Please use this identifier to cite or link to this item: http://hdl.handle.net/1959.13/42858

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Title
Investigation of the role of SRC in capacitation-associated tyrosine phosphorylation of human spermatozoa
Author/Creator
Mitchell, Lisa A.;  Nixon, Brett;  Baker, Mark A.;  Aitken, R. John
Institution
The University of Newcastle. Faculty of Science & Information Technology, School of Environmental and Life Sciences
Description
The process of capacitation is a pre-requisite for mammalian spermatozoa allowing them to gain the ability to fertilize an oocyte. A fundamental part of this mechanism is a dramatic increase in the level of tyrosine phosphorylation. Implicated in this process is a unique cAMP/protein kinase A (PKA)-mediated pathway involving an intermediate PKA-activated tyrosine kinase suggested to be pp60c-src (SRC) in the mouse. This study has verified the importance of SRC as a key intermediate kinase in promoting the tyrosine phosphorylation events associated with human sperm capacitation. The presence of SRC in human spermatozoa was confirmed immunocytochemically and the kinase was localized to subcellular domains compatible with a role in tyrosine phosphorylation. Additionally SRC co-immunoprecipitated with PKA and became activated by phosphorylation of the Y416 residue during human sperm capacitation. Furthermore, the suppression of PKA and SRC through the application of specific inhibitors led to a dramatic decrease in tyrosine phosphorylation. However, although the inhibition of PKA was also accompanied by a suppression of sperm motility, SRC inhibition did not induce a similar response.
Relation
Molecular Human Reproduction Vol. 14, Issue 4, p. 235-243
Publisher Link
http://dx.doi.org/10.1093/molehr/gan007
Date
2008
Publisher
Oxford University Press
Keyword(s)
spermatozoa;  capacitation;  tyrosine phosphorylation;  SRC
Resource Type
journal article
Identifier
http://hdl.handle.net/1959.13/42858
Identifier
ISSN:1360-9947
Reviewed
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Subject
"Molecular Human Reproduction"
 
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