Proteomic changes in mammalian spermatozoa during epididymal maturation.
Epididymal maturation is associated with the activation of a cAMP-induced tyrosine phosphorylation cascade, which is ultimately associated with the expression of capacitation-dependent sperm functions, such as hyperactivated movement and acrosomal exocytosis. As spermatozoa progress through the epididymis they first acquire the capacity to phosphorylate tyrosine on targets on the principal piece, followed by the midpiece. By the time these cells have reached the cauda epididymidis they can phosphorylate the entire tail from neck to endpiece. This particular pattern of phosphorylation is associated with the ontogeny of fully functional spermatozoa that are capable of fertilizing the oocyte. Proteomic analyses indicate that this change is associated with the phosphorylation of several mitochondrial proteins, creation of a mitochondrial membrane potential and activation of mitochondrial free radical generation. At least in rodent species, activation of sperm mitochondria appears to be a particularly important part of epididymal maturation.
Aitken
R John
RJ
The ARC Centre of Excellence in Biotechnology and Development, University of Newcastle, Newcastle, NSW 2308, Australia. jaitken@mail.newcastle.edu.au
Nixon
Brett
B
Lin
Minjie
M
Koppers
Adam J
AJ
Lee
Yun H
YH
Baker
Mark A
MA
D020101:Acrosome Reaction; D000375:Aging; D000818:Animals; D004822:Epididymis / Q000254:growth & development / Q000502:physiology*; D006801:Humans; D008297:Male; D008322:Mammals; D051379:Mice; D020543:Proteome; D013075:Sperm Capacitation / Q000502:physiology*; D013094:Spermatozoa / Q000502:physiology*
D020543:Proteome