Source:http://linkedlifedata.com/resource/pubmed/id/11170275
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2001-2-22
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pubmed:abstractText |
Presence or absence of three distinct bovine seminal heparin-binding proteins (21-31 kDa) recognized in sperm extracts by a monoclonal antibody, M1, is a diagnostic indicator of fertility differences among bulls producing normal semen. We recently identified a 31 kDa fertility-associated antigenin bovine seminal fluid as a unique DNase I-like protein. We now report purification and identification of a 24 kDa seminal heparin-binding protein (HBP-24) recognized by M1. N-terminal microsequence analysis of HBP-24 purified from seminal fluid yielded 20 amino acid residues that displayed 90% identity to the N-terminus of a bovine metalloproteinase inhibitor identified as tissue inhibitor of metalloproteinases-2 (TIMP-2). A single immunoreactive band migrating at 24 kDa was detected in Western blots of cauda epididymal sperm extracts following incubation with purified seminal heparin-binding proteins and subsequent washing in vitro, indicating TIMP-2 bound to sperm membranes. Expression of TIMP-2 mRNA was detected by RT-PCR in bovine bulbourethral gland, prostate, and seminal vesicles. Mobility of the 24 kDa heparin-binding protein increased under nonreducing SDS-PAGE to approximately 21 kDa, characteristic of the reported molecular mass of TIMP-2. To our knowledge, this is the first report of TIMP-2 binding to spermatozoa and of TIMP-2 mRNA expression in bovine accessory sex glands. These results corroborate previous reports regarding the site of production of heparin-binding proteins that are related to bull fertility, and suggest that TIMP-2 influences fertility of bulls, either through inhibition of metalloprotease activity in semen or via undefined activities independent of matrix metalloproteinase (MMP) inhibition.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1040-452X
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pubmed:author | |
pubmed:copyrightInfo |
Copyright 2001 Wiley-Liss, Inc.
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pubmed:issnType |
Print
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pubmed:volume |
58
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
336-41
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11170275-Amino Acid Sequence,
pubmed-meshheading:11170275-Animals,
pubmed-meshheading:11170275-Blotting, Western,
pubmed-meshheading:11170275-Cattle,
pubmed-meshheading:11170275-Fertility,
pubmed-meshheading:11170275-Heparin,
pubmed-meshheading:11170275-Male,
pubmed-meshheading:11170275-Molecular Sequence Data,
pubmed-meshheading:11170275-Protease Inhibitors,
pubmed-meshheading:11170275-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:11170275-Semen,
pubmed-meshheading:11170275-Sequence Alignment,
pubmed-meshheading:11170275-Spermatozoa,
pubmed-meshheading:11170275-Tissue Inhibitor of Metalloproteinase-2
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pubmed:year |
2001
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pubmed:articleTitle |
Identification of a heparin-binding protein in bovine seminal fluid as tissue inhibitor of metalloproteinases-2.
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pubmed:affiliation |
Department of Animal Sciences, University of Arizona, Tucson, Arizona 85721-0038, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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