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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1991-11-13
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pubmed:abstractText |
Synthetic peptides corresponding to cDNA-deduced amino acid sequences unique to the human and mouse retinoic acid receptor gamma 1 (hRAR-gamma 1 and mRAR-gamma 1, respectively) were used to generate anti-RAR-gamma 1 antibodies. Four mAbs were selected, which were directed against peptides found in region A1 (Ab1 gamma (A1)), region F (Ab2 gamma (mF) and Ab4 gamma (hF)) and region D2 (Ab5 gamma (D2)). These antibodies specifically immunoprecipitated and recognized by Western blotting RAR-gamma 1 proteins in COS-1 cells transfected with expression vectors containing the RAR-gamma 1 cDNAs. They all reacted with both human and mouse RAR-gamma 1 proteins, except Ab4 gamma (hF) that was specific for hRAR-gamma 1. Rabbit polyclonal antibodies, directed against a peptide from the mRAR-gamma 1 F region were also obtained (RP gamma (mF)) and found to be specific for mouse RAR-gamma 1 protein. Furthermore, in gel retardation/shift assays the antibodies specifically retarded the migration of complexes obtained with a RA response element (RARE). Antibodies raised against regions D2 and F also recognized the RAR-gamma 2 isoform which differs from RAR-gamma 1 only in the A region. On the other hand, antibodies directed against the A1 region of RAR-gamma 1 (Ab1 gamma (A1)) only reacted with the RAR-gamma 1 protein. The antibodies characterized here allowed us to detect the presence of mRAR-gamma 1 and gamma 2 isoforms in mouse embryos and F9 embryonal carcinoma cells nuclear extracts. They were also used to demonstrate that the mRAR-gamma 1 protein can be phosphorylated and that the phosphorylation occurs mainly in the NH2-terminal A/B region.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1655807-1671708,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1655807-1846598,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/1655807-942051
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0021-9525
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
115
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
535-45
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:1655807-Alkaline Phosphatase,
pubmed-meshheading:1655807-Amino Acid Sequence,
pubmed-meshheading:1655807-Animals,
pubmed-meshheading:1655807-Antibodies, Monoclonal,
pubmed-meshheading:1655807-Blotting, Western,
pubmed-meshheading:1655807-Carrier Proteins,
pubmed-meshheading:1655807-Cloning, Molecular,
pubmed-meshheading:1655807-Embryo, Mammalian,
pubmed-meshheading:1655807-Humans,
pubmed-meshheading:1655807-Mice,
pubmed-meshheading:1655807-Molecular Sequence Data,
pubmed-meshheading:1655807-Peptide Fragments,
pubmed-meshheading:1655807-Phosphorylation,
pubmed-meshheading:1655807-Protein Processing, Post-Translational,
pubmed-meshheading:1655807-Rabbits,
pubmed-meshheading:1655807-Receptors, Retinoic Acid,
pubmed-meshheading:1655807-Transfection,
pubmed-meshheading:1655807-Tretinoin,
pubmed-meshheading:1655807-Tumor Cells, Cultured
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pubmed:year |
1991
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pubmed:articleTitle |
Retinoic acid receptor gamma: specific immunodetection and phosphorylation.
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pubmed:affiliation |
Laboratoire de Génétique Moléculaire des Eucaryotes du Centre National pour la Recherche Scientifique, l'Institut National de la Santé et de la Recherche Medicale, Faculté de Médecine, Strasbourg, France.
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