In vitro phosphorylation of sea urchin sperm adenylate cyclase by cyclic adenosine monophosphate-dependent protein kinase

1991 ◽  
Vol 28 (2) ◽  
pp. 150-157 ◽  
Author(s):  
Louis H. Bookbinder ◽  
Gary W. Moy ◽  
Victor D. Vacquier
Keyword(s):  
Protein Kinase ◽  
Adenylate Cyclase ◽  
Sea Urchin ◽  
Cyclic Adenosine Monophosphate ◽  
Adenosine Monophosphate ◽  
Dependent Protein Kinase ◽  
Dependent Protein ◽  
Sea Urchin Sperm

Crosstalk between protein kinases A and C regulates sea urchin sperm motility

Zygote ◽  
2021 ◽  
pp. 1-12
Author(s):  
Arlet Loza-Huerta ◽  
Hiram Pacheco-Castillo ◽  
Alberto Darszon ◽  
Carmen Beltrán
Keyword(s):  
Protein Kinase ◽  
Sperm Motility ◽  
Sea Urchin ◽  
Sea Urchins ◽  
Dependent Protein Kinase ◽  
Kinase C ◽  
Competitive Inhibitors ◽  
Motility Regulation ◽  
Dependent Protein ◽  
Sea Urchin Sperm

Summary Fertilization, a crucial event for species preservation, in sea urchins, as in many other organisms, requires sperm motility regulation. In Strongylocentrotus purpuratus sea urchins, speract, a sperm chemoattractant component released to seawater from the outer egg layer, attracts sperm after binding to its receptor in the sperm flagellum. Previous experiments performed in demembranated sperm indicated that motility regulation in these cells involved protein phosphorylation mainly due to the cAMP-dependent protein kinase (PKA). However, little information is known about the involvement of protein kinase C (PKC) in this process. In this work, using intact S. purpuratus sea urchin sperm, we show that: (i) the levels of both phosphorylated PKA (PKA substrates) and PKC (PKC substrates) substrates change between immotile, motile and speract-stimulated sperm, and (ii) the non-competitive PKA (H89) and PKC (chelerythrine) inhibitors diminish the circular velocity of sperm and alter the phosphorylation levels of PKA substrates and PKC substrates, while the competitive inhibitors Rp-cAMP and bisindolylmaleimide (BIM) do not. Altogether, our results show that both PKA and PKC participate in sperm motility regulation through a crosstalk in the signalling pathway. These results contribute to a better understanding of the mechanisms that govern motility in sea urchin sperm.

8-pCPT, an Epac activator, impairs conditioned place preference based on nucleus accumbens amphetamine in rats

2013 ◽  
Vol 26 (2) ◽  
pp. 104-111 ◽  
Author(s):  
Sung Woo Park ◽  
Ali Roohbakhsh ◽  
Richard J. Beninger
Keyword(s):  
Nucleus Accumbens ◽  
Protein Kinase ◽  
Dopamine Receptor ◽  
Conditioned Place Preference ◽  
Cyclic Adenosine Monophosphate ◽  
Adenosine Monophosphate ◽  
Place Preference ◽  
Dependent Protein Kinase ◽  
Cyclic Monophosphate ◽  
Dependent Protein

ObjectivesDopamine receptor-mediated 3′,5′-cyclic adenosine monophosphate (cAMP)-dependent intracellular signalling is important for reward-related learning. cAMP activates cAMP-dependent protein kinase (PKA) and exchange protein directly activated by cAMP (Epac). We tested the hypothesis that reward-related learning may be mediated by Epac.MethodsWe evaluated conditioned place preference (CPP) on the basis of nucleus accumbens (NAc) injections of amphetamine (20 μg/0.5 μl/side) plus Sp-adenosine 3′,5′-cyclic monophosphorothioate triethylamanine (Sp-cAMPS) (0.1, 1.0, 10, 15, 20 μg/0.5 μl/side), an activator of both PKA and Epac, or amphetamine (20 μg) plus 8-(4-chlorophenylthio)-2′-O-methyladenosine-3′,5′-cyclic monophosphate (8-pCPT) (0.73, 1.27, 1.45, 2.89, 5.78, 11.56 μg/0.5 μl/side), an activator of Epac.ResultsIn agreement with previous results, Sp-cAMPS dose-dependently impaired CPP. 8-pCPT impaired CPP at one dose (1.45 μg/0.5 μl/side) and we replicated this effect three times.ConclusionThe results implicate Epac in the acquisition of reward-related learning.

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