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(Received for publication, January 24, 1997, and in revised form, June 3, 1997)
From the A new member of the aquaporin (AQP) family has
been identified from rat testis. This gene, referred as aquaporin 7 (AQP7), encodes a 269-amino acid protein that contained the conserved NPA motifs of MIP family proteins. AQP7 has the amino acid sequence homology with other aquaporins (~30%), and it is highest with AQP3
(48%), suggesting that both AQP3 and AQP7 belong to a subfamily in the
MIP family. Injection of AQP7-cRNA into Xenopus oocytes expressed a 26-kDa protein detected by immunoblotting. The expression of AQP7 in oocytes stimulated the osmotic water permeability by 10-fold
which was not inhibited by 0.3 mM mercury chloride. The Arrhenius activation energy for the stimulated water permeability was
low (2.1 kcal/mol). AQP7 also facilitated glycerol and urea transport
by 5- and 9-fold, respectively. The activation energy for glycerol was
also low (5.3 kcal/mol after the correction of the endogenous glycerol
permeability of oocytes). Northern blot analysis revealed a
1.5-kilobase pair transcript expressed abundantly in testis. In
situ hybridization of testis revealed the expression of AQP7 at
late spermatids in seminiferous tubules. The immunohistochemistry of
testis localized the AQP7 expression at late spermatids and at maturing
sperms. AQP7 may play an important role in sperm function.
Volume 272, Number 33,
Issue of August 15, 1997
pp. 20782-20786
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
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