The role of cyclic AMP in the phosphorylation of proteins in human erythrocyte membranes

Charles S. Rubin; Ora M. Rosen

doi:10.1016/0006-291X(73)90857-7

The role of cyclic AMP in the phosphorylation of proteins in human erythrocyte membranes

Charles S. Rubin, Ora M. Rosen

Molecular Pharmacology

Research output: Contribution to journal › Article › peer-review

84 Scopus citations

Abstract

Three protein components of human erythrocyte membranes served as substrates for membrane-bound protein kinase. Cyclic AMP stimulated the rates of phosphorylation of two polypeptides, but the phosphorylation of the principal phosphate-acceptor was not enhanced by the cyclic nucleotide. These observations demonstrate the presence of cyclic AMP-dependent protein kinase and its homologous substrates in erythrocyte membranes and suggest that cyclic AMP could mediate alterations in the properties of membranes.

Original language	English (US)
Pages (from-to)	421-429
Number of pages	9
Journal	Biochemical and Biophysical Research Communications
Volume	50
Issue number	2
DOIs	https://doi.org/10.1016/0006-291X(73)90857-7
State	Published - Jan 23 1973

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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abstract = "Three protein components of human erythrocyte membranes served as substrates for membrane-bound protein kinase. Cyclic AMP stimulated the rates of phosphorylation of two polypeptides, but the phosphorylation of the principal phosphate-acceptor was not enhanced by the cyclic nucleotide. These observations demonstrate the presence of cyclic AMP-dependent protein kinase and its homologous substrates in erythrocyte membranes and suggest that cyclic AMP could mediate alterations in the properties of membranes.",

author = "Rubin, {Charles S.} and Rosen, {Ora M.}",

note = "Funding Information: This work was supported by Grant AM09038 from the National of Health and Grant BC-12B from the American Cancer Society. communication NO. 290 from the Joan and Lester Avnet Institute Molecular Biology. Recipient of a Damon Runyon Postdoctoral Cancer Research Fellowship. Recipient of a Career Development Award from the United States Public Health Service (5KO3 GM22345).",

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AU - Rosen, Ora M.

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PY - 1973/1/23

Y1 - 1973/1/23

N2 - Three protein components of human erythrocyte membranes served as substrates for membrane-bound protein kinase. Cyclic AMP stimulated the rates of phosphorylation of two polypeptides, but the phosphorylation of the principal phosphate-acceptor was not enhanced by the cyclic nucleotide. These observations demonstrate the presence of cyclic AMP-dependent protein kinase and its homologous substrates in erythrocyte membranes and suggest that cyclic AMP could mediate alterations in the properties of membranes.

AB - Three protein components of human erythrocyte membranes served as substrates for membrane-bound protein kinase. Cyclic AMP stimulated the rates of phosphorylation of two polypeptides, but the phosphorylation of the principal phosphate-acceptor was not enhanced by the cyclic nucleotide. These observations demonstrate the presence of cyclic AMP-dependent protein kinase and its homologous substrates in erythrocyte membranes and suggest that cyclic AMP could mediate alterations in the properties of membranes.

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The role of cyclic AMP in the phosphorylation of proteins in human erythrocyte membranes

Abstract

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