Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2011-5-4
pubmed:abstractText
Sexually reproducing animals require an orchestrated communication between spermatozoa and the egg to generate a new individual. Capacitation, a maturational complex phenomenon that occurs in the female reproductive tract, renders spermatozoa capable of binding and fusing with the oocyte, and it is a requirement for mammalian fertilization. Capacitation encompasses plasma membrane reorganization, ion permeability regulation, cholesterol loss and changes in the phosphorylation state of many proteins. Novel tools to study sperm ion channels, image intracellular ionic changes and proteins with better spatial and temporal resolution, are unraveling how modifications in sperm ion transport and phosphorylation states lead to capacitation. Recent evidence indicates that two parallel pathways regulate phosphorylation events leading to capacitation, one of them requiring activation of protein kinase A and the second one involving inactivation of ser/thr phosphatases. This review examines the involvement of ion transporters and phosphorylation signaling processes needed for spermatozoa to achieve capacitation. Understanding the molecular mechanisms leading to fertilization is central for societies to deal with rising male infertility rates, to develop safe male gamete-based contraceptives and to preserve biodiversity through better assisted fertilization strategies.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Calcium, http://linkedlifedata.com/resource/pubmed/chemical/Calcium Channels, http://linkedlifedata.com/resource/pubmed/chemical/Catsper1 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP-Dependent Protein Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Cystic Fibrosis Transmembrane..., http://linkedlifedata.com/resource/pubmed/chemical/Epithelial Sodium Channel, http://linkedlifedata.com/resource/pubmed/chemical/Ion Channels, http://linkedlifedata.com/resource/pubmed/chemical/Phospholipid Transfer Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels, Inwardly..., http://linkedlifedata.com/resource/pubmed/chemical/src-Family Kinases
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1745-7262
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
13
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
395-405
pubmed:meshHeading
pubmed-meshheading:21540868-Animals, pubmed-meshheading:21540868-Calcium, pubmed-meshheading:21540868-Calcium Channels, pubmed-meshheading:21540868-Cyclic AMP-Dependent Protein Kinases, pubmed-meshheading:21540868-Cystic Fibrosis Transmembrane Conductance Regulator, pubmed-meshheading:21540868-Epithelial Sodium Channel, pubmed-meshheading:21540868-Female, pubmed-meshheading:21540868-Fertilization, pubmed-meshheading:21540868-Hydrogen-Ion Concentration, pubmed-meshheading:21540868-Ion Channels, pubmed-meshheading:21540868-Male, pubmed-meshheading:21540868-Membrane Microdomains, pubmed-meshheading:21540868-Phospholipid Transfer Proteins, pubmed-meshheading:21540868-Phosphoprotein Phosphatases, pubmed-meshheading:21540868-Phosphorylation, pubmed-meshheading:21540868-Potassium Channels, Inwardly Rectifying, pubmed-meshheading:21540868-Signal Transduction, pubmed-meshheading:21540868-Sperm Capacitation, pubmed-meshheading:21540868-Spermatozoa, pubmed-meshheading:21540868-src-Family Kinases
pubmed:year
2011
pubmed:articleTitle
Ion channels, phosphorylation and mammalian sperm capacitation.
pubmed:affiliation
Department of Veterinary and Animal Science, Paige Labs, University of Massachusets, Amherst, MA 01003, USA.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural