| http://purl.uniprot.org/citations/7556898 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/7556898 | http://www.w3.org/2000/01/rdf-schema#comment | "An essential step in murine fertilization is the binding of acrosome-intact sperm to specific O-linked glycans on zona pellucida glycoprotein 3 (ZP3). While there is agreement on the primary role of O-linked glycans in sperm-ZP3 binding, there is a striking lack of consensus on both the terminal monosaccharide(s) required for a functional binding site and the cognate protein on the sperm cell surface that recognizes this glycan. Much current debate centers on the essential role of nonreducing terminal N-acetyl-glucosaminyl or alternatively, alpha-galactosyl residues, to form a functional sperm binding ligand. Relevant to this debate, we demonstrated that alpha 1,3-galactosyltransferase (alpha 3-GT), which adds nonreducing terminal alpha-galactosyl residues to glycans, is not expressed in murine spermatocytes or spermatids. The objectives of this study were to determine whether alpha 3-GT is expressed in female germ cells and to compare the pattern of expression of two other terminal glycosyltransferases, beta 1,4-galactosyltransferase (beta 4-GT) and alpha 2,6-sialyltransferase (alpha 6-ST), between male and female germ cells. Total RNA was isolated from growing oocytes obtained from 15-day-old animals, fully grown oocytes, and eggs as well as spermatogonia, spermatocytes, and spermatids. The presence of alpha 3-GT, beta 4-GT, and alpha 6-ST mRNAs was analyzed by an RT-PCR-based assay. Our data demonstrate that the alpha 3-GT gene is expressed in female germ cells, but not in male germ cells. In contrast, both beta 4-GT and alpha 6-ST are expressed during oogenesis and spermatogenesis. This differential expression of alpha 3-GT in female germ cells is consistent with the model of sperm-egg binding in which a nonreducing terminal alpha-galactosyl residue is required for a functional determinant on ZP3 and with our hypothesis that the biological significance for the suppression of alpha 3-GT expression in male germ cells is to prevent sperm-sperm aggregation."xsd:string |
| http://purl.uniprot.org/citations/7556898 | http://purl.org/dc/terms/identifier | "doi:10.1006/dbio.1995.1273"xsd:string |
| http://purl.uniprot.org/citations/7556898 | http://purl.uniprot.org/core/author | "Shaper J.H."xsd:string |
| http://purl.uniprot.org/citations/7556898 | http://purl.uniprot.org/core/author | "Shaper N.L."xsd:string |
| http://purl.uniprot.org/citations/7556898 | http://purl.uniprot.org/core/author | "Wright W.W."xsd:string |
| http://purl.uniprot.org/citations/7556898 | http://purl.uniprot.org/core/author | "Joziasse D.H."xsd:string |
| http://purl.uniprot.org/citations/7556898 | http://purl.uniprot.org/core/author | "Johnston D.S."xsd:string |
| http://purl.uniprot.org/citations/7556898 | http://purl.uniprot.org/core/date | "1995"xsd:gYear |
| http://purl.uniprot.org/citations/7556898 | http://purl.uniprot.org/core/name | "Dev Biol"xsd:string |
| http://purl.uniprot.org/citations/7556898 | http://purl.uniprot.org/core/pages | "224-232"xsd:string |
| http://purl.uniprot.org/citations/7556898 | http://purl.uniprot.org/core/title | "The gene encoding murine alpha 1,3-galactosyltransferase is expressed in female germ cells but not in male germ cells."xsd:string |
| http://purl.uniprot.org/citations/7556898 | http://purl.uniprot.org/core/volume | "171"xsd:string |
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