Sodium bicarbonate in seminal plasma stimulates the motility of mammalian spermatozoa through direct activation of adenylate cyclase.
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Results show that the bicarbonate-sensitive adenylate cyclase system regulates sperm motility and suggest that this system is common to all mammals.About:
This article is published in Journal of Biological Chemistry.The article was published on 1985-08-15 and is currently open access. It has received 403 citations till now. The article focuses on the topics: Cyclase activity & Sperm motility.read more
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Journal ArticleDOI
Capacitation of mouse spermatozoa. II. Protein tyrosine phosphorylation and capacitation are regulated by a cAMP-dependent pathway.
Pablo E. Visconti,Grace D. Moore,Janice L. Bailey,P. Leclerc,Stephanie A. Connors,Dieyun Pan,Patricia Olds-Clarke,Gregory S. Kopf +7 more
TL;DR: Up-regulation of protein tyrosine phosphorylation by cAMP/PKA in sperm is, to the authors' knowledge, the first demonstration of such an interrelationship between tyrosin kinase/phosphatase and PKA signaling pathways.
Journal ArticleDOI
Dynamics of the mammalian sperm plasma membrane in the process of fertilization.
TL;DR: Dynamics in adhesive and fusion properties, molecular composition and architecture of the sperm plasma membrane, as well as membrane derived signalling are reviewed.
Journal ArticleDOI
Regulation of protein phosphorylation during sperm capacitation
TL;DR: Capacitation in vitro has been accomplished using cauda and/or ejaculated sperm incubated under a variety of conditions in defined media that mimic the electrolyte composition of the oviduct fluid, and the action of these media components to promote capacitation at the molecular level is poorly understood.
Journal ArticleDOI
Regulation of Protein Tyrosine Phosphorylation during Bovine Sperm Capacitation by a Cyclic Adenosine 3',5'-Monophosphate-Dependent Pathway
TL;DR: These studies are the first to report a unique interrelationship between tyrosine kinase/phosphatase and cAMP signaling pathways at the level of PK-A in bovine sperm capacitation.
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Cyclic adenosine 3',5'monophosphate-dependent regulation of protein tyrosine phosphorylation in relation to human sperm capacitation and motility.
TL;DR: Results suggest that divergent pathways might regulate tyrosine phosphorylation of p105 and p81 and sperm capacitation after cAMP-dependent phosphorylations of an intermediate protein, and suggest that protein phosphatase PP1 is involved in the two latter phenomena while PP2A mediates sperm capacitations.
References
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Journal Article
Protein Measurement with the Folin Phenol Reagent
TL;DR: Procedures are described for measuring protein in solution or after precipitation with acids or other agents, and for the determination of as little as 0.2 gamma of protein.
Book
The biochemistry of semen and of the male reproductive tract.
TL;DR: Bromural, Its Distribution and Decomposition In the Animal Organism, and its Differential Diagnosis from Neurological Disorders, Acta Neurol.
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Cyclic adenosine 3',5' monophosphate, calcium and protein phosphorylation in flagellar motility.
Joseph S. Tash,Anthony R. Means +1 more
TL;DR: The identification of cAMP-dependent protein kinase, calmodulin and myosin light chain kinase in the sperm head suggests that cAMP and calcium-dependent phosphorylations are also involved in the control of the fertilization process, i.e., the acrosome reaction, in a manner similar to that known for theControl of stimulus/secretion coupling.
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Regulation of protein phosphorylation and motility of sperm by cyclic adenosine monophosphate and calcium.
Joseph S. Tash,Anthony R. Means +1 more
TL;DR: The regulation of flagellar motility in cAMP and calcium includes mechanisms involving the control of the phosphorylation state of sperm proteins, some of which may be axonemal components.
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The activation of motility in quiescent hamster sperm from the epididymis by calcium and cyclic nucleotides.
TL;DR: It appears that sperm are quiescent on the male because they lack cAMP, and that calcium, supplied at ejaculation, initiates rapid cAMP synthesis to produce motility.