The calcium‐sensing receptor regulates protein tyrosine phosphorylation through PDK1 in boar spermatozoa

2019 ◽  
Vol 86 (7) ◽  
pp. 751-761 ◽  
Author(s):  
Beatriz Macías‐García ◽  
Luis J. García‐Marín ◽  
María J. Bragado ◽  
Lauro González‐Fernández
Keyword(s):  
Tyrosine Phosphorylation ◽  
Protein Tyrosine Phosphorylation ◽  
Calcium Sensing Receptor ◽  
Protein Tyrosine ◽  
Calcium Sensing ◽  
Boar Spermatozoa

Quantification of kinetic changes in protein tyrosine phosphorylation and cytosolic Ca2+ concentration in boar spermatozoa during cryopreservation

2012 ◽  
Vol 24 (4) ◽  
pp. 531 ◽  
Author(s):  
A. Kumaresan ◽  
A. P. Siqueira ◽  
M. S. Hossain ◽  
A. Johannisson ◽  
I. Eriksson ◽  
...  
Keyword(s):  
Intracellular Calcium ◽  
Tyrosine Phosphorylation ◽  
Mammalian Species ◽  
Protein Tyrosine Phosphorylation ◽  
Protein Tyrosine ◽  
Quantitative Evidence ◽  
Phosphorylated Proteins ◽  
Straight Line ◽  
Cryopreserved Sperm ◽  
Boar Spermatozoa

Protein tyrosine phosphorylation in sperm is associated with capacitation in several mammalian species. Although tyrosine phosphorylated proteins have been demonstrated in cryopreserved sperm, indicating capacitation-like changes during cryopreservation, these changes have not yet been quantified objectively. We monitored tyrosine phosphorylation, intracellular calcium and sperm kinematics throughout the cryopreservation process, and studied the relationships among them in boar spermatozoa. Sperm kinetics changed significantly during cryopreservation: curvilinear velocity, average path velocity and straight line velocity all decreased significantly (P < 0.05). While the percentage of sperm with high intracellular calcium declined (P < 0.05), global phosphorylation increased significantly (P < 0.01). Specifically, cooling to 5°C induced phosphorylation in the spermatozoa. After cooling, a 32-kDa protein not observed in fresh semen appeared and was consistently present throughout the cryopreservation process. While the level of expression of this phosphoprotein decreased after addition of the second extender, frozen–thawed spermatozoa showed an increased expression. The proportion of sperm cells with phosphorylation in the acrosomal area also increased significantly (P < 0.05) during cryopreservation, indicating that phosphorylation might be associated with capacitation-like changes. These results provide the first quantitative evidence of dynamic changes in the subpopulation of boar spermatozoa undergoing tyrosine phosphorylation during cryopreservation.

scholarly journals Angiotensin II-induced protein tyrosine phosphorylation in neonatal rat cardiac fibroblasts.

1994 ◽  
Vol 269 (30) ◽  
pp. 19626-19632
Author(s):  
W. Schorb ◽  
T.C. Peeler ◽  
N.N. Madigan ◽  
K.M. Conrad ◽  
K.M. Baker
Keyword(s):  
Angiotensin Ii ◽  
Tyrosine Phosphorylation ◽  
Cardiac Fibroblasts ◽  
Neonatal Rat ◽  
Protein Tyrosine Phosphorylation ◽  
Protein Tyrosine
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