Characterization of a plasma membrane-resident albumin-binding protein associated with the proliferation of estrogen-target, serum-sensitive cells.
Identifieur interne : 000208 ( Ncbi/Checkpoint ); précédent : 000207; suivant : 000209Characterization of a plasma membrane-resident albumin-binding protein associated with the proliferation of estrogen-target, serum-sensitive cells.
Auteurs : Charles E. Powell [États-Unis] ; Ana M. Soto ; Cheryl L. Michaelson ; Fantahun Diba ; Françoise Mounier ; Pierre J. Verroust ; Carlos SonnenscheinSource :
- Steroids [ 0039-128X ] ; 2003.
Descripteurs français
- KwdFr :
- Cartographie d'interactions entre protéines, Division cellulaire (), Division cellulaire (physiologie), Fragments peptidiques (pharmacologie), Humains, Immunohistochimie, Liaison aux protéines, Lignée cellulaire tumorale, Oestrogènes (pharmacologie), Protéines membranaires (analyse), Protéines membranaires (métabolisme), Protéines membranaires (physiologie), Récepteurs des oestrogènes (analyse), Sérumalbumine (métabolisme), Sérumalbumine (pharmacologie), Technique de Western.
- MESH :
- analyse : Protéines membranaires, Récepteurs des oestrogènes.
- métabolisme : Protéines membranaires, Sérumalbumine.
- pharmacologie : Fragments peptidiques, Oestrogènes, Sérumalbumine.
- physiologie : Division cellulaire, Protéines membranaires.
- Cartographie d'interactions entre protéines, Division cellulaire, Humains, Immunohistochimie, Liaison aux protéines, Lignée cellulaire tumorale, Technique de Western.
English descriptors
- KwdEn :
- Blotting, Western, Cell Division (drug effects), Cell Division (physiology), Cell Line, Tumor, Estrogens (pharmacology), Humans, Immunohistochemistry, Membrane Proteins (analysis), Membrane Proteins (metabolism), Membrane Proteins (physiology), Peptide Fragments (pharmacology), Protein Binding, Protein Interaction Mapping, Receptors, Estrogen (analysis), Serum Albumin (metabolism), Serum Albumin (pharmacology).
- MESH :
- chemical , analysis : Membrane Proteins, Receptors, Estrogen.
- chemical , metabolism : Membrane Proteins, Serum Albumin.
- chemical , pharmacology : Estrogens, Peptide Fragments, Serum Albumin.
- drug effects : Cell Division.
- physiology : Cell Division, Membrane Proteins.
- Blotting, Western, Cell Line, Tumor, Humans, Immunohistochemistry, Protein Binding, Protein Interaction Mapping.
Abstract
Estrogens control the proliferation of their target cells through a receptor-mediated pathway. Recently presented evidence suggests that estradiol cancels the proliferative inhibition exerted by human albumin (HA) and recombinant human albumin (rHA) on estrogen-target serum-sensitive cells (indirect-negative hypothesis). We postulate that this mechanism requires the presence of a plasma membrane estrogen receptor (mER) and a plasma membrane albumin-binding protein (mABP). Direct evidence confirming the presence of mERalpha in MCF7 cells has recently been presented. Herein, we now show that Western blot analysis of purified T47D membrane proteins with the C542 ERalpha specific monoclonal antibody also revealed specific, multiple M(r) mERs (67, 110, and 130k M(r)). In addition, Western blot analysis with an ABP antiserum revealed a potential 60k M(r) ABP in both MCF7 and T47D plasma membrane extracts. No such evidence was observed in similar extracts from ER-negative, serum-insensitive MDA-MB231 cells. Ligand blot analysis of similar plasma membrane extracts with bovine serum albumin confirmed the presence of a 60k M(r) ABP in MCF7 and T47D cells; again, no such evidence was observed in comparable extracts from MDA-MB231 cells. Fluorescence and confocal microscopy of MCF7 cells fixed in 2.0% paraformaldehyde/0.1% glutaraldehyde identified specific membrane ABP antigenic sites by immunocytochemistry. Serum-insensitive MDA-MB231 cells fixed and labeled similarly did not exhibit this mABP. These results suggest that the proposed mABP is expressed only in serum-sensitive estrogen-target cells and is not expressed in cells insensitive to the proliferative inhibition of HA and rHA. Also, the present data suggest that the proposed mABP may be the recognition mechanism by which both HA and rHA inhibit MCF7 and T47D cell proliferation.
