Distribution of a seminal plasma-associated protein kinase inhibitor in normal, oligozoospermic, and vasectomized men.

Human sperm-free seminal plasma contains an inhibitor, which is protein in nature, of the histone kinase present in seminal plasma. Since protein kinase inhibitors have been observed to be present in spermatozoa, the objective of the present study was to determine whether this seminal plasma-associated enzyme inhibitor originates from the sperm, or whether it is a component of accessory secretion(s) comprising the seminal plasma. Sperm-free seminal plasma from normospermic (greater than 20 X 10(6) sperm/ml), oligozoospermic (less than or equal to 20 X 10(6) sperm/ml), and vasectomized donors was obtained, and inhibitor-enriched fractions were prepared by (NH4)2SO4 fractionation and gel filtration. Contamination of the sperm-free seminal plasma by spermatozoa or spermatozoan components was negligible as assessed by light microscopy, polyacrylamide gel electrophoresis, and measurement of the activity of cyclic adenosine 3',5'-monophosphate (cAMP)-dependent protein kinase. Specific (inhibitory units/mg protein) and total inhibitory activities were determined in each of the donors by constructing linear inhibition curves using various concentrations of inhibitor. The results were correlated with the initial sperm concentration. There was no apparent relationship between the amount of inhibitory activity present and the initial sperm concentration. The histone kinase inhibitor also did not appear to be associated with testicular or epididymal secretions since it was observed in the seminal plasma of vasectomized donors. It is concluded that this inhibitor of histone kinase originates from the accessory secretions comprising the human ejaculate.

[1]  V. Vacquier,et al.  Effects of extracellular egg factors on sperm guanylate cyclase. , 1985, Science.

[2]  J. K. Bentley,et al.  A peptide associated with eggs causes a mobility shift in a major plasma membrane protein of spermatozoa. , 1984, The Journal of biological chemistry.

[3]  H. Toeg,et al.  Characterization and localization of cAMP-dependent protein kinases in rat caudal epididymal sperm. , 1984, The Journal of biological chemistry.

[4]  V. Vacquier,et al.  Dephosphorylation of a major sperm membrane protein is induced by egg jelly during sea urchin fertilization. , 1983, Proceedings of the National Academy of Sciences of the United States of America.

[5]  M. Wilson,et al.  Tissue sources of protein kinase activities in human seminal fluid: studies of normal, oligozoospermic, and vasectomized men. , 1983, Fertility and sterility.

[6]  A. Rephaeli,et al.  Calmodulin stimulation of 45Ca2+ transport and protein phosphorylation in cholinergic synaptic vesicles. , 1982, Proceedings of the National Academy of Sciences of the United States of America.

[7]  W. Catterall,et al.  Selective phosphorylation of the alpha subunit of the sodium channel by cAMP-dependent protein kinase. , 1982, The Journal of biological chemistry.

[8]  A. Means,et al.  Regulation of protein phosphorylation and motility of sperm by cyclic adenosine monophosphate and calcium. , 1982, Biology of reproduction.

[9]  D. Babcock,et al.  Purification and characterization of a calcium transport inhibitor protein from bovine seminal plasma. , 1982, The Journal of biological chemistry.

[10]  T. Chrisman,et al.  Activation of endogenous phosphorylase kinase in liver glycogen pellet by cAMP-dependent protein kinase. , 1980, The Journal of biological chemistry.

[11]  D. Garbers,et al.  Regulation of sea urchin sperm cyclic AMP-dependent protein kinases by an egg associated factor. , 1980, Biology of reproduction.

[12]  D. Babcock,et al.  Alteration of membrane permeability to calcium ions during maturation of bovine spermatozoa. , 1979, Developmental biology.

[13]  D. Babcock,et al.  Increased calcium-ion influx is a component of capacitation of spermatozoa. , 1978, The Biochemical journal.

[14]  E. Fischer,et al.  Isolation and properties of the bovine brain protein inhibitor of adenosine 3′:5′‐monophosphate‐dependent protein kinases , 1978, FEBS letters.

[15]  O. Rosen,et al.  Purification of a protein inhibitor of adenosine 3':5'-monophosphate-dependent protein kinase from bovine myocardium by a non-denaturing procedure. , 1977, Journal of cyclic nucleotide research.

[16]  A. Means,et al.  Isolation and characterization of a protein from rat testis which inhibits cyclic AMP-dependent protein kinase and phosdiesterase. , 1977, The Journal of biological chemistry.

[17]  T. Soderling,et al.  Regulation of adenosine 3',5'-monophosphate-dependent protein kinase. I. Preliminary characterization of the adipose tissue enzyme in crude extracts. , 1973, The Journal of biological chemistry.

[18]  E. Krebs,et al.  Purification and Characterization of a Protein Inhibitor of Adenosine 3',5'-Monophosphate-dependent Protein Kinases , 1971 .

[19]  U. K. Laemmli,et al.  Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.

[20]  Oliver H. Lowry,et al.  Protein measurement with the Folin phenol reagent. , 1951, The Journal of biological chemistry.

[21]  T. Mann,et al.  Male reproductive function and semen. , 1981 .

[22]  D. Garbers,et al.  The regulation of spermatozoa by calcium and cyclic nucleotides. , 1980 .