Proceedings: Relation of cyclic AMP to sperm motility

Reproduction ◽  
1973 ◽  
Vol 35 (3) ◽  
pp. 591-591 ◽  
Author(s):  
J Tash ◽  
T Mann
Keyword(s):  
1998 ◽  
Vol 10 (4) ◽  
pp. 299 ◽  
Author(s):  
Bijay S. Jaiswal ◽  
Gopal C. Majumder

An investigation was carried out to analyse the biochemical parameters influencing forward motility (FM) initiation in vitro in the goat caput-epididymal immature spermatozoa. Forward motility was induced in approximately 55% of caput-sperm upon incubation in an alkaline (pH 8.0) modified Ringer’s solution containing theophylline (30 mM) (an inhibitor of cyclic AMP phosphodiesterase), dialysed epi-didymal plasma (EP) and bicarbonate. Both EP and bicarbonate induced sperm motility in a dose-dependent manner, and at saturating doses EP (0.6 mg protein mL–1) and bicarbonate (25 mM) induced FM in approx-imately 38% and 44% of the cells, respectively. The motility-promoting efficacy of EP was attributed to a heat-stable protein termed ‘forward motility protein’ (FMP). Bicarbonate served as an initiator as well as a stabilizer of FM and its action was not dependent on FMP. FMP can induce FM in the caput-sperm, but it is not essential for sperm motility initiation. Alteration of the medium pH from 6.60 to 8.00 caused a marked increase in the EP or bicarbonate-dependent sperm FM initiation, as well as intrasperm pH. At the physio-logical pH, bicarbonate served as a much more potent motility activator than FMP, although both the motility promoters showed maximal efficacy at alkaline pH (~7.8). EP as well as bicarbonate elevated the intrasperm cyclic AMP level. Unlike EP, bicarbonate is capable of increasing intrasperm pH. The intrasperm pH increased from 6.54 0.02 to 6.77 0.03 during sperm transit from caput to cauda. The data are con-sistent with the view that FMP activates sperm forward motility by enhancing the intrasperm cyclic AMP level and that extracellular bicarbonate and pH play a vital role in the initiation of sperm FM during the epi-didymal transit.


1983 ◽  
Vol 6 (4) ◽  
pp. 337-348 ◽  
Author(s):  
Doriano Fabbro ◽  
Axel Jochum ◽  
Marco Balerna ◽  
Aldo Campana ◽  
Urs Eppenberger

1987 ◽  
Vol 29 (1) ◽  
pp. 47-56 ◽  
Author(s):  
KATSUMI ISHIDA ◽  
MAKOTO OKUNO ◽  
SACHIKO MORISAWA ◽  
TOSHIKO MOHRI ◽  
HIDEO MOHRI ◽  
...  
Keyword(s):  

Zygote ◽  
1999 ◽  
Vol 8 (S1) ◽  
pp. S59-S60 ◽  
Author(s):  
Mamoru Nomura ◽  
Kazuo Inaba ◽  
Masaaki Morisawa

Protein phosphorylation is highly coupled with sperm motility activation in several animal species. The micro-tubule based flagellar motor protein, dynein, is a candidate for a phosphoprotein related to sperm activation in many animal species (Morisawa & Hayashi, 1985; Hayashi et al., 1987; Dey & Brokaw, 1991; Stephens & Prior, 1992; Inaba et al., 1998, 1999). Sperm motility of the ascidians Ciona intestinalis and C. savignyi is activated by a factor derived from unfertilised eggs named sperm activating and attracting factor (SAAF). SAAF elevates the intracellular cyclic AMP (cAMP) level by a mechanism dependent on membrane hyperpolarisation and extracellular Ca2+ (Yoshida et al., 1994; Izumi et al., 1999). Experiments using demembranated Ciona sperm showed that cAMP is required prior to ATP for the activation of axonemal movement (Opreska & Brokaw, 1983; Morisawa et al., 1984; Brokaw, 1985; Dey & Brokaw, 1991; Chaudhry et al., 1995) and that many sperm flagellar proteins including dynein light chain are phosphorylated during incubation of demembranated sperm with ATP and cAMP (Dey & Brokaw, 1991). However, there is no evidence of which proteins are phosphorylated during the SAAF-dependent activation of Ciona sperm motility.


Reproduction ◽  
2007 ◽  
Vol 134 (4) ◽  
pp. 569-576 ◽  
Author(s):  
Fei Qu ◽  
Xiaoqian Ying ◽  
Wei Guo ◽  
Qiangsu Guo ◽  
Guowu Chen ◽  
...  

Sperm motility is essential for male reproduction or natural fertilization. The cyclic AMP (cAMP)/cAMP-dependent protein kinase A (PKA) signaling pathway is generally recognized as one of the significant signaling pathways in the regulation of mammalian spermatozoan motility. Since Zn-α2-glycoprotein (ZAG) activity in mammalian adipose tissue is mediated via the β3-adrenoreceptor, with upregulation of the cAMP pathway, we hypothesize that ZAG may play the same role in sperm motility regulation, a new factor of regulation of sperm motility. Therefore, the gene encoding human ZAG was cloned and polyclonal antibodies were generated, and then laser scanning confocal microscopy and flow cytometry were employed to identify this protein in human spermatozoa. The results showed that ZAG protein was mostly localized on the pre-equatorial region covering the acrosome, neck, and middle piece of the flagellum of spermatozoa. Furthermore, using computer-assisted sperm analysis, we found that anti-human ZAG antibodies could significantly reduce the motility of human swim-up spermatozoa after 90- or 120-min incubation (P<0.05 andP<0.01 respectively), together with the decreasing of intracellular cAMP and PKA levels. In conclusion, these data suggest that ZAG is present in human spermatozoa and may be involved in the regulation of sperm motility via the cAMP/PKA signaling pathway.


1984 ◽  
Vol 131 (6) ◽  
pp. 1255-1255
Author(s):  
D. Fabbro ◽  
A. Jochum ◽  
M. Balerna ◽  
A. Campana ◽  
U. Eppenberger

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