| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
|
|
|
|||||||
|
|||||||||
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reactive oxygen species (superoxide anion, hydrogen peroxide, and nitric oxide) are involved in human sperm capacitation and associated tyrosine phosphorylation through a cAMP- and protein kinase A-mediated pathway. Recently we evidenced the double phosphorylation of the Threonine-Glutamine-Tyrosine motif (P-Thr-Glu-Tyr-P) in human sperm proteins of 80 and 105 kDa during capacitation. The objective of this study was to investigate the role of reactive oxygen species in the regulation of this process and immunolocalize the P-Thr-Glu-Tyr-P motif in human spermatozoa. Superoxide dismutase and catalase did not prevent, and exogenous addition of superoxide anion or hydrogen peroxide did not trigger, the increase in P-Thr-Glu-Tyr-P related to sperm capacitation. However, L-NAME (a competitive inhibitor of L-arginine for nitric oxide synthase) prevented, and a nitric oxide donor promoted, the increase in P-Thr-Glu-Tyr-P related to sperm capacitation. In addition, L-arginine reversed the inhibitory effect of L-NAME on capacitation and associated increase of P-Thr-Glu-Tyr-P. Therefore, the regulation of P-Thr-Glu-Tyr-P is specific to nitric oxide and not to superoxide anion or hydrogen peroxide. The nitric oxide-mediated increase of P-Thr-Glu-Tyr-P involved protein tyrosine kinase, MEK, or MEK-like kinases and protein kinase C but not protein kinase A. The P-Thr-Glu-Tyr-P motif was immunolocalized to the principal piece region of spermatozoa. In conclusion, nitric oxide regulates the level of P-Thr-Glu-Tyr-P in sperm proteins of 80 and 105 kDa during capacitation. These data evidence for the first time a specific role for nitric oxide in signal transduction events leading to sperm capacitation.
This article has been cited by other articles:
|
|
 |
|
  G. Machado-Oliveira, L. Lefievre, C. Ford, M. B. Herrero, C. Barratt, T. J. Connolly, K. Nash, A. Morales-Garcia, J. Kirkman-Brown, and S. Publicover Mobilisation of Ca2+ stores and flagellar regulation in human sperm by S-nitrosylation: a role for NO synthesised in the female reproductive tract Development, November 15, 2008; 135(22): 3677 - 3686. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 C. O'Flaherty, E. de Lamirande, and C. Gagnon Reactive Oxygen Species and Protein Kinases Modulate the Level of Phospho-MEK-Like Proteins During Human Sperm Capacitation Biol Reprod, July 1, 2005; 73(1): 94 - 105. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 L. Liguori, E. de Lamirande, A. Minelli, and C. Gagnon Various protein kinases regulate human sperm acrosome reaction and the associated phosphorylation of Tyr residues and of the Thr-Glu-Tyr motif Mol. Hum. Reprod., March 1, 2005; 11(3): 211 - 221. [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]
|
|
|
|
|
|
J. Seligman, Y. Zipser, and N. S. Kosower Tyrosine Phosphorylation, Thiol Status, and Protein Tyrosine Phosphatase in Rat Epididymal Spermatozoa Biol Reprod, September 1, 2004; 71(3): 1009 - 1015. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
B. Willipinski-Stapelfeldt, J. Lubberstedt, S. Stelter, K. Vogt, A. K. Mukhopadhyay, and D. Muller Comparative analysis between cyclic GMP and cyclic AMP signalling in human sperm Mol. Hum. Reprod., July 1, 2004; 10(7): 543 - 552. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
C. O'Flaherty, E. de Lamirande, and C. Gagnon Phosphorylation of the Arginine-X-X-(Serine/Threonine) motif in human sperm proteins during capacitation: modulation and protein kinase A dependency Mol. Hum. Reprod., May 1, 2004; 10(5): 355 - 363. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
