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Title: G/sub o/ protein of fat cells: role in hormonal regulation of agonist-stimulated phosphatidyl inositol breakdown

Abstract

Incubating rat fat cell membranes in the presence of (/sup 32/P)NAD/sup +/ and pertussis toxin (PT) results in the ADP-ribosylation of two peptides (M/sub r/ = 41,000 and 40,000). The 41,000-M/sub r/ peptide is the inhibitory G-protein of adenylate cyclase (G/sub i/). The 40,000-M/sub r/ peptide radiolabeled in the presence of (/sup 32/P)NAD/sup +/ and PT has been purified from rabbit heart and bovine brain, but has not been identified uniformly in membranes of fat cells. Two rabbit polyclonal antisera raised against the alpha-subunit of bovine brain G/sub o/ were used to probe the nature of the 40,000-M/sub r/ peptide in rat fat cell membranes that had been separated by gel electrophoresis in the presence of sodium dodecyl sulfate and transferred electrophoretically to nitrocellulose. Both antisera specific for the alpha-subunit of G/sub o/ recognized the M/sub r/ = 40,000 peptide of fat cells that is ADP-ribosylated in the presence of PT. PT treatment of rat fat cells blocks epinephrine-stimulated inositol 1,4,5 trisphosphate (IP/sub 3/) generation. The inhibition of IP/sub 3/ generation by PT suggests a role for either G/sub i/ or G/sub o/ in receptor-mediated phosphatidyl inositol breakdown in the rat fat cell.

Authors:
; ;
Publication Date:
Research Org.:
State Univ. of New York, Stony Brook
OSTI Identifier:
5326873
Report Number(s):
CONF-8606151-
Journal ID: CODEN: FEPRA; TRN: 86-031389
Resource Type:
Conference
Journal Name:
Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)
Additional Journal Information:
Journal Volume: 45:6; Conference: 76. annual meeting of the Federation of American Society for Experimental Biology, Washington, DC, USA, 8 Jun 1986
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; FAT CELLS; CHEMICAL COMPOSITION; INOSITOL; METABOLISM; PEPTIDES; LABELLING; BRAIN; CATTLE; CELL MEMBRANES; ELECTROPHORESIS; NAD; PHOSPHORUS 32; RATS; TOXINS; TRACER TECHNIQUES; ANIMAL CELLS; ANIMALS; ANTIGENS; BETA DECAY RADIOISOTOPES; BETA-MINUS DECAY RADIOISOTOPES; BODY; CARBOHYDRATES; CELL CONSTITUENTS; CENTRAL NERVOUS SYSTEM; COENZYMES; CONNECTIVE TISSUE CELLS; DAYS LIVING RADIOISOTOPES; DOMESTIC ANIMALS; INOSITOLS; ISOTOPE APPLICATIONS; ISOTOPES; LIGHT NUCLEI; MAMMALS; MATERIALS; MEMBRANES; MONOSACCHARIDES; NERVOUS SYSTEM; NUCLEI; NUCLEOTIDES; ODD-ODD NUCLEI; ORGANIC COMPOUNDS; ORGANS; PHOSPHORUS ISOTOPES; PROTEINS; RADIOISOTOPES; RODENTS; RUMINANTS; SACCHARIDES; SOMATIC CELLS; TOXIC MATERIALS; VERTEBRATES; 550201* - Biochemistry- Tracer Techniques

Citation Formats

Rapiejko, P J, Northup, J K, and Malbon, C C. G/sub o/ protein of fat cells: role in hormonal regulation of agonist-stimulated phosphatidyl inositol breakdown. United States: N. p., 1986. Web.
Rapiejko, P J, Northup, J K, & Malbon, C C. G/sub o/ protein of fat cells: role in hormonal regulation of agonist-stimulated phosphatidyl inositol breakdown. United States.
Rapiejko, P J, Northup, J K, and Malbon, C C. 1986. "G/sub o/ protein of fat cells: role in hormonal regulation of agonist-stimulated phosphatidyl inositol breakdown". United States.
@article{osti_5326873,
title = {G/sub o/ protein of fat cells: role in hormonal regulation of agonist-stimulated phosphatidyl inositol breakdown},
author = {Rapiejko, P J and Northup, J K and Malbon, C C},
abstractNote = {Incubating rat fat cell membranes in the presence of (/sup 32/P)NAD/sup +/ and pertussis toxin (PT) results in the ADP-ribosylation of two peptides (M/sub r/ = 41,000 and 40,000). The 41,000-M/sub r/ peptide is the inhibitory G-protein of adenylate cyclase (G/sub i/). The 40,000-M/sub r/ peptide radiolabeled in the presence of (/sup 32/P)NAD/sup +/ and PT has been purified from rabbit heart and bovine brain, but has not been identified uniformly in membranes of fat cells. Two rabbit polyclonal antisera raised against the alpha-subunit of bovine brain G/sub o/ were used to probe the nature of the 40,000-M/sub r/ peptide in rat fat cell membranes that had been separated by gel electrophoresis in the presence of sodium dodecyl sulfate and transferred electrophoretically to nitrocellulose. Both antisera specific for the alpha-subunit of G/sub o/ recognized the M/sub r/ = 40,000 peptide of fat cells that is ADP-ribosylated in the presence of PT. PT treatment of rat fat cells blocks epinephrine-stimulated inositol 1,4,5 trisphosphate (IP/sub 3/) generation. The inhibition of IP/sub 3/ generation by PT suggests a role for either G/sub i/ or G/sub o/ in receptor-mediated phosphatidyl inositol breakdown in the rat fat cell.},
doi = {},
url = {https://www.osti.gov/biblio/5326873}, journal = {Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)},
number = ,
volume = 45:6,
place = {United States},
year = {Thu May 01 00:00:00 EDT 1986},
month = {Thu May 01 00:00:00 EDT 1986}
}

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