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Mol. Hum. Reprod. Advance Access originally published online on November 12, 2004
Molecular Human Reproduction 2005 11(1):43-51; doi:10.1093/molehr/gah126
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Molecular Human Reproduction vol. 11 no. 1 © European Society of Human Reproduction and Embryology 2004; all rights reserved

{alpha}-SNAP and NSF are required in a priming step during the human sperm acrosome reaction

C.N. Tomes1,3, G.A. De Blas1, M.A. Michaut1,2,4, E.V. Farré1, O. Cherhitin2, P.E. Visconti2,5 and L.S. Mayorga1

1Laboratorio de Biología Celular y Molecular, Instituto de Histología y Embriología (IHEM-CONICET), Facultad de Ciencias Médicas, CC 56, Universidad Nacional de Cuyo, 5500 Mendoza, Argentina, 2 Department of Cell Biology, Center for Recombinant Gamete Contraceptive Vaccinogens, University of Virginia, Room 3-101 Jordan Hall, 1300 Jefferson Park Ave, Charlottesville, VA 22903, USA

3 To whom correspondence should be addressed at: Laboratorio de Biología Celular y Molecular, Instituto de Histología y Embriología. Facultad de Ciencias Médicas. CC 56 Universidad Nacional de Cuyo, 5500 Mendoza, Argentina. Email: ctomes{at}fcm.uncu.edu.ar

The acrosome is a membrane-limited granule that overlies the nucleus of the mature spermatozoon. In response to physiological or pharmacological stimuli it undergoes a special type of Ca2+-dependent exocytosis termed the acrosome reaction (AR), which is an absolute prerequisite for fertilization. Aided by a streptolysin-O permeabilization protocol developed in our laboratory, we have previously demonstrated requirements for Rab3A, N-ethylmaleimide-sensitive factor (NSF), several soluble NSF-attachment protein receptor (SNARE) proteins, and synaptotagmin VI in the human sperm AR. Here, we show that {alpha}-soluble NSF-attachment protein ({alpha}-SNAP), a protein essential for most fusion events through its interaction with NSF and the SNARE complex, exhibits a direct role in the AR. First, the presence of {alpha}-SNAP is demonstrated by the Western blot of human sperm protein extracts. Immunostaining experiments reveal an acrosomal localization for this protein. Second, the Ca2+ and Rab3A-triggered ARs are inhibited by anti-{alpha}-SNAP antibodies. Third, bacterially expressed {alpha}-SNAP abolishes exocytosis in a fashion that depends on its interaction with NSF. Fourth, we show a requirement for {alpha}-SNAP/NSF in a prefusion step early in the exocytotic pathway, after the tethering of the acrosome to the plasma membrane and before the efflux of intra-acrosomal Ca2+. These results suggest a key role for {alpha}-SNAP/NSF in the AR, and strengthen our understanding of the molecular players involved in the vesicle-to-plasma membrane fusion taking place during exocytosis.

Key words: acrosome/exocytosis/NSF/{alpha}-SNAP/sperm

4Present address: Biology Department, 3749 Hamilton Walk, 224 Leidy Labs, University of Pennsylvania, Philadelphia, PA 191046018, USA

5Present address: 208 Paige Labs, Department of Veterinary and Animal Sciences, University of Massachusetts, Amherst, MA 01003, USA


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