Am J Physiol Cell Physiol AJP: Gastrointestinal and Liver Physiology
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Am J Physiol Cell Physiol 275: C1459-C1464, 1998;
0363-6143/98 $5.00
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Vol. 275, Issue 6, C1459-C1464, December 1998

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

Michio Kuwahara1, Kenichi Ishibashi1, Yong Gu1, Yoshio Terada1, Yuji Kohara2, Fumiaki Marumo1, and Sei Sasaki1

1 Second Department of Internal Medicine, School of Medicine, Tokyo Medical and Dental University, Tokyo 113-8519; and 2 Gene Network Laboratory, National Institute of Genetics, Mishima 441-8540, Japan

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 (Pf) 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 Pf 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


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