Source:http://linkedlifedata.com/resource/pubmed/id/12887271
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2003-7-30
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pubmed:abstractText |
The role of follistatin as an activin-binding protein has dominated the study of this molecule for the last 10 years. However, there is emerging evidence that follistatin has a role in modulating the biology of other members of the transforming growth factor beta (TGF-beta) superfamily. This review summarizes the current concepts encompassing follistatin biochemistry as well as molecules with which it is functionally associated. Moreover, the importance of the two follistatin isoforms (follistatin-288 and follistatin-315) is discussed with particular emphasis on the regulation of the ovary. In addition to activin, this review discusses the functions of other members of the TGF-beta superfamily, for example growth differentiation factor 9 (GDF-9), bone morphogenetic protein 15 (BMP-15), BMP-6, BMP-4 and BMP-7, in the ovary, and the potential interactions between follistatin and these growth factors. The complex network of TGF-beta superfamily growth factor members involved in the modulation of ovarian function and the interactions of follistatin with these proteins is highlighted.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Activins,
http://linkedlifedata.com/resource/pubmed/chemical/Follistatin,
http://linkedlifedata.com/resource/pubmed/chemical/Inhibins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms,
http://linkedlifedata.com/resource/pubmed/chemical/Transforming Growth Factor beta
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1470-1626
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
126
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
133-48
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12887271-Activins,
pubmed-meshheading:12887271-Female,
pubmed-meshheading:12887271-Follistatin,
pubmed-meshheading:12887271-Homeostasis,
pubmed-meshheading:12887271-Humans,
pubmed-meshheading:12887271-Inhibins,
pubmed-meshheading:12887271-Ovary,
pubmed-meshheading:12887271-Protein Binding,
pubmed-meshheading:12887271-Protein Isoforms,
pubmed-meshheading:12887271-Signal Transduction,
pubmed-meshheading:12887271-Transforming Growth Factor beta
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pubmed:year |
2003
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pubmed:articleTitle |
Regulation of ovarian function by the TGF-beta superfamily and follistatin.
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pubmed:affiliation |
Centre for Molecular Reproduction and Endocrinology, Monash Institute of Reproduction and Development, Monash University, Melbourne, Victoria 3168, Australia.
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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