HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal My Folders Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Francavilla, F. Articles by Romano, R. Search for Related Content PubMed PubMed Citation Articles by Francavilla, F. Articles by Romano, R. Agricola Articles by Francavilla, F. Articles by Romano, R.

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

^a Department of Internal Medicine, Section of Andrology, University of L'Aquila, 67100 L'Aquila, Italy ^b Centro di Medicina della Riproduzione, 90141 Palermo, Italy

ABSTRACT

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 µM) 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.

FOOTNOTES

First decision: 10 December 1999.

¹ This work was supported by MURST-Italy, project "Glycobiology of fertilization" and by CARISPAQ, L'Aquila, Italy.

² Correspondence: Felice Francavilla, Dipartimento di Medicina Interna, Università de L'Aquila, Via S. Sisto 22/E, 67100 L'Aquila, Italy. FAX: 39 862 432858; francavi{at}cc.univaq.it

This article has been cited by other articles:

				J. Lapointe, M. Roy, I. St-Pierre, S. Kimmins, D. Gauvreau, L. A. MacLaren, and J.-F. Bilodeau Hormonal and Spatial Regulation of Nitric Oxide Synthases (NOS) (Neuronal NOS, Inducible NOS, and Endothelial NOS) in the Oviducts Endocrinology, December 1, 2006; 147(12): 5600 - 5610. [Abstract] [Full Text] [PDF]

				W.C.L. Ford Regulation of sperm function by reactive oxygen species Hum. Reprod. Update, September 1, 2004; 10(5): 387 - 399. [Abstract] [Full Text] [PDF]

				A. Revelli, D. Ghigo, F. Moffa, M. Massobrio, and I. Tur-Kaspa Guanylate Cyclase Activity and Sperm Function Endocr. Rev., August 1, 2002; 23(4): 484 - 494. [Abstract] [Full Text] [PDF]