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* To whom correspondence should be addressed. E-mail: rmturner{at}vet.upenn.edu.
Both cyclic AMP (cAMP)/Protein Kinase-A (PK-A) and Calcium (Ca++) signaling pathways are known to be involved in the regulation of motility in mammalian sperm. Calmodulin (CaM) is a ubiquitous Ca++ sensor that has been implicated as playing a role in the acrosome reaction. Here we identify an insoluble pool of CaM in sperm and show that the protein, in addition to its presence in the acrosome, also is found in the principal piece of the flagellum. These findings are consistent with, though not proof of, the presence of a pool of CaM in the fibrous sheath. The Ca++/CaM dependent protein kinase II
, (CaMKII
) a downstream target of Ca++/CaM, similarly localizes to the principal piece. In addition, we confirm earlier reports that a CaM inhibitor decreases sperm motility. However, we find that this inhibition can be largely reversed by stimulation of PK-A if substrates for oxidative respiration are present in the medium. Our results suggest that a Ca++/CaM/CaMKII signaling pathway in the sperm principal piece is involved in regulating sperm motility and that this pathway may function either in parallel with, or upstream of the cAMP/PK-A pathway.
Key words: Sperm
calmodulin
flagellum
signaling
sperm motility
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