Source:http://linkedlifedata.com/resource/pubmed/id/12074561
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2002-6-20
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pubmed:abstractText |
We have previously described the affinity of a pig sperm surface protein, P68, to mammalian zonae pellucidae (ZP). In this report, we identified P68 as arylsulfatase A (AS-A) based on the presence of P68 tryptic peptide sequences in the pig testis AS-A cDNA sequence. Our objective was to demonstrate the presence of AS-A on the sperm surface and to elucidate its role in ZP binding. Immunogold electron microscopy revealed the presence of AS-A on the sperm surface. Furthermore, live pig sperm and the extract of peripheral sperm plasma membrane proteins exhibited AS-A's desulfation activity. Significantly, the role of pig sperm surface AS-A in ZP binding was demonstrated by dose-dependent decreases of sperm-ZP binding upon sperm pretreatment with anti-AS-A IgG/Fab, and by the binding of Alexa-430-conjugated sperm surface AS-A to homologous ZP. ZP pretreatment with anti-pig-ZP3 antibody abolished AS-A binding, suggesting that ZP3, recognized as the pig sperm receptor, was AS-A's binding ligand. This was further confirmed by the ability of exogenous ZP3 to competitively inhibit AS-A-ZP binding. Similarly, purified ZP3alpha, a major sperm receptor component of ZP3, exhibited great inhibitory effect on AS-A-ZP binding. All of these results designated a new function of AS-A in gamete interaction.
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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 |
Jul
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pubmed:issn |
0012-1606
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pubmed:author |
pubmed-author:BergerTrishT,
pubmed-author:BuhrMaryM,
pubmed-author:CarmonaEuridiceE,
pubmed-author:EkkerMarcM,
pubmed-author:FluhartyArvan LAL,
pubmed-author:PromdeeLimthongL,
pubmed-author:SoboloffTanyaT,
pubmed-author:TanphaichitrNongnujN,
pubmed-author:WeerachatyanukulWattanaW,
pubmed-author:WhiteDawnD
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pubmed:copyrightInfo |
(c) 2002 Elsevier Science (USA).
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
247
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
182-96
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12074561-Amino Acid Sequence,
pubmed-meshheading:12074561-Animals,
pubmed-meshheading:12074561-Cell Membrane,
pubmed-meshheading:12074561-Cerebroside-Sulfatase,
pubmed-meshheading:12074561-Female,
pubmed-meshheading:12074561-Male,
pubmed-meshheading:12074561-Molecular Sequence Data,
pubmed-meshheading:12074561-Sequence Alignment,
pubmed-meshheading:12074561-Sperm-Ovum Interactions,
pubmed-meshheading:12074561-Spermatozoa,
pubmed-meshheading:12074561-Swine,
pubmed-meshheading:12074561-Zona Pellucida
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pubmed:year |
2002
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pubmed:articleTitle |
Arylsulfatase a is present on the pig sperm surface and is involved in sperm-zona pellucida binding.
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pubmed:affiliation |
Hormones/Growth/Development Research Group, Ottawa Health Research Institute, Ontario, Canada K1Y 4E9.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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