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Abstract
Voltage-dependent anion channel (VDAC) is mainly located in the mitochondrial outer membrane and participates in many biological processes. In mammals, three VDAC subtypes (VDAC1, 2 and 3) have been identified. Although VDAC has been extensively studied in various tissues and cells, there is little knowledge about the distribution and function of VDAC in male mammalian reproductive system. Several studies have demonstrated that VDAC exists in mammalian spermatozoa and is implicated in spermatogenesis, sperm maturation, motility and fertilization. However, there is no knowledge about the respective localization and function of three VDAC subtypes in human spermatozoa. In this study, we focused on the presence of VDAC2 in human spermatozoa and its possible role in the acrosomal integrity and acrosome reaction using specific anti-VDAC2 monoclonal antibody for the first time. The results exhibited that native VDAC2 existed in the membrane components of human spermatozoa. The co-incubation of spermatozoa with anti-VDAC2 antibody did not affect the acrosomal integrity and acrosome reaction, but inhibited ionophore A23187-induced intracellular Ca2+ increase. Our study suggested that VDAC2 was located in the acrosomal membrane or plasma membrane of human spermatozoa, and played putative roles in sperm functions through mediating Ca2+ transmembrane transport.
Highlights
Voltage-dependent anion channel (VDAC), as a membrane channel protein, is firstly identified in the mitochondrial outer membrane of Paramecium Aurelia [1,2]
To firstly assess the specificity of anti-VDAC2 monoclonal antibody used in our study, we observed the antibody reaction to three recombinant human VDAC proteins derived from the testis
We focused on the presence and functional role of VDAC2 in human spermatozoa
Summary
Voltage-dependent anion channel (VDAC), as a membrane channel protein, is firstly identified in the mitochondrial outer membrane of Paramecium Aurelia [1,2]. It has been discovered in the mitochondrial outer membrane of most eukaryotes [3]. VDAC is once thought to be only localized in the mitochondrial outer membrane [18,19] This protein is recently found in the plasma membrane or other non-mitochondrial cellular components, which implies that VDAC has more novel functions [20,21,22]
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