PMID: 6535450Jan 1, 1984Paper

Phosphorylation of cAMP-dependent protein kinases in normal and abnormal human sperm

Archives of Andrology
U Eppenberger, D Fabbro

Abstract

The molecular characterization and distribution of cAMP-dependent protein kinases (cAPK) of normal and pathological (reduced progressive motility or altered morphology) human semen were investigated. Photoaffinity labeling with 8-N3-[32P]cAMP of human sperm cytosols revealed four specific cAMP-binding proteins (MW: 52 kD, 47 kD, 42 kD, and 37 kD) with the following quantitative distribution: 65% (47 kD), 30% (52 kD), and less than 5% (42/37 kD). In contrast, the seminal plasma of the respective semen samples incorporated the 8-azido cAMP photolabel predominantly into the 37 kD protein (greater than 50%). The cAMP-binding proteins with MW of 52 kD and 47 kD corresponded to the regulatory subunits R II and R I of the respective cAPK isoenzymes I and II. Neither qualitative nor quantitative differences could be detected in the distribution between seminal plasma and sperm as well as in the molecular properties of RI (47 kD), R II (52 kD), and of their proteolytic products (42 kD and 37 kD) between normal and pathological human semen. DEAE-cellulose chromatography revealed that type II isozyme was the predominant form (80% of the total cAMP-dependent protein kinase activity of sperm); the protein kinase isozyme pattern was similar ...Continue Reading

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