Biomaterial Database

Protein kinase C activity and protein phosphorylation in mouse sperm. 1991

Y Endo, and S Komatsu, and M Hirai, and S Suzuki, and N Shimizu

Department of Obstetrics and Gynecology, Keio University School of Medicine, Tokyo.

It has been suggested that the Ca2+ and phospholipid dependent protein kinase (protein kinase C; PKC) plays some intermediary roles in the regulation of the zona pellucida-induced acrosome reaction in mouse sperm. We here demonstrated that PKC activity is in the cytosol fraction of mouse sperm and that treatment of sperm with a PKC activator, 12-O-tetradecanoyl phorbol 13-acetate (TPA), induces translocation of PKC to the membrane fraction. Treatment of epididymal sperm with 20 ng/ml TPA or 20 microM of the Ca2+ ionophore A23187 did not induce any specific protein phosphorylation. However, two specific proteins, with molecular weights of 215 kDa and 35 kDa, were significantly phosphorylated when sperm were incubated with A23187 prior to TPA treatment. A similar synergistic effect of TPA and A23187 was observed in Ca2+ accumulation in sperm. We also demonstrated that exogenous PKC purified from human pancreatic cells catalyzes the phosphorylation of these two proteins in vitro as well. The present data support the idea that the activation of PKC and subsequent protein phosphorylation are involved in the regulation of the zona pellucida-induced acrosome reaction.

UI	MeSH Term	Description	Entries
D008297	Male		Males
D010743	Phospholipids	Lipids containing one or more phosphate groups, particularly those derived from either glycerol (phosphoglycerides see GLYCEROPHOSPHOLIPIDS) or sphingosine (SPHINGOLIPIDS). They are polar lipids that are of great importance for the structure and function of cell membranes and are the most abundant of membrane lipids, although not stored in large amounts in the system.	Phosphatides,Phospholipid
D010766	Phosphorylation	The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.	Phosphorylations
D011493	Protein Kinase C	An serine-threonine protein kinase that requires the presence of physiological concentrations of CALCIUM and membrane PHOSPHOLIPIDS. The additional presence of DIACYLGLYCEROLS markedly increases its sensitivity to both calcium and phospholipids. The sensitivity of the enzyme can also be increased by PHORBOL ESTERS and it is believed that protein kinase C is the receptor protein of tumor-promoting phorbol esters.	Calcium Phospholipid-Dependent Protein Kinase,Calcium-Activated Phospholipid-Dependent Kinase,PKC Serine-Threonine Kinase,Phospholipid-Sensitive Calcium-Dependent Protein Kinase,Protein Kinase M,Calcium Activated Phospholipid Dependent Kinase,Calcium Phospholipid Dependent Protein Kinase,PKC Serine Threonine Kinase,Phospholipid Sensitive Calcium Dependent Protein Kinase,Phospholipid-Dependent Kinase, Calcium-Activated,Serine-Threonine Kinase, PKC
D002118	Calcium	A basic element found in nearly all tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes.	Coagulation Factor IV,Factor IV,Blood Coagulation Factor IV,Calcium-40,Calcium 40,Factor IV, Coagulation
D003600	Cytosol	Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.	Cytosols
D005260	Female		Females
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D013084	Sperm-Ovum Interactions	Interactive processes between the oocyte (OVUM) and the sperm (SPERMATOZOA) including sperm adhesion, ACROSOME REACTION, sperm penetration of the ZONA PELLUCIDA, and events leading to FERTILIZATION.	Ovum-Sperm Interactions,Sperm Penetration,Egg-Sperm Interactions,Gamete Interactions,Oocyte-Sperm Interactions,Sperm-Egg Interactions,Sperm-Egg Penetration,Sperm-Oocyte Interactions,Sperm-Oocyte Penetration,Sperm-Ovum Penetration,Sperm-Zona Pellucida Penetration,Egg Sperm Interactions,Egg-Sperm Interaction,Gamete Interaction,Oocyte Sperm Interactions,Oocyte-Sperm Interaction,Ovum Sperm Interactions,Ovum-Sperm Interaction,Sperm Egg Interactions,Sperm Egg Penetration,Sperm Oocyte Interactions,Sperm Oocyte Penetration,Sperm Ovum Interactions,Sperm Ovum Penetration,Sperm Penetrations,Sperm Zona Pellucida Penetration,Sperm-Egg Interaction,Sperm-Egg Penetrations,Sperm-Oocyte Interaction,Sperm-Oocyte Penetrations,Sperm-Ovum Interaction,Sperm-Ovum Penetrations,Sperm-Zona Pellucida Penetrations
D013094	Spermatozoa	Mature male germ cells derived from SPERMATIDS. As spermatids move toward the lumen of the SEMINIFEROUS TUBULES, they undergo extensive structural changes including the loss of cytoplasm, condensation of CHROMATIN into the SPERM HEAD, formation of the ACROSOME cap, the SPERM MIDPIECE and the SPERM TAIL that provides motility.	Sperm,Spermatozoon,X-Bearing Sperm,X-Chromosome-Bearing Sperm,Y-Bearing Sperm,Y-Chromosome-Bearing Sperm,Sperm, X-Bearing,Sperm, X-Chromosome-Bearing,Sperm, Y-Bearing,Sperm, Y-Chromosome-Bearing,Sperms, X-Bearing,Sperms, X-Chromosome-Bearing,Sperms, Y-Bearing,Sperms, Y-Chromosome-Bearing,X Bearing Sperm,X Chromosome Bearing Sperm,X-Bearing Sperms,X-Chromosome-Bearing Sperms,Y Bearing Sperm,Y Chromosome Bearing Sperm,Y-Bearing Sperms,Y-Chromosome-Bearing Sperms