Arginine Induced Stimulation of Rabbit Sperm Motility

Radany, E. W.; Atherton, R. W.

doi:10.3109/01485018108999330

Cited by 9 publications

(7 citation statements)

References 10 publications

(6 reference statements)

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“…NOS have been immunolocalized in the acrosome and tail of human, mouse and bovine spermatozoa (Herrero et al, 1996;Meiser & Schulz, 2003). Incorporation of l-arginine in culture media stimulates the motility of human and rabbit spermatozoa (Keller & Polakoski, 1975;Randany & Atherton, 1981). l-Arginine also induces capacitation and acrosome reaction in boar and cryopreserved bull spermatozoa (Funahasi, 2002;O'Flaherty et al, 2004).…”

mentioning

confidence: 99%

Tyrosine phosphorylation of a 38‐kDa capacitation‐associated buffalo (Bubalus bubalis) sperm protein is induced by L‐arginine and regulated through a cAMP/PKA‐independent pathway

Roy

Atreja

2007

Int J of Andrology

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The aim of the present study was to determine the effect of L-arginine on nitric oxide (NO*) synthesis, capacitation and protein tyrosine phosphorylation in buffalo spermatozoa. Ejaculated buffalo spermatozoa were capacitated in the absence or presence of heparin, or L-arginine or N(omega)-nitro-L-arginine methyl ester (L-NAME), an inhibitor of nitric oxide synthase (NOS) for 6 h. Capacitating spermatozoa generated NO* both spontaneously and following stimulation with L-arginine and L-NAME quenched such L-arginine-induced NO* production. Immunolocalization of NOS suggested for existence of constitutive NOS in buffalo spermatozoa. L-Arginine (10 mm) was found to be a potent capacitating agent and addition of L-NAME to the incubation media attenuated both L-arginine and heparin-induced capacitation and suggested that NO* is involved in the capacitation of buffalo spermatozoa. Two sperm proteins of M(r) 38 000 (p38) and 20 000 (p20) were tyrosine phosphorylated extensively by both heparin and L-arginine. Of these, the tyrosine phosphorylation of p38 was insensitive to both induction by cAMP agonists as well as inhibition by a protein kinase A (PKA) inhibitor. Further, most of these L-arginine-induced tyrosine phosphorylated proteins were localized to the midpiece and principal piece regions of flagellum of capacitated spermatozoa and suggested that sperm flagellum takes active part during capacitation. These results indicated that L-arginine induces capacitation of buffalo spermatozoa through NO* synthesis and tyrosine phosphorylation of specific sperm proteins involving a pathway independent of cAMP/PKA.

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confidence: 99%

Tyrosine phosphorylation of a 38‐kDa capacitation‐associated buffalo (Bubalus bubalis) sperm protein is induced by L‐arginine and regulated through a cAMP/PKA‐independent pathway

Roy

Atreja

2007

Int J of Andrology

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“…These molecules act as chelating agents (especially of toxic metals), serve as oxidizable substrates for spermatozoa, provide buffers with protective influence on sperm cells, and undergo further metabolic changes in semen under the influence of transaminases and deaminases. Our results indicating the presence of arginine in goat cauda EF are highly implicated in its effect, in particular, stimulation of mammalian sperm motility in vitro (27)(28)(29), and in its beneficial effect on the sperm count for oligospermic semen after massive oral doses (30,31).…”

Section: Discussionmentioning

confidence: 93%

Identification of Low-Molecular-Weight Compounds in Goat Epididymis Using Multinuclear Nuclear Magnetic Resonance

Patel

Srivastava

Phadke

et al. 1999

Analytical Biochemistry

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“…When spermatozoa of the same species are stored in motility-inhibiting saline solution, motility can be improved by the addition of 50 mmol/l glycine in comparison with the control (He and Woods 2003). Arginine is known to increase the density and motility of spermatozoa in mammals when administered with the diet and the motility under in vitro incubation conditions (Radany andAtherton 1981, Sukardi et al 2006). Arginine serves as the sole substrate for nitric oxide synthesis, and its action on sperm might be via nitric oxide (Donnelly et al 1997).…”

Section: Discussionmentioning

confidence: 96%

“…Seminal fluid free amino acids stimulate the metabolic activity of spermatozoa (Patel et al 1998), increase the spermatozoa survival, and have detoxifying functions (Al-Hakim et al 1970;Ibrahim and Boldizsar 1981). Glycine (Llanos et al 2001;Sato et al 2000) and arginine (Radany and Atherton 1981;Patel et al 1998) increase the spermatozoa density and improve the motility or the acrosome reaction.…”

Section: Introductionmentioning

confidence: 95%

A comparative study on the composition and importance of free amino acids in semen of gilthead sea bream, Sparus aurata, and perch, Perca fluviatilis

Lahnsteiner

2010

Fish Physiol Biochem

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A comparative study was conducted on the free amino acid composition of gilthead sea bream, Sparus aurata, and perch, Perca fluviatilis. Also the effect of 21 free amino acids on sperm motility was investigated. Spermatozoa were incubated in species-specific motility-inhibiting saline solution containing the different amino acids for 48 h. Thereafter, the motility was activated and investigated using computer-assisted cell motility analysis. Twelve free amino acids, respectively, were detected in S. aurata and P. fluviatilis semen. Arginine, cysteine, glutamic acid, leucine, and methionine occurred in semen of both species. In S. aurata, arginine, glycine, hydroxyproline, lysine, and phenylalanine in concentrations of 1.25 and 2.50 mmol/l, methionine in a concentration of 2.5 mmol/l, and serine in a concentration of 1.25 mmol/l had a positive effect on the motility of spermatozoa. In P. fluviatilis, alanine, asparagine, cysteine, glycine, isoleucine, lysine, methionine, serine, threonine, and valine in concentrations of 2.50 mmol/l positively affected motility. From these data, it can be concluded that the amino acid composition and the effect on motility are species specific. Possible consequences for spermatozoa functionality are discussed.

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Arginine Induced Stimulation of Rabbit Sperm Motility

Cited by 9 publications

References 10 publications

Tyrosine phosphorylation of a 38‐kDa capacitation‐associated buffalo (Bubalus bubalis) sperm protein is induced by L‐arginine and regulated through a cAMP/PKA‐independent pathway

Tyrosine phosphorylation of a 38‐kDa capacitation‐associated buffalo (Bubalus bubalis) sperm protein is induced by L‐arginine and regulated through a cAMP/PKA‐independent pathway

Identification of Low-Molecular-Weight Compounds in Goat Epididymis Using Multinuclear Nuclear Magnetic Resonance

A comparative study on the composition and importance of free amino acids in semen of gilthead sea bream, Sparus aurata, and perch, Perca fluviatilis

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