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Vol. 11, Issue 9, 3031-3044, September 2000

The Unique Catalytic Subunit of Sperm cAMP-dependent Protein Kinase Is the Product of an Alternative Calpha mRNA Expressed Specifically in Spermatogenic Cells

Jovenal T. San Agustin, Curtis G. Wilkerson,* and George B. Witmandagger

Department of Cell Biology, University of Massachusetts Medical School, Worcester, Massachusetts 01655

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 Cs, whose amino terminus differs from those of published C isoforms of other species. Isolation and sequencing of cDNA clones encoding ovine Cs and Calpha 1 (the predominant somatic isoform) now reveal that Cs is the product of an alternative transcript of the Calpha gene. Cs cDNA clones from murine and human testes also were isolated and sequenced, indicating that Cs is of ancient origin and widespread in mammals. In the mouse, Cs 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 Cs first appears in pachytene spermatocytes. This is the first demonstration of a cell type-specific expression for any C isoform. The conservation of Cs throughout mammalian evolution suggests that the unique structure of Cs is important in the subunit's localization or function within the sperm.


* Present address: Michigan State University-Department of Energy Plant Research Laboratory, East Lansing, MI 48824.

dagger Corresponding author. E-mail address: george.witman{at}umassmed.edu.


Molecular Biology of the Cell
Vol. 11, 3031-3044, September 2000
Copyright © 2000 by The American Society for Cell Biology



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