Regulation of bovine sperm motility and cyclic adenosine 3',5'- monophosphate by adenosine and its analogues

Vijayaraghavan, Srinivasan; Hoskins, Dale D.

doi:10.1095/biolreprod34.3.468

Cited by 51 publications

(48 citation statements)

References 4 publications

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“…A role in sperm adenosine transport appears unlikely since spermatozoa are reported not to take up adenosine from the medium (Brown & Casillas, 1984;Vijayaraghavan & Hoskins, 1986). However, in many tissues it provides a source of adenosine which acts as an intercellular messenger (reviewed by Berne et al, 1983).…”

Section: Methodsmentioning

confidence: 99%

“…However, in many tissues it provides a source of adenosine which acts as an intercellular messenger (reviewed by Berne et al, 1983). Spermatozoa appear to express stimulatory adenosine receptors on adenylate cyclase when uncapacitated and exogenous adenosine exerts positive effects on sperm function which result from an elevation of intracellular cAMP (Vijayaraghavan & Hoskins, 1986;Aitken et ai, 1986). Both extracellular production and metabolism of adenosine can occur in this in-vitro capacitation system and this may have important consequences for the development of fertilizing ability.…”

Section: Methodsmentioning

confidence: 99%

“…Recent evidence suggests that stimulatory adenosine receptors (A2) are expressed in uncapacitated but not in capacitated mouse spermatozoa . Adenosine and its analogues also exert a positive effect on sperm function, promoting sperm motility by elevating intracellular cAMP (Vijayaraghavan & Hoskins, 1986;Aitken et al, 1986). While extracellular adenosine affects cellular activity through receptors on adenylate cyclase, intracellular adenosine can influence several metabolic pathways (Fox & Kelley, 1978).…”

Section: Introductionmentioning

confidence: 99%

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Enzymes of adenosine metabolism in mouse sperm suspensions

Monks

Fraser²

1988

Reproduction

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Summary. The enzymes of adenosine metabolism were investigated in suspensions of epididymal mouse spermatozoa incubated under conditions which support capacitation in vitro. High levels of adenosine deaminase activity were found in sperm suspensions, but the enzyme was located in the surrounding medium and was not intrinsic to spermatozoa. 5\m='\-Nucleotidase was also present in the surrounding medium while in sperm cells it existed as an ecto-enzyme. Adenosine was not metabolized by washed spermatozoa under conditions used for the assay of adenosine deaminase or adenosine kinase, but it was metabolized rapidly by unwashed sperm suspensions. Incubation of sperm suspensions in conditions which modulate fertilizing ability resulted in small alterations in intrinsic 5\m='\-nucleotidase activity of spermatozoa. In contrast, the activity of adenosine deaminase was not consistently modulated by such maniupulations.Adenosine deaminase and 5\m='\-nucleotidase exhibited similar kinetic parameters to enzymes from other sources and their activities were inhibited by coformycin and \ g = a \ , \ g = b \ \ x = r e q -\ methylene adenosine 5\m='\-diphosphate, respectively. These studies highlight the low adenosine-metabolizing ability of spermatozoa coupled with the extensive metabolism in the medium which surrounds them. Extracellular adenosine metabolism can therefore occur and may modulate capacitation in vitro.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Enzymes of adenosine metabolism in mouse sperm suspensions

Monks

Fraser²

1988

Reproduction

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“…Adenosine is related to the acquisition of motility of sperm (Aitken et al, 1986;Vijayaraghavan and Hoskins, 1986), and nucleoside transport systems were characterized in rat epididymis epithelial cells (Leung et al, 2001). However, there is no information about nucleoside transport systems at the BTB, which is formed mainly by Sertoli cells.…”

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confidence: 99%

Nucleoside Transport at the Blood-Testis Barrier Studied with Primary-Cultured Sertoli Cells

Kato

Maeda

Akaike

et al. 2004

J Pharmacol Exp Ther

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Nucleosides are essential for nucleotide synthesis in testicular spermatogenesis. In the present study, the mechanism of the supply of nucleosides to the testicular system across the blood-testis barrier was studied using primary-cultured Sertoli cells from rats and TM4 cells from mice. Uptake of uridine by these cells was time-and concentration-dependent. Uridine uptake was decreased under Na ϩ -free conditions, and the system was presumed to be high affinity, indicating an Na ϩ -dependent concentrative nucleoside transporter (CNT) is involved. On the other hand, nitrobenzylthioinosine, a potent inhibitor of Na ϩ -independent equilibrative nucleoside transporters (ENTs), inhibited uridine uptake by the Sertoli cells in a concentration-dependent manner. Expression of nucleoside transporters ENT1, ENT2, ENT3, CNT1, CNT2, and CNT3 was detected in Sertoli cells by reverse transcriptase-polymerase chain reaction analysis. Inhibition studies of the uptake of uridine by various nucleosides both in the presence and absence of Na ϩ indicated that the most of those expressed nucleoside transporters, ENTs and CNTs, are involved functionally. These results demonstrated that Sertoli cells are equipped with multiple nucleoside transport systems, including ENT1, ENT2, and CNTs, to provide nucleosides for spermatogenesis.

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“…The efficiency of high levels of certain phosphodiesterase inhibitors in initiating motility of the immotile caput sperm is due to both their ability to elevate intrasperm cAMP levels and their efficacy as weak bases to increase intracellular pH [ 1241. Caudal sperm motility, on the other hand, can be stimulated by either an elevation of intracellular pH or an increase in cellular cAMP levels [125] [46]. Increases in intracellular pH are also involved in activation of sea urchin spermatozoa [76].…”

Section: Calcium Ion Camp and Intracellular Phmentioning

confidence: 99%

Biochemical Parameters of Initiation and Regulation of Sperm Motility

Majumder

Dey

Haldar

et al. 1990

Archives of Andrology

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Studies of in vitro models demonstrate that a forward motility protein (FMP) is required for the initiation of forward motility in the immature epididymal spermatozoa. FMP is a heat-stable glycoprotein derived from epididymal plasma. During the epididymal maturation of spermatozoa in vivo, there is a marked increase of intrasperm pH and level of cyclic adenosine monophosphate (CAMP). Several studies suggest that exogenous FMP in concert with elevated intrasperm pH and level of cAMP initiates flagellar motility during the epididymal transit of sperm. cAMP activates sperm cytosolic CAMPdependent protein kinases, which in turn phosphorylate multiple intrasperm phosphoproteins that may regulate flagellar motility. Exogenous calcium ion activates intact sperm motility, although it inhibits motility of demembranated cells on reactivation. Occurrence of CAMP-dependent type I and II protein kinases, a novel CAMP-independent protein kinase, and a phosphoprotein phosphatase has been demonstrated on the external surface of spermatozoa. The sperm surface has a coupled-enzyme system: ecto-CAMP-independent protein kinase and phosphoprotein phosphatase that regulate the phosphorylation and dephosphorylation of endogenous sperm ectophosphoproteins. The specific activities of these ectoenzymes increase markedly during forward progression, suggesting that they may have a role in regulating flagellar motility.

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Regulation of bovine sperm motility and cyclic adenosine 3',5'- monophosphate by adenosine and its analogues

Cited by 51 publications

References 4 publications

Enzymes of adenosine metabolism in mouse sperm suspensions

Enzymes of adenosine metabolism in mouse sperm suspensions

Nucleoside Transport at the Blood-Testis Barrier Studied with Primary-Cultured Sertoli Cells

Biochemical Parameters of Initiation and Regulation of Sperm Motility

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