Abstract
Syntaxins are membrane integrated Q‐SNARE proteins known to participate in exocytosis. Vesicle docking involves the binding of two plasma membrane proteins, syntaxin and SNAP‐25, to the vesicle membrane protein VAMP to form a stable trimeric core complex; synaptophysin is thought to regulate the formation of this complex. Although the members of Q‐SNARE proteins are characterized in somatic cells, it is not known whether related proteins function in the sperm acrosome reaction. The objective of the present study is to identify and localize syntaxin and synaptophysin in bovine epididymal spermatozoa. Western blots of caput and cauda sperm lysates and plasma membrane fractions stained with anti‐syntaxin and anti‐synaptophysin showed the presence of a 31kDa and 38kDa band in both sperm lysates and plasma membrane fractions, respectively. Indirect immunofluorescence localized syntaxin to the anterior but not equatorial regions of the acrosomal segment. Syntaxin was recovered in the anti‐syntaxin immunoprecipitation pellet. Coimmunoprecipitation analysis will be utilized to identify the syntaxin‐associated protein(s) complex during capacitation and acrosome reaction of bovine spermatozoa. It is assumed that syntaxin‐2 and synaptophysin may be involved in triggering the acrosome reaction through a ligand‐receptor mediated signal transduction pathway. NIH 1SC3GM096875 and FSU‐RISE ‐ STEM Grants.
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