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PMID: 3199814 Published · ppublish English Journal Article

Characterization of p29, an estrogen-receptor associated tumor marker.

Journal of steroid biochemistry ·Vol. 31 ·No. 5 ·1988-11-00 ·Pages 745-50

Coffer AI, King RJ

Abstract

Monoclonal antibody D5, raised against cytosolic human estrogen receptor (ER) reacts with p29, a receptor-associated cytoplasmic serine phosphoprotein which does not bind steroid, While p29 selectively binds GTP and to a lesser extent ATP, in vitro GTP binding does not result in p29 phosphorylation. Under ER activating conditions, p29 associates with cytosolic ER; GTP, ATP and sodium molybdate block formation of immunoprecipitable p29-ER complexes. Nucleotide binding data suggest a role for p29 in the estrogen response machinery, possibly at the level of phosphate or nucleotide metabolism.

MeSH Terms
Adenosine Triphosphate/metabolism Biomarkers, Tumor/analysis Breast Neoplasms/analysis Cell Line Female Guanosine Triphosphate/metabolism Heat-Shock Proteins Humans Myometrium/analysis Phosphoproteins/analysis Phosphorylation Receptors, Estrogen/metabolism
Chemicals
Biomarkers, Tumor Heat-Shock Proteins Phosphoproteins Receptors, Estrogen Guanosine Triphosphate Adenosine Triphosphate
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Coffer A I
Department of Hormone Biochemistry, Imperial Cancer Research Fund, London, England.
King R J
Article Info
Journal
Journal of steroid biochemistry
Abbr.
J Steroid Biochem
ISSN
0022-4731
Published
1988-11-00
Pages
745-50
Language
English
Region
England
NLM ID
0260125
Subset
IM
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