PROTEIN-PHOSPHORYLATION REGULATES THE MOUSE SPERM ACROSOME REACTION INDUCED BY THE ZONA-PELLUCIDA

被引:13
作者
FURUYA, S [1 ]
ENDO, Y [1 ]
OBA, M [1 ]
MATSUI, Y [1 ]
NOZAWA, S [1 ]
SUZUKI, S [1 ]
机构
[1] KEIO UNIV,SCH MED,DEPT OBSTET & GYNECOL,35 SHINANOMACHI,SHINJUKU KU,TOKYO 160,JAPAN
关键词
MOUSE SPERM; ACROSOME REACTION; ZONA-PELLUCIDA; PROTEIN PHOSPHORYLATION; CHLORTETRACYCLINE FLUORESCENCE ASSAY;
D O I
10.1007/BF01203964
中图分类号
Q3 [遗传学];
学科分类号
071007 ; 090102 ;
摘要
Recently, the ligand-receptor signal transduction mechanism has been implicated in mediating the zona pellucida (ZP)-induced acrosome reaction. Little is known about the role of protein phosphorylation in this specific event. We examine whether modification of protein phosphorylation and dephosphorylation affects the kinetics of the acid-solubilized ZP-induced acrosome reaction of mouse sperm. Mouse epididymal sperm were incubated in modified Krebs-Ringer bicarbonate medium for a period of 90 to 120 min and then treated with 2 acid-solubilized ZP/mul for an additional 60 min. The chlortetracycline fluorescence assay was used to monitor the acrosome reaction. Capacitated sperm were inhibited from undergoing acid-solubilized ZP-induced acrosome reaction in the presence of an inhibitor of cyclic nucleotide-dependent protein kinase, H8; activators of the Ca2+- and phospholipid-dependent protein kinase (protein kinase C); an inhibitor of phosphatases 1 and 2A, okadaic acid; or an inhibitor of protein tyrosine kinases, genistein. The addition of inhibitors of protein kinase C, such as staurosporine, H7, and protein kinase C [19-36] pseudosubstrate, inhibited the phorbol ester-dependent inhibition of the acid-solubilized ZP-induced acrosome reaction. The present study suggests that protein phosphorylation and dephosphorylation play a regulatory role in the process of the ZP-induced acrosome reaction.
引用
收藏
页码:384 / 390
页数:7
相关论文
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