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(Received for publication, March 24, 1997)
From the Second Department of Internal Medicine, School of
Medicine, Tokyo Medical and Dental University, 1-5-45 Yushima,
Bunkyo-ku, Tokyo 113, Japan
ABSTRACT The aquaporin-2 (AQP2) vasopressin water channel
is translocated to the apical membrane upon vasopressin stimulation.
Phosphorylation of serine 256 of AQP2 by cAMP-dependent
protein kinase has been shown, but its relation to
vasopressin-regulated translocation has not been elucidated. To address
this question, wild type (WT) AQP2 and a mutant with alanine in place
of serine 256 of AQP2 (S256A) were expressed in LLC-PK1 cells by
electroporation. Measurements by a stopped-flow light-scattering method
revealed that the osmotic water permeability (Pf)
of LLC-PK1 cells transfected with WT was 69.6 ± 6.5 µm/s
(24.8 ± 2.2 µm/s for mock-transfected), and stimulation by 500 µM 8-(4-chlorophenylthio)-cAMP increased the
Pf by 85 ± 12%. When S256A AQP2 was
transfected, the cAMP-dependent increase in the
Pf was only 8 ± 5%. After cAMP stimulation,
the increase in surface expression of AQP2 determined by surface biotin
labeling was 4 ± 10%, significantly less than that for WT
(88 ± 5%). In addition, an in vivo
[32P]orthophosphate labeling assay demonstrated
significant phosphorylation of WT AQP2 and only minimal phosphorylation
of S256A AQP2 in LLC-PK1 cells. Our results indicated that serine 256 of AQP2 is necessary for regulatory exocytosis and that cAMP-responsive
redistribution of AQP2 may be regulated by phosphorylation of AQP2.
INTRODUCTION The urine concentration system in the kidney is regulated mainly
by vasopressin, an antidiuretic hormone that increases the osmotic
water permeability of the collecting duct cells, resulting in bulk
reabsorption of free water (1-3). The cellular actions of vasopressin
in the collecting duct cell have been partially resolved since the
identification of the vasopressin water channel aquaporin-2
(AQP2)1 (4, 5). Vasopressin has been shown
to induce regulatory redistribution of AQP2 from endosomal compartments
to the apical membrane (6-8). These observations have directly proved
the shuttle hypothesis that exo- and endocytosis of water
channel-containing vesicles account for the regulatory effects of
vasopressin on water permeability of the collecting duct cells (9,
10).
Despite elucidation of the regulatory translocation of AQP2, the
potential interactions between vasopressin-induced intracellular cAMP
accumulation and AQP2 trafficking remain unknown. It has been shown
that cAMP-dependent phosphorylation of AQP2 expressed in
the Xenopus oocyte slightly increased osmotic water
permeability without changing AQP2 surface expression (11), but the
increase was far too small to account for the dramatic increase in
water permeability of collecting duct cells. Many channels have been shown to be functionally regulated by their phosphorylation (12), but
the direct regulation of AQP2 channel functions through phosphorylation is minimal at best and is still controversial (13). On the other hand,
the physiological significance of regulatory effects on AQP2
trafficking has been emphasized. Regulatory delivery and sorting of
membrane proteins have been observed in many cell types (14, 15). Many
vesicle-associated proteins that regulate vesicle trafficking have been
identified, and some of them have been shown to exist in association
with AQP2-containing vesicles (16).
Recently, extrinsic expression of AQP2 in kidney-derived cell lines has
been reported, and cAMP-dependent regulatory exocytosis has
been shown (17). c-Myc-tagged AQP2 was expressed in LLC-PK1 cells, a
cell type that is known to express the vasopressin type 2 receptor and
increase intracellular cAMP concentration upon vasopressin stimulation,
and vasopressin-induced translocation of the channel was observed (18).
Although AQP2 was transferred to the basolateral membrane rather than
to the apical membrane where AQP2 is bound in intact kidney cells, the
study showed that LLC-PK1 cells are suitable for studying the
regulatory translocation of AQP2. Furthermore, the study postulated
that AQP2 itself is one of the key components of the vesicle
trafficking system. This notion raises the possibility that in addition
to its regulation through vesicle-associated proteins, the vesicle
trafficking system may also be regulated through modifications of AQP2.
