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(Received for publication, January 29, 1997, and in revised form, April 17, 1997)
From the Departments of Medicine and Physiology, Cardiovascular
Research Institute, University of California,
San Francisco, California 94143-0521
The goal of this study was to compare single
channel water and glycerol permeabilities of mammalian aquaporins (AQP)
1-5 and the major intrinsic protein of lens fiber (MIP). Each of the
six cloned cDNAs from rat was left untagged or was epitope-tagged with c-Myc or FLAG at either the N or C terminus so that results would
not depend on epitope identity or location. The constructs were
expressed in Xenopus oocytes for measurement of osmotic
water permeability (Pf), [3H]glycerol
uptake, and protein expression. Each of the 30 epitope-tagged constructs was expressed strongly at the oocyte plasma membrane. The
10-min uptake of [3H]glycerol was increased significantly
(range of 4.5-8-fold over control) in oocytes expressing untagged AQP3
(GLIP) and each of the four tagged AQP3 constructs;
[3H]glycerol uptake was not increased in oocytes
expressing AQP1, AQP2, AQP4, AQP5, or MIP. In oocytes microinjected
with 5 ng of cRNA, average Pf values (in cm/s × 10
Volume 272, Number 26,
Issue of June 27, 1997
pp. 16140-16146
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
3) were 0.67 ± 0.06 (control), 19 ± 2 (AQP1), 10 ± 1 (AQP2), 8 ± 2 (AQP3), 29 ± 1 (AQP4),
10 ± 1 (AQP5), and 1.3 ± 0.2 (MIP), and they were
relatively insensitive to the presence, identity, or location of the
epitope tag. Pf values were not affected by protein
kinase A or C activation. After normalization for plasma membrane
expression by immunoprecipitation of microdissected plasma membranes,
single channel water permeabilities (pf, referenced to the AQP1 pf of 6 × 1014
cm3/s) were (in cm3/s × 1014) 3.3 ± 0.2 (AQP2), 2.1 ± 0.3 (AQP3),
24 ± 0.6 (AQP4), 5.0 ± 0.4 (AQP5), and 0.25 ± 0.05 (MIP); pf values were insensitive to epitope
identity and location. These results indicate very different intrinsic
water permeabilities for the mammalian aquaporin homologs, with the
pf value for AQP4 remarkably higher than those for
the others. The pf values establish limits on
aquaporin tissue densities required for physiological function and
suggest significant structural and functional differences among the
aquaporins.
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