Acrosome membrane associated protein kinase activity in hamster spermatozoa

Acrosomal membranes isolated from the caput and cauda epididymal spermatozoa of hamster exhibited protein kinase activity and the endogenous protein substrates that were phosphorylated in the acrosomal membranes of caput and cauda spermatozoa were not all the same. The kinase activity was identified...

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Bibliographic Details
Published in:FEBS letters 1996-11, Vol.396 (2), p.123-126
Main Authors: Devi, K.Uma, Ahmad, M.Basheer, Shivaji, S.
Format: Article
Language:English
Subjects:
1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine - pharmacology
Acrosomal membrane
Acrosome - enzymology
Animals
Cricetinae
Cyclic AMP - pharmacology
Enzyme Inhibitors - pharmacology
Epididymis
Genistein
Hamster spermatozoa
Heparin - pharmacology
Isoflavones - pharmacology
Male
Membrane protein
Membrane Proteins - metabolism
Phosphorylation
Phosphotyrosine - metabolism
Protein kinase
Protein-Tyrosine Kinases - antagonists & inhibitors
Protein-Tyrosine Kinases - metabolism
Sperm maturation
Spermidine - pharmacology
Spermine - pharmacology
Tyrosine specific protein kinase
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Summary:Acrosomal membranes isolated from the caput and cauda epididymal spermatozoa of hamster exhibited protein kinase activity and the endogenous protein substrates that were phosphorylated in the acrosomal membranes of caput and cauda spermatozoa were not all the same. The kinase activity was identified as a cAMP independent type and the use of specific stimulators and inhibitors indicated that the activity was not due to casein kinase, protein kinase A or protein kinase C but due to a tyrosine specific protein kinase that was not inhibited by Genistein. Phosphotyrosine was identified as the predominant phosphorylated residue in the proteins.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(96)01077-0