DOI: 10.1016/s0039-128x(03)00047-3
PubMed: 12906933
Affiliations:
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pubmed:12906933Le document en format XML
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<author><name sortKey="Powell, Charles E" sort="Powell, Charles E" uniqKey="Powell C" first="Charles E" last="Powell">Charles E. Powell</name>
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<term>Cell Division (physiology)</term>
<term>Cell Line, Tumor</term>
<term>Estrogens (pharmacology)</term>
<term>Humans</term>
<term>Immunohistochemistry</term>
<term>Membrane Proteins (analysis)</term>
<term>Membrane Proteins (metabolism)</term>
<term>Membrane Proteins (physiology)</term>
<term>Peptide Fragments (pharmacology)</term>
<term>Protein Binding</term>
<term>Protein Interaction Mapping</term>
<term>Receptors, Estrogen (analysis)</term>
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<term>Serum Albumin (pharmacology)</term>
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<term>Fragments peptidiques (pharmacologie)</term>
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<term>Immunohistochimie</term>
<term>Liaison aux protéines</term>
<term>Lignée cellulaire tumorale</term>
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<front><div type="abstract" xml:lang="en">Estrogens control the proliferation of their target cells through a receptor-mediated pathway. Recently presented evidence suggests that estradiol cancels the proliferative inhibition exerted by human albumin (HA) and recombinant human albumin (rHA) on estrogen-target serum-sensitive cells (indirect-negative hypothesis). We postulate that this mechanism requires the presence of a plasma membrane estrogen receptor (mER) and a plasma membrane albumin-binding protein (mABP). Direct evidence confirming the presence of mERalpha in MCF7 cells has recently been presented. Herein, we now show that Western blot analysis of purified T47D membrane proteins with the C542 ERalpha specific monoclonal antibody also revealed specific, multiple M(r) mERs (67, 110, and 130k M(r)). In addition, Western blot analysis with an ABP antiserum revealed a potential 60k M(r) ABP in both MCF7 and T47D plasma membrane extracts. No such evidence was observed in similar extracts from ER-negative, serum-insensitive MDA-MB231 cells. Ligand blot analysis of similar plasma membrane extracts with bovine serum albumin confirmed the presence of a 60k M(r) ABP in MCF7 and T47D cells; again, no such evidence was observed in comparable extracts from MDA-MB231 cells. Fluorescence and confocal microscopy of MCF7 cells fixed in 2.0% paraformaldehyde/0.1% glutaraldehyde identified specific membrane ABP antigenic sites by immunocytochemistry. Serum-insensitive MDA-MB231 cells fixed and labeled similarly did not exhibit this mABP. These results suggest that the proposed mABP is expressed only in serum-sensitive estrogen-target cells and is not expressed in cells insensitive to the proliferative inhibition of HA and rHA. Also, the present data suggest that the proposed mABP may be the recognition mechanism by which both HA and rHA inhibit MCF7 and T47D cell proliferation.</div>
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<name sortKey="Michaelson, Cheryl L" sort="Michaelson, Cheryl L" uniqKey="Michaelson C" first="Cheryl L" last="Michaelson">Cheryl L. Michaelson</name>
<name sortKey="Mounier, Francoise" sort="Mounier, Francoise" uniqKey="Mounier F" first="Françoise" last="Mounier">Françoise Mounier</name>
<name sortKey="Sonnenschein, Carlos" sort="Sonnenschein, Carlos" uniqKey="Sonnenschein C" first="Carlos" last="Sonnenschein">Carlos Sonnenschein</name>
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<country name="États-Unis"><region name="Massachusetts"><name sortKey="Powell, Charles E" sort="Powell, Charles E" uniqKey="Powell C" first="Charles E" last="Powell">Charles E. Powell</name>
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