| pubmed-article:17566275 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17566275 | lifeskim:mentions | umls-concept:C0007452 | lld:lifeskim |
| pubmed-article:17566275 | lifeskim:mentions | umls-concept:C0039005 | lld:lifeskim |
| pubmed-article:17566275 | lifeskim:mentions | umls-concept:C0043519 | lld:lifeskim |
| pubmed-article:17566275 | lifeskim:mentions | umls-concept:C0037868 | lld:lifeskim |
| pubmed-article:17566275 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
| pubmed-article:17566275 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:17566275 | lifeskim:mentions | umls-concept:C0237881 | lld:lifeskim |
| pubmed-article:17566275 | lifeskim:mentions | umls-concept:C0750502 | lld:lifeskim |
| pubmed-article:17566275 | pubmed:dateCreated | 2007-6-14 | lld:pubmed |
| pubmed-article:17566275 | pubmed:abstractText | The zona pellucida that surrounds the mammalian oocyte plays a role in species-selective sperm-egg interactions. In the pig and cattle, the zona pellucida consists of ZPA, ZPB and ZPC. Sperm binding activity of porcine zona glycoproteins is conferred by tri- and tetra-antennary complex-type in cattle it is conferred by a high-mannose-type chain o f f ive mannose residues. Non-reducing terminal residues of these N-linked chains, beta-galactosyl residues in pig and alpha-mannosyl residues in cattle, are involved in the binding of zona glycoproteins to respective spermatozoa. The major N-linked chains of recombinant porcine ZPB expressed using the baculovirus-Sf9 cell expression system are pauci- and high-mannose-type chains that are different in structure to the major neutral N-linked chains of the porcine zona but similar to those of the bovine zona. The mixture of porcine ZPB/ZPC co-expressed in Sf9 cells binds to bovine sperm but not to porcine sperm, indicating an essential role of the N-linked chains in species-selective recognition of sperm in pig and cattle. Asn to Asp mutations at either of two of the N-glycosylation sites of ZPB, residue 203 or 220, significantly reduce the sperm-binding activity of the ZPB/ZPC mixture, while a similar mutation at Asn333 has no effect on binding. These results coincide with our previous report that tri- and tetra-antennary complex-type chains are localized at Asn220 in native porcine ZPB and suggest that the N-glycans located in the N-terminal half of the ZP domain of porcine ZPB are involved in sperm-zona binding. | lld:pubmed |
| pubmed-article:17566275 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17566275 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17566275 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17566275 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17566275 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17566275 | pubmed:author | pubmed-author:NakanoMM | lld:pubmed |
| pubmed-article:17566275 | pubmed:author | pubmed-author:KanaiSS | lld:pubmed |
| pubmed-article:17566275 | pubmed:author | pubmed-author:YonezawaNN | lld:pubmed |
| pubmed-article:17566275 | pubmed:volume | 63 | lld:pubmed |
| pubmed-article:17566275 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17566275 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17566275 | pubmed:pagination | 217-28 | lld:pubmed |
| pubmed-article:17566275 | pubmed:meshHeading | pubmed-meshheading:17566275... | lld:pubmed |
| pubmed-article:17566275 | pubmed:meshHeading | pubmed-meshheading:17566275... | lld:pubmed |
| pubmed-article:17566275 | pubmed:meshHeading | pubmed-meshheading:17566275... | lld:pubmed |
| pubmed-article:17566275 | pubmed:meshHeading | pubmed-meshheading:17566275... | lld:pubmed |
| pubmed-article:17566275 | pubmed:meshHeading | pubmed-meshheading:17566275... | lld:pubmed |
| pubmed-article:17566275 | pubmed:meshHeading | pubmed-meshheading:17566275... | lld:pubmed |
| pubmed-article:17566275 | pubmed:meshHeading | pubmed-meshheading:17566275... | lld:pubmed |
| pubmed-article:17566275 | pubmed:meshHeading | pubmed-meshheading:17566275... | lld:pubmed |
| pubmed-article:17566275 | pubmed:meshHeading | pubmed-meshheading:17566275... | lld:pubmed |
| pubmed-article:17566275 | pubmed:meshHeading | pubmed-meshheading:17566275... | lld:pubmed |
| pubmed-article:17566275 | pubmed:meshHeading | pubmed-meshheading:17566275... | lld:pubmed |
| pubmed-article:17566275 | pubmed:meshHeading | pubmed-meshheading:17566275... | lld:pubmed |
| pubmed-article:17566275 | pubmed:meshHeading | pubmed-meshheading:17566275... | lld:pubmed |
| pubmed-article:17566275 | pubmed:meshHeading | pubmed-meshheading:17566275... | lld:pubmed |
| pubmed-article:17566275 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17566275 | pubmed:articleTitle | Structural significance of N-glycans of the zona pellucida on species-selective recognition of spermatozoa between pig and cattle. | lld:pubmed |
| pubmed-article:17566275 | pubmed:affiliation | Graduate School of Science and Technology, Chiba University, 1-33, Yayoi-cho, Inage-ku, Chiba 263-8522, Japan. nyoneza@faculty.chiba-u.jp | lld:pubmed |
| pubmed-article:17566275 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17566275 | pubmed:publicationType | Review | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17566275 | lld:pubmed |
