rdf:type |
|
lifeskim:mentions |
umls-concept:C0006556,
umls-concept:C0007452,
umls-concept:C0007589,
umls-concept:C0009017,
umls-concept:C0013935,
umls-concept:C0017262,
umls-concept:C0018270,
umls-concept:C0029045,
umls-concept:C0185117,
umls-concept:C0205065,
umls-concept:C0213144,
umls-concept:C0679058,
umls-concept:C1511938,
umls-concept:C1547699,
umls-concept:C2700640,
umls-concept:C2911684
|
pubmed:issue |
1
|
pubmed:dateCreated |
2002-3-28
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pubmed:abstractText |
Growth differentiation factor-9 (GDF-9), a member of the transforming growth factor-beta superfamily, is known to be expressed specifically in ovaries of various mammalian species and to be important for normal follicular development in mice. In the present study, a cDNA encoding for bovine GDF-9 was isolated and characterized, and expression of GDF-9 mRNA in ovarian oocytes and in-vitro-derived embryos was examined. Isolation of bovine GDF-9 was achieved using the polymerase chain reaction (PCR) with primers based on an ovine GDF-9 cDNA sequence. A 1385 bp cDNA encodes a deduced 453-amino acid sequence which contains the proregion (318 residues) and the mature protein (135 residues) portion. The deduced amino acid sequence of bovine GDF-9 is 98 and 93% identical to ovine GDF-9 and human GDF-9 in the mature portion of the molecule, respectively. Results from reverse transcription (RT)-PCR analysis detected bovine GDF-9 mRNA in preantral follicles (150-200 microm in diameter), early antral follicles (400-800 microm in diameter), and immature oocytes, whereas no detectable PCR signal was observed in cumulus/granulosa cells. In addition, bovine GDF-9 mRNA continued to be expressed in developing embryos up to the 8-cell stage, but was undetectable at the blastocyst stage. These findings give rise to new possibilities regarding an additional physiological role of GDF-9 in early embryonic development as well as in the development of follicles.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/BMP15 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Bmp15 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Bone Morphogenetic Protein 15,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/GDF9 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Gdf9 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Growth Differentiation Factor 9,
http://linkedlifedata.com/resource/pubmed/chemical/Growth Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Intercellular Signaling Peptides...
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pubmed:status |
MEDLINE
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pubmed:issn |
1520-4553
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:volume |
3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3-10
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:11918837-Amino Acid Sequence,
pubmed-meshheading:11918837-Animals,
pubmed-meshheading:11918837-Base Sequence,
pubmed-meshheading:11918837-Blastocyst,
pubmed-meshheading:11918837-Bone Morphogenetic Protein 15,
pubmed-meshheading:11918837-Cattle,
pubmed-meshheading:11918837-Cloning, Molecular,
pubmed-meshheading:11918837-DNA, Complementary,
pubmed-meshheading:11918837-Female,
pubmed-meshheading:11918837-Fertilization in Vitro,
pubmed-meshheading:11918837-Gene Expression Regulation, Developmental,
pubmed-meshheading:11918837-Growth Differentiation Factor 9,
pubmed-meshheading:11918837-Growth Substances,
pubmed-meshheading:11918837-Humans,
pubmed-meshheading:11918837-Intercellular Signaling Peptides and Proteins,
pubmed-meshheading:11918837-Mice,
pubmed-meshheading:11918837-Molecular Sequence Data,
pubmed-meshheading:11918837-Oocytes,
pubmed-meshheading:11918837-Pregnancy,
pubmed-meshheading:11918837-Sequence Alignment
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pubmed:year |
2001
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pubmed:articleTitle |
Molecular cloning of a cDNA encoding a bovine growth differentiation factor-9 (GDF-9) and expression of GDF-9 in bovine ovarian oocytes and in vitro-produced embryos.
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pubmed:affiliation |
Research Institute for the Functional Peptides, Yamagata, Japan. sendai@func-p.co.jp
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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