Carbohydrate-based interactions on the route of a spermatozoon to fertilization

被引:129
作者
Töpfer-Petersen, E [1 ]
机构
[1] Hannover Sch Vet Med, Inst Reprod Med, D-30559 Hannover, Germany
关键词
gamete recognition; oviduct; spermatozoa; zona pellucida; zona pellucida-binding proteins;
D O I
10.1093/humupd/5.4.314
中图分类号
R71 [妇产科学];
学科分类号
100211 ;
摘要
Male and female intercommunication along the route which the spermatozoon takes to fertilization utilizes the information potential of carbohydrates, A hierarchy of carbohydrate-based binding events exists ranging fi om spermatozoa-oviduct interaction to primary and secondary binding between spermatozoon and oocyte, Before in-vivo fertilization can occur, spermatozoa are stored in the caudal part of the isthmus, in tight contact with the epithelium cells lining the oviduct, The sperm reservoir seems to be created by surface-associated sperm lectins recognizing epithelial glycoconjugates. With the changing conditions in the oviduct at the time of ovulation, spermatozoa may shed those sperm lectins, creating new surfaces which allow spermatozoa to be released from the epithelium, complete capacitation and interact with the oocyte in the appropriate manner. The first contact between both gametes occurs at the spermatozoa-zona pellucida interface. The 'primary' binding initiates the acrosomal exocytosis of the spermatozoa, followed by the 'secondary' binding of the acrosome-reacted spermatozoon that in consequence leads to sperm penetration through the zona pellucida, Primary and secondary binding events are directed by the cooperative interactions of multiple carbohydrate-recognition systems that may act in a hierarchical and redundant manner. The current perspective will focus on the role of carbohydrate-binding sperm proteins in the sequence of binding events during fertilization in the pig.
引用
收藏
页码:314 / 329
页数:16
相关论文
共 144 条
[31]  
Eble JA, 1997, INTEGRIN LIGAND INTE
[32]  
Einspanier R, 1996, REPROD DOMEST ANIM, V31, P107, DOI 10.1111/j.1439-0531.1995.tb00012.x
[33]   Molecular cloning and characterization of P47, a novel boar sperm-associated zona pellucida-binding protein homologous to a family of mammalian secretory proteins [J].
Ensslin, M ;
Vogel, T ;
Calvete, JJ ;
Thole, HH ;
Schmidtke, J ;
Matsuda, T ;
Töpfer-Petersen, E .
BIOLOGY OF REPRODUCTION, 1998, 58 (04) :1057-1064
[34]   MOUSE ZP1 ENCODES A ZONA-PELLUCIDA PROTEIN HOMOLOGOUS TO EGG ENVELOPE PROTEINS IN MAMMALS AND FISH [J].
EPIFANO, O ;
LIANG, LF ;
DEAN, J .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (45) :27254-27258
[35]   AM67, a secretory component of the guinea pig sperm acrosomal matrix, is related to mouse sperm protein sp56 and the complement component 4-binding proteins [J].
Foster, JA ;
Friday, BB ;
Maulit, MT ;
Blobel, C ;
Winfrey, VP ;
Olson, GE ;
Kim, KS ;
Gerton, GL .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (19) :12714-12722
[36]   Ionic control of sperm function [J].
Fraser, LR .
REPRODUCTION FERTILITY AND DEVELOPMENT, 1995, 7 (04) :905-925
[37]   Animal lectins [J].
Gabius, HJ .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1997, 243 (03) :543-576
[38]   Chromosome localization of the mouse zonadhesin gene and the human zonadhesin gene (ZAN) [J].
Gao, Z ;
Harumi, T ;
Garbers, DL .
GENOMICS, 1997, 41 (01) :119-122
[39]   MEMBRANE-BINDING PEPTIDE FROM THE C2 DOMAIN OF FACTOR-VIII FORMS AN AMPHIPATHIC STRUCTURE AS DETERMINED BY NMR-SPECTROSCOPY [J].
GILBERT, GE ;
BALEJA, JD .
BIOCHEMISTRY, 1995, 34 (09) :3022-3031
[40]   ACTIVATION OF A G-PROTEIN COMPLEX BY AGGREGATION OF BETA-1,4-GALACTOSYLTRANSFERASE ON THE SURFACE OF SPERM [J].
GONG, XH ;
DUBOIS, DH ;
MILLER, DJ ;
SHUR, BD .
SCIENCE, 1995, 269 (5231) :1718-1721