In this study, by expressing wild-type and mutant AQP2 in LLC-PK1
cells, we examined the roles of phosphorylation of serine 256 (a
residue phosphorylated by cAMP-dependent protein kinase) in
the regulatory exocytosis of AQP2. Demonstrations of the regulatory
effects of channel phosphorylation on channel translocation would
provide new insights into the cell biology of membrane trafficking.
EXPERIMENTAL PROCEDURES Serine 256 of
rat AQP2 was replaced with alanine by polymerase chain reaction-based
site-directed mutagenesis to produce the S256A AQP2 mutant. The
nucleotide sequences of both strands of the mutant were verified by a
fluorescence sequencer (model 373A, Applied Biosystems). Polymerase
chain reaction fragment codings for open reading frames of wild-type
(WT) and S256A AQP2 (4) were subcloned into the HindIII and
XbaI site of the mammalian cell expression vector pcDNA3
(Invitrogen, San Diego, CA). Transfection was performed by
electroporation using a Gene Pulser (Bio-Rad). Subconfluent cells were
detached from dishes by trypsin treatment and were suspended. ~1 × 107 cells suspended in 600 µl of PBS were
electroporated at 350 V with 960 microfarads, using 20 µg of the
appropriate plasmid DNA. In most experiments, cells ~24 h after
transfection were used. In each transfection, 2 µg of
pcDNA3.1/lacZ plasmid (Invitrogen) was co-transfected to
verify transfection efficiency. Examinations using the Osmotic water
permeability of LLC-PK1 cells was measured by a light-scattering method
using a SX.18MV stopped-flow apparatus (Applied Photophysics Ltd.,
Leatherhead, United Kingdom) equipped with a circulating water bath.
Transfected cells grown on plastic dishes were detached by incubating
with 0.25% trypsin for 5 min at 37 °C. Cells were collected, and
trypsin was neutralized by washing twice and incubating with DMEM
containing 10% fetal calf serum for a few hours at 37 °C in a
polystyrene tube to prevent attachment of cells. The cells were then
suspended with DMEM at a concentration of ~5 × 106
cells/ml. In some experiments, cells were incubated in DMEM containing 500 µM 8-(4-chlorophenylthio)-cAMP (cpt-cAMP) for 30 min
at 37 °C before the assay. The cell suspension was abruptly mixed
with PBS containing 600 mM mannitol, and cells were imposed
with 300 mM inwardly directed osmotic gradient. A decrease
in cell volume due to osmotic water efflux driven by the osmotic
gradient was monitored as the time-dependent increase in
90° scattered light intensity monitored at 466 nm. A light intensity
trace was obtained in each sample by averaging three to seven
measurements. Data were fit to single exponential curves, and osmotic
water permeability (Pf) was determined as described
(19) by iteratively solving the following equation with Mathematica
software (Wolfram Research, Champaign, IL),
Volume 272, Number 23,
Issue of June 6, 1997
pp. 14800-14804
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
,
-Gal staining
kit (Invitrogen) revealed that >70% of the cells were expressing the
lacZ gene.
where V(t) is cell volume at time
t, SAV is initial cell surface area to volume
ratio (6 × 10
(Eq. 1)
5 cm1, calculated from
the average cell diameter of 10 µm measured by phase-contrast
microscopy), vw is the molar volume of water (vw = 18 cm3/mol),
Osmin is osmolarity inside the cell, and
Osmout is osmolarity outside the cell.
ABSTRACTSDS-polyacrylamide gel electrophoresis
(PAGE) was performed as described (20). Cells grown on a 30-mm plastic
dish were treated with 150 µl of 1 × reporter lysis buffer
(Promega, Madison, WI) for 15 min. Cell lysates were centrifuged for 1 min at 15,000 × g at 4 °C to remove cell debris.
