Source:http://linkedlifedata.com/resource/pubmed/id/11273033
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| Predicate | Object |
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| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
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| pubmed:dateCreated |
2001-3-1
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| pubmed:abstractText |
Fertilisation is a highly programmed process by which two radically different cells, sperm and egg, unite to form a zygote, a cell with somatic chromosome numbers. Development of the zygote begins immediately after sperm and egg haploid pronuclei come together, pooling their chromosomes to form a single diploid nucleus with the parental genes. Mammalian fertilisation is the net result of a complex set of molecular events which allow the capacitated spermatozoa to recognise and bind to the egg's extracellular coat, the zona pellucida (ZP), undergo the acrosome reaction, and fuse with the egg plasma membrane. Sperm-zona (egg) interaction leading to fertilisation is a species-specific carbohydrate-mediated event which depends on glycan-recognising proteins (glycosyltransferases/glycosidases/lectin-like molecules) on sperm plasma membrane (receptors) and their complementary glycan units (ligands) on ZP. The receptor-ligand interaction event initiates a signal transduction pathway resulting in the exocytosis of acrosomal contents. The hydrolytic action of the sperm glycohydrolases and proteases released at the site of sperm-egg interaction, along with the enhanced thrust generated by the hyperactivated beat pattern of the bound spermatozoon, are important factors regulating the penetration of egg investments. This review focuses on sperm molecules believed to be important for the interaction with the female genital tract, passage through cumulus oophorus and attachment to ZP, induction of the acrosome reaction, secondary binding events, and passage through the ZP. An understanding of the expression and modifications of molecules thought to be important in multiple events leading to fertilisation will allow new strategies to block these modifications and alter sperm function.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Egg Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Enzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoside Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, IGF Type 2,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/zona pellucida glycoproteins
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| pubmed:status |
MEDLINE
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| pubmed:month |
Feb
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| pubmed:issn |
0967-1994
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
9
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
51-69
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| pubmed:dateRevised |
2007-11-14
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| pubmed:meshHeading |
pubmed-meshheading:11273033-Acrosome,
pubmed-meshheading:11273033-Animals,
pubmed-meshheading:11273033-Carbohydrate Sequence,
pubmed-meshheading:11273033-Cell Membrane,
pubmed-meshheading:11273033-Cricetinae,
pubmed-meshheading:11273033-Egg Proteins,
pubmed-meshheading:11273033-Enzymes,
pubmed-meshheading:11273033-Exocytosis,
pubmed-meshheading:11273033-Female,
pubmed-meshheading:11273033-Genitalia, Female,
pubmed-meshheading:11273033-Glycoside Hydrolases,
pubmed-meshheading:11273033-Guinea Pigs,
pubmed-meshheading:11273033-Humans,
pubmed-meshheading:11273033-Male,
pubmed-meshheading:11273033-Mammals,
pubmed-meshheading:11273033-Membrane Glycoproteins,
pubmed-meshheading:11273033-Mice,
pubmed-meshheading:11273033-Molecular Sequence Data,
pubmed-meshheading:11273033-Rabbits,
pubmed-meshheading:11273033-Rats,
pubmed-meshheading:11273033-Receptor, IGF Type 2,
pubmed-meshheading:11273033-Receptors, Cell Surface,
pubmed-meshheading:11273033-Sperm-Ovum Interactions,
pubmed-meshheading:11273033-Spermatozoa
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| pubmed:year |
2001
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| pubmed:articleTitle |
Mammalian sperm molecules that are potentially important in interaction with female genital tract and egg vestments.
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| pubmed:affiliation |
Department of Obstetrics & Gynecology, Vanderbilt School of Medicine, Nashville, Tennessee 37232-2633, USA. daulat.tulsiani@mcmail.vanderbilt.edu
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review
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