Abstract
We report the initial biochemical characterization and the primary structure of a guinea pig sperm acrosomal pentaxin (apexin). Pentaxins are a family of penta- or decameric serum proteins that includes serum amyloid protein and C-reactive protein. Apexin consists of disulfide-linked 50-kDa subunits that give rise to an oligomeric protein. Apexin and a sperm protein related to complement receptors coelute with affinity-purified fertilin (PH-30), a potential sperm-egg membrane fusion protein. However, no evidence for a functional association of apexin with fertilin was found. Apexin is localized to the acrosome of mature guinea pig sperm and is thus the first pentaxin for which a defined intracellular localization has been reported. Whereas the C-terminal portion of apexin is clearly related to serum pentaxins, the N-terminal domain shows no strong homology to other known proteins. Northern blot analysis of different tissues revealed expression in the testis. Apexin is distinct from the pentaxins serum amyloid protein and C-reactive protein and may have evolved to perform functions other than those performed by serum pentaxins, such as intracellular protein sorting to the acrosome.
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