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Structure and function of epididymal protein cysteine-rich secretory protein-1 Roberts KP; Johnston DS; Nolan MA; Wooters JL; Waxmonsky NC; Piehl LB; Ensrud-Bowlin KM; Hamilton DWAsian J Androl 2007[Jul]; 9 (4): 508-14Cysteine-rich secretory protein-1 (CRISP-1) is a glycoprotein secreted by the epididymal epithelium. It is a member of a large family of proteins characterized by two conserved domains and a set of 16 conserved cysteine residues. In mammals, CRISP-1 inhibits sperm-egg fusion and can suppress sperm capacitation. The molecular mechanism of action of the mammalian CRISP proteins remains unknown, but certain non-mammalian CRISP proteins can block ion channels. In the rat, CRISP-1 comprises two forms referred to as Proteins D and E. Recent work in our laboratory demonstrates that the D form of CRISP-1 associates transiently with the sperm surface, whereas the E form binds tightly. When the spermatozoa are washed, the E form of CRISP-1 persists on the sperm surface after all D form has dissociated. Cross-linking studies demonstrate different protein-protein interaction patterns for D and E, although no binding partners for either protein have yet been identified. Mass spectrometric analyses revealed a potential post-translational modification on the E form that is not present on the D form. This is the only discernable difference between Proteins D and E, and presumably is responsible for the difference in behavior of these two forms of rat CRISP-1. These studies demonstrate that the more abundant D form interacts with spermatozoa transiently, possibly with a specific receptor on the sperm surface, consistent with a capacitation-suppressing function during sperm transit and storage in the epididymis, and also confirm a tightly bound population of the E form that could act in the female reproductive tract.|Amino Acid Sequence[MESH]|Animals[MESH]|Conserved Sequence[MESH]|Humans[MESH]|Male[MESH]|Mammals[MESH]|Membrane Glycoproteins/*genetics/metabolism[MESH]|Molecular Sequence Data[MESH]|Rats[MESH]|Spermatozoa/*physiology[MESH] |
