The cAMP-Dependent Protein Kinase in Sea Urchin Sperm Tails: Association of the Enzyme with the Flagellar Axonemes

1990 ◽  
Vol 108 (1) ◽  
pp. 1-3 ◽  
Author(s):  
Etsuo Yokota ◽  
Issei Mabuchi
Keyword(s):  
Protein Kinase ◽  
Sea Urchin ◽  
Dependent Protein Kinase ◽  
Camp 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.

scholarly journals Evidence that cAMP-dependent protein kinase and a protein factor are involved in reactivation of triton X-100 models of sea urchin and starfish spermatozoa.

1982 ◽  
Vol 92 (3) ◽  
pp. 777-782 ◽  
Author(s):  
K Ishiguro ◽  
H Murofushi ◽  
H Sakai
Keyword(s):  
Protein Kinase ◽  
Sea Urchin ◽  
Kinase Inhibitor ◽  
Protein Kinase Inhibitor ◽  
Rabbit Muscle ◽  
Dependent Protein Kinase ◽  
Camp Dependent Protein Kinase ◽  
Protein Factor ◽  
Dependent Protein ◽  
Triton X

A fraction obtained from detergent-extract of sea urchin or starfish spermatozoa using DEAE-cellulose chromatography reactivated Triton X-100 models of the spermatozoa in a cAMP-dependent manner. The DEAE fraction contained cAMP-dependent protein kinase with a high level of specific activity. Rabbit muscle inhibitor protein highly specific for cAMP-dependent protein kinases inhibited the ability of the deae fraction to induce reactivation of Triton X-100 models.l This inhibition paralleled inhibition of cAMP-dependent protein kinase activity of the DEAE fraction, suggesting participation of the enzyme in the cAMP-dependent reactivation of Triton X-100 models. However, cAMP-dependent protein kinase further purified from the DEAE fraction was incapable of reactivating these models by itself. A protein factor which was separated from the protein kinase in the course of purification of the enzyme was found to also be necessary for the reactivation. When cAMP-dependent protein kinase was pretreated with protein kinase inhibitor before addition of the protein factor, the reactivation of Triton X-100 models was no longer detected. However, after the protein factor had been incubated with cAMP and cAMP-dependent protein kinase, protein kinase inhibitor did not repress reactivation of Triton X-100 models. We propose that the reactivation needs phosphorylation of the protein factor by cAMP-dependent protein kinase.

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