochemistry Study Section (PB)
Project Start
1981-03-01
Project End
1986-02-28
Budget Start
1985-03-01
Budget End
1986-02-28
Support Year
5
Fiscal Year
1985
Total Cost
Indirect Cost

  Institution

Name
Harvard University
Department
Type
Schools of Arts and Sciences
DUNS #
071723621
City
Cambridge
State
MA
Country
United States
Zip Code

  Publications

Chiacchia, K B (1991) Quantitation of the class I disulfides of the insulin receptor. Biochem Biophys Res Commun 176:1178-82
Mortensen, E R; Drachman, J G; Guidotti, G (1991) The alpha beta monomer of the insulin receptor has hormone-responsive tyrosine kinase activity. Biochem J 273(Pt 1):49-56
Brennan Jr, W A (1988) Developmental aspects of the rat brain insulin receptor: loss of sialic acid and fluctuation in number characterize fetal development. Endocrinology 122:2364-70
Wang, C; Brennan Jr, W A (1988) Rat skeletal muscle, liver and brain have different fetal and adult forms of the glucose transporter. Biochim Biophys Acta 946:11-8
Chiacchia, K B (1988) Reoxidation of the class I disulfides of the rat adipocyte insulin receptor is dependent upon the presence of insulin: the class I disulfide of the insulin receptor is extracellular. Biochemistry 27:4894-902
Wang, C (1987) The D-glucose transporter is tissue-specific. Skeletal muscle and adipose tissue have a unique form of glucose transporter. J Biol Chem 262:15689-95
Wang, C (1985) Insulin-stimulated glucose uptake in rat diaphragm during postnatal development: lack of correlation with the number of insulin receptors and of intracellular glucose transporters. Proc Natl Acad Sci U S A 82:3621-5
Lytton, J (1985) The catalytic subunits of the (Na+,K+)-ATPase alpha and alpha(+) isozymes are the products of different genes. Biochem Biophys Res Commun 132:764-9
Lytton, J (1985) Insulin affects the sodium affinity of the rat adipocyte (Na+,K+)-ATPase. J Biol Chem 260:10075-80