Control of flatfish sperm motility by CO2 and carbonic anhydrase
Identifieur interne : 001290 ( Main/Merge ); précédent : 001289; suivant : 001291Control of flatfish sperm motility by CO2 and carbonic anhydrase
Auteurs : Kazuo Inaba [Japon] ; Catherine Dréanno [France] ; Jacky Cosson [France]Source :
- Cell Motility and the Cytoskeleton [ 0886-1544 ] ; 2003-07.
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Abstract
Sperm motility in flatfishes shows unique characteristics. The flagellar movement either in vivo or in permeabilized models is arrested by the presence of 25–100 mM HCO3−, or by gentle perfusion with CO2 gas. To understand the molecular basis of this property, sperm Triton‐soluble proteins and flagellar proteins from several species were analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis. An abundant 29‐kDa protein was observed only in flatfish species. Partial amino acid sequences identified this protein as a carbonic anhydrase, an enzyme involved in the interconversion of CO2 and HCO3−. 6‐ethoxyzolamide, a specific inhibitor of carbonic anhydrase inhibits sperm motility, especially at low pH. In the case of HCO3−‐arrested sperm, the motility is restored by addition of 6‐ethoxyzolamide. Taken together, these results suggest that a novel pH/ HCO3−‐dependent regulatory mechanism mediated by carbonic anhydrase is involved in the motility control in flatfish sperm. Cell Motil. Cytoskeleton 55:174–187, 2003. © 2003 Wiley‐Liss, Inc.
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DOI: 10.1002/cm.10119
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Cytoskeleton</title><idno type="ISSN">0886-1544</idno><idno type="eISSN">1097-0169</idno><imprint><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><date type="published" when="2003-07">2003-07</date><biblScope unit="volume">55</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="174">174</biblScope><biblScope unit="page" to="187">187</biblScope></imprint><idno type="ISSN">0886-1544</idno></series><idno type="istex">F7E079A96CC9E5B71BB8D28415B527BECE7BC3E6</idno><idno type="DOI">10.1002/cm.10119</idno><idno type="ArticleID">CM10119</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0886-1544</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>creatine kinase</term><term>ethoxyzolamide</term><term>flounder</term><term>sperm axoneme</term><term>teleost flagella</term><term>turbot</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Sperm motility in flatfishes shows unique characteristics. The flagellar movement either in vivo or in permeabilized models is arrested by the presence of 25–100 mM HCO3−, or by gentle perfusion with CO2 gas. To understand the molecular basis of this property, sperm Triton‐soluble proteins and flagellar proteins from several species were analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis. An abundant 29‐kDa protein was observed only in flatfish species. Partial amino acid sequences identified this protein as a carbonic anhydrase, an enzyme involved in the interconversion of CO2 and HCO3−. 6‐ethoxyzolamide, a specific inhibitor of carbonic anhydrase inhibits sperm motility, especially at low pH. In the case of HCO3−‐arrested sperm, the motility is restored by addition of 6‐ethoxyzolamide. Taken together, these results suggest that a novel pH/ HCO3−‐dependent regulatory mechanism mediated by carbonic anhydrase is involved in the motility control in flatfish sperm. Cell Motil. Cytoskeleton 55:174–187, 2003. © 2003 Wiley‐Liss, Inc.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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