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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
8
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pubmed:dateCreated |
1995-1-19
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pubmed:databankReference |
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pubmed:abstractText |
Anti-Müllerian hormone, also called Müllerian-inhibiting substance or factor, is a glycoprotein dimer belonging to the transforming growth factor-beta superfamily and synthesized by immature Sertoli cells and postnatal granulosa cells. Anti-Müllerian hormone plays a key role in sex differentiation by inducing the regression of Müllerian ducts in the male fetus. It is also responsible for the stunting and masculinization of fetal ovaries in bovine freemartin fetuses and may be involved in the control of follicular maturation in the postnatal ovary. Using a degenerate probe for a consensus region of the transforming growth factor-beta receptor superfamily to screen a complementary DNA library from rabbit fetal ovaries, we cloned a complementary DNA coding for a transmembrane serine/threonine kinase, which is expressed around the fetal Müllerian duct, in fetal and adult granulosa cells, and in immature Sertoli cells. Two transcripts, generated by alternative splicing of an exon coding for an N-terminal 61-amino acid domain, are strongly expressed in anti-Müllerian hormone target organs and Sertoli cells. The longer, 569-amino acid, isoform binds anti-Müllerian hormone when transiently expressed in COS cells and is believed to encode its functional receptor.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Anti-Mullerian Hormone,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Growth Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Peptide,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Transforming Growth...,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Testicular Hormones,
http://linkedlifedata.com/resource/pubmed/chemical/anti-Mullerian hormone receptor
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0888-8809
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1006-20
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:7997230-Amino Acid Sequence,
pubmed-meshheading:7997230-Animals,
pubmed-meshheading:7997230-Anti-Mullerian Hormone,
pubmed-meshheading:7997230-Base Sequence,
pubmed-meshheading:7997230-CHO Cells,
pubmed-meshheading:7997230-Cercopithecus aethiops,
pubmed-meshheading:7997230-Cloning, Molecular,
pubmed-meshheading:7997230-Cricetinae,
pubmed-meshheading:7997230-DNA, Complementary,
pubmed-meshheading:7997230-Female,
pubmed-meshheading:7997230-Fibroblasts,
pubmed-meshheading:7997230-Glycoproteins,
pubmed-meshheading:7997230-Growth Inhibitors,
pubmed-meshheading:7997230-Humans,
pubmed-meshheading:7997230-Male,
pubmed-meshheading:7997230-Mice,
pubmed-meshheading:7997230-Molecular Sequence Data,
pubmed-meshheading:7997230-Multigene Family,
pubmed-meshheading:7997230-Protein-Serine-Threonine Kinases,
pubmed-meshheading:7997230-RNA, Messenger,
pubmed-meshheading:7997230-RNA Splicing,
pubmed-meshheading:7997230-Rabbits,
pubmed-meshheading:7997230-Rats,
pubmed-meshheading:7997230-Rats, Wistar,
pubmed-meshheading:7997230-Receptors, Peptide,
pubmed-meshheading:7997230-Receptors, Transforming Growth Factor beta,
pubmed-meshheading:7997230-Recombinant Fusion Proteins,
pubmed-meshheading:7997230-Sequence Alignment,
pubmed-meshheading:7997230-Sequence Homology, Amino Acid,
pubmed-meshheading:7997230-Testicular Hormones,
pubmed-meshheading:7997230-Tumor Cells, Cultured
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pubmed:year |
1994
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pubmed:articleTitle |
Cloning, expression, and alternative splicing of the receptor for anti-Müllerian hormone.
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pubmed:affiliation |
Unité de Recherches sur l'Endocrinologie du Développement, (INSERM), Département de Biologie, Ecole Normale Supérieure, Montrouge, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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