Control of flatfish sperm motility by CO2 and carbonic anhydrase. Inaba, K., Dréanno, C., & Cosson, J. Cell Motility, 55(3):174–187, 2003. _eprint: https://onlinelibrary.wiley.com/doi/pdf/10.1002/cm.10119
Control of flatfish sperm motility by CO2 and carbonic anhydrase [link]Paper  doi  abstract   bibtex   
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.
@article{inaba_control_2003,
	title = {Control of flatfish sperm motility by {CO2} and carbonic anhydrase},
	volume = {55},
	copyright = {Copyright © 2003 Wiley‐Liss, Inc.},
	issn = {1097-0169},
	url = {https://onlinelibrary.wiley.com/doi/abs/10.1002/cm.10119},
	doi = {10.1002/cm.10119},
	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.},
	language = {en},
	number = {3},
	urldate = {2020-03-03},
	journal = {Cell Motility},
	author = {Inaba, Kazuo and Dréanno, Catherine and Cosson, Jacky},
	year = {2003},
	note = {\_eprint: https://onlinelibrary.wiley.com/doi/pdf/10.1002/cm.10119},
	keywords = {Inaba K},
	pages = {174--187}
}

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