title: Identification of the molecular chaperone, heat shock protein 1 (chaperonin 10), in the reproductive tract and in capacitating spermatozoa in the male mouse.
abstract: Mammalian spermatozoa must undergo epididymal maturation in the male reproductive tract and capacitation in the female tract before acquiring the ability to fertilize an oocyte. Previous studies from our laboratory have demonstrated a causal relationship between capacitation-associated surface phosphotyrosine expression and the ability of mouse spermatozoa to recognize the oocyte and engage in sperm-zona pellucida interaction. Our previous analyses of the surface phosphoproteome of capacitated murine spermatozoa identified two molecular chaperones, heat shock protein (HSP) D1 and HSP90B1, with well-characterized roles in protein folding and the assemblage of multimeric protein complexes. The expression of these chaperones was restricted to the rostral aspect of the sperm head, in an ideal position to mediate sperm-zona pellucida interaction. Herein, we report the characterization of an additional chaperone in this location, HSPE1 (chaperonin 10; HSP10). This chaperone was identified using a coimmunoprecipitation strategy employing HSPD1 as bait. The putative interaction between HSPE1 and HSPD1 was supported by reciprocal immunoprecipitation and colocalization studies, which demonstrated the coordinated appearance of both proteins on the surface of the sperm head during capacitation. However, the surface exposure of the protein was lost upon induction of acrosomal exocytosis, as would be expected of a protein potentially involved in sperm-zona pellucida interaction. Collectively, these data invite speculation that a number of molecular chaperones are involved in modification of the sperm surface during capacitation to render these cells functionally competent to engage the process of fertilization.
authors.affiliation: Reproductive Science Group, School of Environmental and Life Sciences, University of Newcastle, Callaghan, New South Wales 2308, Australia.
authors.forename: Andrew
authors.initials: A
authors.lastname: Walsh
authors.forename: Dean
authors.initials: D
authors.lastname: Whelan
authors.forename: Amanda
authors.initials: A
authors.lastname: Bielanowicz
authors.forename: Brooke
authors.initials: B
authors.lastname: Skinner
authors.forename: R John
authors.initials: RJ
authors.lastname: Aitken
authors.forename: Moira K
authors.initials: MK
authors.lastname: O'Bryan
authors.forename: Brett
authors.initials: B
authors.lastname: Nixon
mesh_terms: D020101:Acrosome Reaction / Q000502:physiology; D000818:Animals; D018835:Chaperonin 10 / Q000302:isolation & purification / Q000502:physiology*; D018834:Chaperonin 60 / Q000502:physiology; D004822:Epididymis / Q000378:metabolism; D005260:Female; D005306:Fertilization / Q000502:physiology; D047468:Immunoprecipitation; D008297:Male; D008562:Membrane Glycoproteins / Q000502:physiology; D051379:Mice; D013075:Sperm Capacitation / Q000502:physiology*; D013084:Sperm-Ovum Interactions / Q000502:physiology; D013094:Spermatozoa / Q000378:metabolism; D013737:Testis / Q000378:metabolism
chemical_list: D018835:Chaperonin 10; D018834:Chaperonin 60; D008562:Membrane Glycoproteins; C053387:endoplasmin