Involvement of protein tyrosine phosphorylation of human sperm in capacitation acrosome reaction and zona pellucida binding

10.2741/a126 ◽  
1996 ◽  
Vol 1 (4) ◽  
pp. d206-213 ◽  
Author(s):  
R. K Naz
Keyword(s):  
Tyrosine Phosphorylation ◽  
Zona Pellucida ◽  
Acrosome Reaction ◽  
Human Sperm ◽  
Protein Tyrosine Phosphorylation ◽  
Protein Tyrosine

scholarly journals KCNQ1 Potassium Channel Expressed in Human Sperm Is Involved in Sperm Motility, Acrosome Reaction, Protein Tyrosine Phosphorylation, and Ion Homeostasis During Capacitation

2021 ◽  
Vol 12 ◽  
Author(s):  
Tian Gao ◽  
Kun Li ◽  
Fei Liang ◽  
Jianmin Yu ◽  
Ajuan Liu ◽  
...  
Keyword(s):  
Membrane Potential ◽  
Potassium Channels ◽  
Tyrosine Phosphorylation ◽  
Sperm Motility ◽  
Western Blotting ◽  
Acrosome Reaction ◽  
Ion Homeostasis ◽  
Human Sperm ◽  
Protein Tyrosine Phosphorylation ◽  
Protein Tyrosine

Potassium channels are involved in membrane hyperpolarization and ion homeostasis regulation during human sperm capacitation. However, the types of potassium channels in human sperm remain controversial. The voltage-gated ion channel KCNQ1 is ubiquitously expressed and regulates key physiological processes in the human body. In the present study, we investigated whether KCNQ1 is expressed in human sperm and what role it might have in sperm function. The expression and localization of KCNQ1 in human sperm were evaluated using Western blotting and indirect immunofluorescence. During capacitation incubation, human sperm were treated with KCNQ1- specific inhibitor chromanol 293B. Sperm motility was analyzed using a computer-assisted sperm analyzer. The acrosome reaction was studied using fluorescein isothiocyanate-conjugated Pisum sativum agglutinin staining. Protein tyrosine phosphorylation levels and localization after capacitation were determined using Western blotting and immunofluorescence. Intracellular K+, Ca2+, Cl−, pH, and membrane potential were analyzed using fluorescent probes. The results demonstrate that KCNQ1 is expressed and localized in the head and tail regions of human sperm. KCNQ1 inhibition reduced sperm motility, acrosome reaction rates, and protein tyrosine phosphorylation but had no effect on hyperactivation. KCNQ1 inhibition also increased intracellular K+, membrane potential, and intracellular Cl−, while decreasing intracellular Ca2+ and pH. In conclusion, the KCNQ1 channel plays a crucial role during human sperm capacitation.

Luteinizing hormone modulates intracellular calcium, protein tyrosine phosphorylation and motility during human sperm capacitation

2017 ◽  
Vol 483 (2) ◽  
pp. 834-839 ◽  
Author(s):  
Aideé S. López-Torres ◽  
María E. González-González ◽  
Esperanza Mata-Martínez ◽  
Fernando Larrea ◽  
Claudia L. Treviño ◽  
...  
Keyword(s):  
Luteinizing Hormone ◽  
Intracellular Calcium ◽  
Tyrosine Phosphorylation ◽  
Human Sperm ◽  
Protein Tyrosine Phosphorylation ◽  
Sperm Capacitation ◽  
Protein Tyrosine

scholarly journals Cholecystokinin receptors regulate sperm protein tyrosine phosphorylation via uptake of HCO3−

Reproduction ◽  
2015 ◽  
Vol 150 (4) ◽  
pp. 257-268 ◽  
Author(s):  
Yuchuan Zhou ◽  
Yanfei Ru ◽  
Huijuan Shi ◽  
Yanjiao Wang ◽  
Bin Wu ◽  
...  
Keyword(s):  
Tyrosine Phosphorylation ◽  
Human Sperm ◽  
Peptide Hormone ◽  
Mature Sperm ◽  
Protein Tyrosine Phosphorylation ◽  
Sperm Capacitation ◽  
Protein Tyrosine ◽  
Cck Receptors ◽  
Cck2 Receptor

Cholecystokinin (CCK), a peptide hormone and a neurotransmitter, was detected in mature sperm two decades ago. However, the exact role of CCK and the types of CCK receptors (now termed CCK1 and CCK2) in sperm have not been identified. Here, we find that CCK1 and CCK2 receptors are immunolocalized to the acrosomal region of mature sperm. The antagonist of CCK1 or CCK2 receptor strongly activated the soluble adenylyl cyclase/cAMP/protein kinase A signaling pathway that drives sperm capacitation-associated protein tyrosine phosphorylation in dose- and time-dependent manners. But these actions of stimulation were abolished when sperm were incubated in the medium in the absence of HCO3−. Further investigation demonstrated that the inhibitor of CCK1 or CCK2 receptor could accelerate the uptake of HCO3−and significantly elevate the intracellular pH of sperm. Interestingly, the synthetic octapeptide of CCK (CCK8) showed the same action and mechanism as antagonists of CCK receptors. Moreover, CCK8 and the antagonist of CCK1 or CCK2 receptor were also able to accelerate human sperm capacitation-associated protein tyrosine phosphorylation by stimulating the influx of HCO3−. Thus, the present results suggest that CCK and its receptors may regulate sperm capacitation-associated protein tyrosine phosphorylation by modulating the uptake of HCO3−.

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