Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 14-Day Trial for You or Your Team.

Learn More →

A water channel of the nematode C. elegans and its implications for channel selectivity of MIP proteins

A water channel of the nematode C. elegans and its implications for channel selectivity of MIP... Abstract A genome project focusing on the nematode Caenorhabditis elegans has demonstrated the presence of eight cDNAs belonging to the major intrinsic protein superfamily. We functionally characterized one of these cDNAs named C01G6.1. Injection of C01G6.1 cRNA increased the osmotic water permeability ( P f ) of Xenopus oocytes 11-fold and the urea permeability 4.5-fold but failed to increase the glycerol permeability. It has been speculated that the MIP family may be separated into two large subfamilies based on the presence or absence of two segments of extra amino acid residues (∼15 amino acids) at the second and third extracellular loops. Because C01G6.1 (designated AQP-CE1), AQP3, and glycerol facilitator (GlpF) all have these two segments, we replaced the segments of AQP-CE1 with those of AQP3 and GlpF to identify their roles. The functional characteristics of these mutants were principally similar to that of wild-type AQP-CE1, although the values of P f and urea permeability were decreased by 39–74% and 28–65%, respectively. These results suggest that the two segments of extra amino acid residues may not contribute to channel selectivity or formation of the route for small solutes. aquaporin glycerol facilitator water permeability glycerol permeability urea permeability major intrinsic protein Caenorhabditis elegans Footnotes Address for reprint requests: M. Kuwahara, Second Dept. of Internal Medicine, Tokyo Medical and Dental Univ., Yushima, Bunkyo-ku, Tokyo 113-8519, Japan. The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked “ advertisement ” in accordance with 18 U.S.C. §1734 solely to indicate this fact. Copyright © 1998 the American Physiological Society http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png AJP - Cell Physiology The American Physiological Society

A water channel of the nematode C. elegans and its implications for channel selectivity of MIP proteins

Loading next page...
 
/lp/the-american-physiological-society/a-water-channel-of-the-nematode-c-elegans-and-its-implications-for-SykAJr13Bj

References

References for this paper are not available at this time. We will be adding them shortly, thank you for your patience.

Publisher
The American Physiological Society
Copyright
Copyright © 2010 the American Physiological Society
ISSN
0363-6143
eISSN
1522-1563
Publisher site
See Article on Publisher Site

Abstract

Abstract A genome project focusing on the nematode Caenorhabditis elegans has demonstrated the presence of eight cDNAs belonging to the major intrinsic protein superfamily. We functionally characterized one of these cDNAs named C01G6.1. Injection of C01G6.1 cRNA increased the osmotic water permeability ( P f ) of Xenopus oocytes 11-fold and the urea permeability 4.5-fold but failed to increase the glycerol permeability. It has been speculated that the MIP family may be separated into two large subfamilies based on the presence or absence of two segments of extra amino acid residues (∼15 amino acids) at the second and third extracellular loops. Because C01G6.1 (designated AQP-CE1), AQP3, and glycerol facilitator (GlpF) all have these two segments, we replaced the segments of AQP-CE1 with those of AQP3 and GlpF to identify their roles. The functional characteristics of these mutants were principally similar to that of wild-type AQP-CE1, although the values of P f and urea permeability were decreased by 39–74% and 28–65%, respectively. These results suggest that the two segments of extra amino acid residues may not contribute to channel selectivity or formation of the route for small solutes. aquaporin glycerol facilitator water permeability glycerol permeability urea permeability major intrinsic protein Caenorhabditis elegans Footnotes Address for reprint requests: M. Kuwahara, Second Dept. of Internal Medicine, Tokyo Medical and Dental Univ., Yushima, Bunkyo-ku, Tokyo 113-8519, Japan. The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked “ advertisement ” in accordance with 18 U.S.C. §1734 solely to indicate this fact. Copyright © 1998 the American Physiological Society

Journal

AJP - Cell PhysiologyThe American Physiological Society

Published: Dec 1, 1998

There are no references for this article.