Source:http://linkedlifedata.com/resource/pubmed/id/17005942
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
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| pubmed:dateCreated |
2006-12-21
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| pubmed:abstractText |
Members of the RNase superfamily participate in a diverse array of biological processes, including RNA degradation, antipathogen activities, angiogenesis, and digestion. In the present study, we cloned the rat RNase9 gene by in silico methods and genome walking based on homology to the Macaca mulatta (rhesus monkey) epididymal RNase9. The gene is located on chromosome 15p14, spanning two exons, and is clustered with other members of the RNase A superfamily. It contains 1279 bp and encodes 182 amino acids, including a 24-amino acid signal peptide, and it has unique features known from other RNases. Unlike those other members, the rat RNase9 mRNA was specifically expressed in the epididymis, especially in the caput and corpus, and exhibited an androgen-dependent expression pattern but was downregulated in an epididymitis animal model. The RNASE9 was expressed in a principal cell-specific pattern. Interestingly, most of the principal cells in the caput expressed the RNASE9; however, in the distal caput, the principal cells showed a checkerboard-like pattern of immunoreactivity. We also observed that the RNASE9 was bound on the acrosomal domain of sperm. Its potential roles in sperm maturation are discussed.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Androgens,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonuclease, Pancreatic,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Testosterone Propionate
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| pubmed:status |
MEDLINE
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| pubmed:month |
Jan
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| pubmed:issn |
0006-3363
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
76
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
63-73
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| pubmed:dateRevised |
2009-11-19
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| pubmed:meshHeading |
pubmed-meshheading:17005942-Amino Acid Sequence,
pubmed-meshheading:17005942-Androgens,
pubmed-meshheading:17005942-Animals,
pubmed-meshheading:17005942-Base Sequence,
pubmed-meshheading:17005942-Cloning, Molecular,
pubmed-meshheading:17005942-DNA, Complementary,
pubmed-meshheading:17005942-Epididymis,
pubmed-meshheading:17005942-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:17005942-Inflammation,
pubmed-meshheading:17005942-Male,
pubmed-meshheading:17005942-Molecular Sequence Data,
pubmed-meshheading:17005942-RNA, Messenger,
pubmed-meshheading:17005942-Rats,
pubmed-meshheading:17005942-Ribonuclease, Pancreatic,
pubmed-meshheading:17005942-Ribonucleases,
pubmed-meshheading:17005942-Sequence Homology, Amino Acid,
pubmed-meshheading:17005942-Spermatozoa,
pubmed-meshheading:17005942-Testosterone Propionate,
pubmed-meshheading:17005942-Vas Deferens,
pubmed-meshheading:17005942-Vasectomy
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| pubmed:year |
2007
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| pubmed:articleTitle |
RNase9, an androgen-dependent member of the RNase A family, is specifically expressed in the rat epididymis.
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| pubmed:affiliation |
Shanghai Key Laboratory for Molecular Andrology, State Key Laboratory of Molecular Biology.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
|