The nitric oxide synthase of mouse spermatozoa

Herrero, Marı́a Belén; Goin, Juan Carlos; Boquet, M.; Canteros, M. Griselda; Franchi, A; Martı́nez, Silvina Pérez; Polak, Julia M.; Viggiano, J.M.; Gimeno, M.F.

doi:10.1016/s0014-5793(97)00570-x

Cited by 35 publications

(20 citation statements)

References 30 publications

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“…An immunoreactivity for cNOS was observed in mouse [16] and human sperm [16][17][18]. In mouse sperm, a NOS isoform was revealed at Western blot analysis as a unique band of M r ϭ 140 kDa, recognized by both eNOS and bNOS antibodies [19] and more recently, in human sperm, as a band of M r ϭ 145 kDa, recognized by eNOS antibodies [20]. The ability of sperm to synthesize NO during in vitro capacitation was demonstrated in the mouse by measuring L-[ 14 C]citrulline generation [19] and in man, by measuring nitrite accumulation [17] as well as L-[ 3 H]citrulline generation [20]; in the mouse, L-[ 14 C]citrulline generation was inhibited by L-NAME in a dose-dependent manner [19].…”

Section: Introductionmentioning

confidence: 99%

Nitric Oxide Synthase Inhibition in Human Sperm Affects Sperm-Oocyte Fusion but Not Zona Pellucida Binding1

Francavilla

Santucci

Macerola

et al. 2000

Biology of Reproduction

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There is recent evidence that mouse and human spermatozoa contain constitutive nitric oxide synthase (cNOS) and can synthesize nitric oxide. The aim of this study was to investigate whether the inhibition of human sperm cNOS could affect sperm-oocyte fusion and sperm binding to the zona pellucida (ZP). N(G)-nitro-L-arginine methyl ester (L-NAME) was used as cNOS inhibitor. Sperm-oocyte fusion was evaluated using the hamster egg penetration test (HEPT). The ZP binding was evaluated using the hemizona assay. L-NAME added from the onset of capacitation strongly inhibited sperm-oocyte fusion. This inhibitory effect was dose dependent, stereospecific, and suppressed by L-arginine in a dose-dependent manner. L-NAME also inhibited sperm-oocyte fusion in the HEPT enhanced with progesterone (P), where P (5 microM) was added for 15 min to capacitated sperm. A lesser but significant inhibition was also observed when sperm suspensions were exposed to L-NAME following capacitation in both versions of HEPT. On the contrary, L-NAME did not affect ZP binding. In conclusion, the present study provides the evidence that cNOS plays a role in the human sperm's capacity to fuse with oocyte but not in the ZP binding.

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Section: Introductionmentioning

confidence: 99%

Nitric Oxide Synthase Inhibition in Human Sperm Affects Sperm-Oocyte Fusion but Not Zona Pellucida Binding1

Francavilla

Santucci

Macerola

et al. 2000

Biology of Reproduction

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“…Thus nitric oxide appears to be crucial for the processes driving successful fertilization (reviewed in [46,47]). NOS isoforms were found in sperm of different mammal species such as mice [48], bulls [49], boars [50], and humans [51]. The abovementioned and well-known duality of NO's effects, depending upon concentrations, was also described in spermatozoa.…”

Section: No Roles In Spermatozoamentioning

confidence: 88%

From Nitric Oxide Toward S-Nitrosylation: Expanding Roles in Gametes and Embryos

Ješeta¹,

Sedmı́ková²,

Bodart³

2017

Nitric Oxide Synthase - Simple Enzyme-Complex Roles

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Nitric oxide (NO) is a gasotransmitter involved in various aspects of reproduction. The observational data from different species, such as sea urchin, ascidians, amphibians, rodents, porcine, bovine, and human, suggest that NO might have a significant role in reproduction through several mechanisms. This proposed role might appear preserved through evolution; however, the effects of NO also depend on the species or stages considered. There has been debate over the physiological relevance of NO, though the benefits of its use in assisted reproduction are now widely recognized. Over the past years, S-nitrosylation has provided a new angle to decipher the mechanisms through which NO exerts its actions. This chapter summarizes, in a nonexhaustive manner, research that explores the role of NO in gametes and embryos.

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“…Herrero et al [29] showed that mouse spermatozoa can synthesize L-citrulline, depending on the concentration of L-arginine present in the incubation medium while different concentrations of N(G)-nitro-L-arginine methyl ester (L-NAME) inhibit the formation of the amino acid. Furthermore, when sperm protein extracts were incubated under denaturing and nonreducing conditions and then subjected to immunoblotting assay, a protein fraction of 140 kDa was recognized by the three anti-NOS antibodies.…”

Section: Nos/no Duo In the Reproductive Systemmentioning

confidence: 99%

Nitric Oxide: Key Features in Spermatozoa

Staicu¹,

Parra²

2017

Nitric Oxide Synthase - Simple Enzyme-Complex Roles

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Several in vitro studies have pointed to the importance of nitric oxide (NO) in the female and male reproductive system in mammals. Its functions vary from preventing oocyte aging, improving the integrity of the microtubular spindle apparatus in aged oocytes, modulating the contraction of the oviduct, to regulating sperm physiology by affecting the motility, inducing chemotaxis in spermatozoa, regulating tyrosine phosphorylation, enhancing the sperm-zona pellucida binding ability, and modulating the acrosomal reaction. In spermatozoa, NO exerts its functions in different ways, which involve key elements such as the soluble isoform of guanylate cyclase, cyclic guanosine monophosphate (cGMP), cyclic adenosine monophosphate (cAMP), protein kinase A (PKA), adenylate cyclase, and the extracellular signal-regulated kinase (ERK) pathway. Furthermore, NO leads to the S-nitrosylation of several sperm proteins, among them a substantial group associated with energy generation and cell movement, but also with signal transduction, suggesting a role for S-nitrosylation in sperm motility and in modulating the sperm function, respectively. In this chapter, an overview of how NO modulates the sperm physiology is presented, based on the knowledge acquired to this day.

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The nitric oxide synthase of mouse spermatozoa

Cited by 35 publications

References 30 publications

Nitric Oxide Synthase Inhibition in Human Sperm Affects Sperm-Oocyte Fusion but Not Zona Pellucida Binding1

Nitric Oxide Synthase Inhibition in Human Sperm Affects Sperm-Oocyte Fusion but Not Zona Pellucida Binding1

From Nitric Oxide Toward S-Nitrosylation: Expanding Roles in Gametes and Embryos

Nitric Oxide: Key Features in Spermatozoa

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