UMMS Affiliation

Department of Cell Biology; Program in Molecular Medicine

Publication Date


Document Type



*Alternative Splicing; Amino Acid Sequence; Animals; Base Sequence; Brain; Catalytic Domain; Cattle; Cloning, Molecular; Consensus Sequence; Cyclic AMP-Dependent Protein Kinases; Humans; Isoenzymes; Male; Mice; Molecular Sequence Data; Protein Subunits; Rats; Recombinant Proteins; Sequence Alignment; Sequence Homology, Amino Acid; Sheep; Spermatogenesis; Spermatozoa; Testis


Life Sciences | Medicine and Health Sciences


cAMP-dependent protein kinase has a central role in the control of mammalian sperm capacitation and motility. Previous protein biochemical studies indicated that the only cAMP-dependent protein kinase catalytic subunit (C) in ovine sperm is an unusual isoform, termed C(s), whose amino terminus differs from those of published C isoforms of other species. Isolation and sequencing of cDNA clones encoding ovine C(s) and Calpha1 (the predominant somatic isoform) now reveal that C(s) is the product of an alternative transcript of the Calpha gene. C(s) cDNA clones from murine and human testes also were isolated and sequenced, indicating that C(s) is of ancient origin and widespread in mammals. In the mouse, C(s) transcripts were detected only in testis and not in any other tissue examined, including ciliated tissues and ovaries. Finally, immunohistochemistry of the testis shows that C(s) first appears in pachytene spermatocytes. This is the first demonstration of a cell type-specific expression for any C isoform. The conservation of C(s) throughout mammalian evolution suggests that the unique structure of C(s) is important in the subunit's localization or function within the sperm.


Mol Biol Cell. 2000 Sep;11(9):3031-44.

Journal/Book/Conference Title

Molecular biology of the cell

Related Resources

Link to Article in PubMed

PubMed ID