Journal article
Structure and function of epididymal protein cysteine-rich secretory protein-1
Asian journal of andrology, Vol.9(4), pp.508-514
07/2007
Handle:
https://hdl.handle.net/2376/108009
PMID: 17589788
Abstract
Cysteine-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.
Metrics
10 Record Views
Details
- Title
- Structure and function of epididymal protein cysteine-rich secretory protein-1
- Creators
- Kenneth P Roberts - Department of Urologic Surgery, University of Minnesota, MMC 394, 420 Delaware Street SE, Minneapolis, MN 55455, USA. rober040@umn.eduDaniel S JohnstonMichael A NolanJoseph L WootersNicole C WaxmonskyLaura B PiehlKathy M Ensrud-BowlinDavid W Hamilton
- Publication Details
- Asian journal of andrology, Vol.9(4), pp.508-514
- Academic Unit
- Elson S. Floyd College of Medicine
- Publisher
- China
- Grant note
- HD11962 / NICHD NIH HHS
- Identifiers
- 99900546844701842
- Language
- English
- Resource Type
- Journal article