Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2001-6-25
pubmed:databankReference
pubmed:abstractText
The zona pellucida, a transparent envelope surrounding the mammalian oocyte, comprises three glycoproteins, ZPA, ZPB and ZPC, and plays important roles in fertilization. We have previously reported that apparent relative molecular masses of bovine zona glycoproteins on SDS/PAGE under nonreducing conditions after removal of poly N-acetyllactosamine at the nonreducing portion of sugar chains with endo-beta-galactosidase are 72 000, 58 000 and 45 000 [Noguchi, S., Yonezawa, N., Katsumata, T., Hashizume, K.,Kuwayama, M., Hamano, S., Watanabe, S. & Nakano, M. (1994) Biochim. Biophys. Acta 1201, 7-14]. The N-terminal amino-acid sequences and crossreactivity to antibodies specific to each porcine zona component show that the bovine components correspond to porcine ZPA, ZPB and ZPC, respectively. In this study, we deduced amino-acid sequences of bovine ZPA and ZPB by cDNA cloning and sequencing. Identities in amino-acid sequences between bovine and porcine counterparts were 77% for ZPA and 75% for ZPB, whereas between bovine and murine counterparts identities were 57% for ZPA and 37% for ZPB. The positions of Cys were completely conserved in bovine ZPA and ZPB compared with counterparts of other mammalian species. Bovine ZPA was processed between Ala and Asp on fertilization, suggesting that the consensus motif for the processing is Ala-Asp-Asp/Glu. We purified bovine zona components and examined their sperm-binding activity with an in vitro competition assay and sperm-bead-binding assay. As a result, ZPB showed the strongest sperm-binding activity among the components. ZPC also showed sperm-binding activity and the activity per molecule was about one-sixth that of ZPB according to the result of the sperm-bead-binding assay. We could not determine if ZPA has significant sperm-binding activity, but the activity may be much lower than that of ZPB even if ZPA has significant activity. Thus, ZPB may play a major role in sperm binding in bovine zona.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:volume
268
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3587-94
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed-meshheading:11422390-Amino Acid Sequence, pubmed-meshheading:11422390-Animals, pubmed-meshheading:11422390-Base Sequence, pubmed-meshheading:11422390-Cattle, pubmed-meshheading:11422390-Chromatography, High Pressure Liquid, pubmed-meshheading:11422390-DNA, Complementary, pubmed-meshheading:11422390-Egg Proteins, pubmed-meshheading:11422390-Glycoside Hydrolases, pubmed-meshheading:11422390-Male, pubmed-meshheading:11422390-Membrane Glycoproteins, pubmed-meshheading:11422390-Molecular Sequence Data, pubmed-meshheading:11422390-Receptors, Cell Surface, pubmed-meshheading:11422390-Sequence Homology, Amino Acid, pubmed-meshheading:11422390-Sperm-Ovum Interactions, pubmed-meshheading:11422390-Spermatozoa, pubmed-meshheading:11422390-Zona Pellucida, pubmed-meshheading:11422390-beta-Galactosidase
pubmed:year
2001
pubmed:articleTitle
Molecular cloning of bovine zona pellucida glycoproteins ZPA and ZPB and analysis for sperm-binding component of the zona.
pubmed:affiliation
Graduate School of Science and Technology, and Department of Chemistry, Chiba University, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't