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From the * Ontogenie et Reproduction, Centre de
Recherche du Centre Hospitalier Universitaire de Québec-Centre
Hospitalier de l'Université Laval, Ste-Foy, Québec, Canada; the
Département
d'Obstétrique/Gynécologie, Centre de Recherche en Biologie de la
Reproduction, Université Laval, Ste-Foy, Québec, Canada; and the
Departments of Pediatrics, Human Genetics, and
Pharmacology and Therapeutics, McGill University, and the Research Institute
at the Montreal Children's Hospital of the McGill University Health Centre,
Montreal, Canada.
Present address: The Jackson
Laboratory, 600 Main St, Bar Harbor, ME 04609.
| Correspondence to: Pierre Leclerc, Ontogenie et Reproduction, Centre de Recherche du CHUQ-CHUL, 2705 Boul. Laurier, Ste-Foy, QC, Canada G1V 4G2 (e-mail: pierre.leclerc{at}crchul.ulaval.ca). |
An increase in protein tyrosine phosphorylation occurs during sperm
capacitation in numerous species. The involvement of Src-related tyrosine
kinases in this phenomenon has been demonstrated using different inhibitors
specifically targeting this family of enzymes. In mammals, this group of
nonreceptor tyrosine kinases is made up of 8 members with similar SRC homology
domain 3 (SH3) and SH2 domains. Although some members of this group of enzymes
can compensate for one another, showing some redundancy, each is unique and
may perform specific functions during male germ cell development. To further
characterize the importance of Src-related tyrosine kinases in the events
leading to proper sperm formation, and because no inhibitor affecting a single
gene product exists, expression of Src, Yes1, Fyn,
Lyn, Lck, Hck, Blk, and Fgr was
assessed by real-time polymerase chain reaction in developing mouse testes and
in enriched populations of mouse spermatogenic cells, revealing distinct
expression profiles for each kinase during testis development and in isolated
male germ cells. Immunolocalization of SRC, LYN, and HCK in adult mouse testes
as well as in mature spermatozoa further confirmed differential localization
of these kinases during spermatogenesis. Although mRNA levels of these latter
kinases were higher in spermatogonia and spermatocytes than in spermatids,
protein levels were highest in spermatids, suggesting delayed transcript
translation. Taken together, these results clearly show an uneven expression
of each kinase in different spermatogenic cells, indicating that each member
may play a different role during spermatogenesis, in addition to highlighting
the complexity of Src-related kinase expression regulation in male germ cells.
Furthermore, differential localization of these tyrosine kinases in mature
spermatozoa also suggests a specific role for each member in sperm function
and integrity.
Key words: Reproductive tract, sperm, spermatogenesis, tyrosine kinase
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