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PMID: 179086 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Binding of insulin to isolated nuclei.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 73 ·No. 5 ·1976-05-00 ·Pages 1427-31

Goldfine ID, Smith GJ

Abstract

Specific binding sites for 125I-labeled insulin were detected in purified nuclei isolated from rat liver. Binding was rapid, reversible and directly proportional to the number of nuclei employed. Unlabeled native insulin, at concentrations as low as 1ng/ml, significantly inhibited the binding of labeled hormone, whereas unlabeled proinsulin and desoctapeptide insulin were less potent. In contrast, glucagon, thyrotropin, growth hormone (somatotropin), and prolactin were without effect. Under identical incubation conditions, 125I-labeled glucagon bound to liver plasma membranes 5- to 10-fold more strongly than did insulin; in contrast glucoagon did not bind to liver nuclei. These studies demonstrate the presence of specific binding sites for insulin in purified nuclei isolated from rat liver. In addition, they suggest that the nucleus may be an intracellular site of insulin action.

MeSH Terms
Animals Cell Membrane/metabolism Cell Nucleus/metabolism Female Glucagon/metabolism Insulin/metabolism Kinetics Liver/ultrastructure Rats Receptors, Cell Surface Triiodothyronine/metabolism
Chemicals
Insulin Receptors, Cell Surface Triiodothyronine Glucagon
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Goldfine I D
Smith G J
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37 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.73.5.1427
Published
1976-05-00
Pages
1427-31
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC430309
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.73.5.1427 PMC Full Text View journal details
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