Ten µl of the supernatant was denatured in SDS sample buffer (1.5%
SDS, 30 mM Tris-HCl, pH 6.8, 2.5% -mercaptoethanol, and
5% (v/v) glycerol) at 80 °C for 10 min, resolved in 10-20%
gradient SDS-PAGE for 1 h with a 40-mA current, and
electrotransferred to an ECL nitrocellulose membrane (Amersham Corp.)
using a Fastblot semi-dry blotting apparatus (Biometra, Goettingen,
Germany). After the membrane was blocked with Superblock (Promega) for
1 h at 23 °C and washed once with TBS-T (20 mM
Tris, 150 mM NaCl, 0.05% Tween 20, pH 7.4), it was incubated with affinity-purified antibody against a synthetic peptide
corresponding to 15 carboxyl-terminal amino acid residues of rat AQP2
(4) diluted at ~1 µg/ml in TBS-T, washed three times with TBS-T,
incubated with a 1:200 dilution of biotin-labeled anti-rabbit IgG
antibody (Vector, Burlingame, CA), washed, and incubated again with a
1:50 dilution of ABC mixture (Vector). The blot was visualized by
ECL-enhanced chemiluminescence using an ECL mini-camera (Amersham
Corp.).
24 h after transfection, LLC-PK1 cells were washed with PBS and detached from the dishes by incubating with 0.25% trypsin, 50 mM EDTA. The cells were collected and washed twice with DMEM, incubated with DMEM for 1 h at 37 °C, and washed once with ice-cold PBS. ~1 × 105 cells were suspended with 1 ml of ice-cold biotinylation buffer containing 0.5 mg/ml ImmunoPure Sulfo-NHS-LC-Biotin (Pierce) and incubated for 45 min with gentle rotation at 4 °C (21). The cells were then rinsed and suspended with 1 ml of lysis buffer (Promega), and the cell lysates were precleaned by incubation with 50 µl of protein A-agarose (Oncogene Research Products, Cambridge, MA) for 1 h at 4 °C using an end-over-end rotator. Precleaned lysates were incubated with 1:1,000 diluted affinity-purified anti-rat AQP2 antibody at 4 °C for 1 h with end-over-end rotation. 50 µl of protein A-agarose was then added and incubated 24 h at 4 °C with end-over-end rotation. The samples were washed 5 times with lysis buffer, suspended with 20 µl of SDS sample buffer, denatured at 80 °C for 10 min, loaded onto 10-20% gradient SDS-polyacrylamide gel, electrophoresed, and electrotransferred as described above. Blots were blocked as described above, reacted with streptavidin-horseradish peroxidase (KPL, Gaithersburg, MD), and visualized using the same method as that used for immunoblotting. In some experiments half of the immunoprecipitated sample was electrophoresed, blotted, and examined by ECL-enhanced chemiluminescence to ascertain that the amount of immunoprecipitated AQP2 from each sample was similar. Linearity of the biotin quantitation in the range of the amount used in our experiments was confirmed by applying a serial dilution of the samples to SDS-PAGE and then blotting and visualizing as described above.
Metabolic Labeling and Phosphorylation AssayAbout 106 transfected cells were metabolically labeled by incubation with 1 mCi of [32P]orthophosphate for 4 h in 1 ml of phosphate-free Dulbecco's modified Eagle's medium at 37 °C. 500 µM cpt-cAMP was then added to the medium and incubated for 30 min. The cells were pelleted, washed twice with ice-cold PBS, and suspended with 1 ml of lysis buffer. After 15 min of gentle mixing, AQP2 was immunoprecipitated as described for surface biotinylation, resolved with 10-20% gradient SDS-polyacrylamide gel electrophoresis, dried, and visualized by autoradiography.
RESULTS
WT AQP2 and a mutant AQP2 in which serine 256 was replaced with
alanine (S256A) were expressed in LLC-PK1 cells by electroporation, and
transient expression of AQP2 was examined by Western blotting (Fig.
1). Immunoreactive AQP2 was not detected in either
native LLC-PK1 cells (data not shown) or LLC-PK1 cells transfected with mock vector, indicating that LLC-PK1 cells do not express an AQP2-like protein. A predominant band of ~29 kDa was detected in lysates from
cells transfected with WT AQP2. The band was not detected with
preimmune serum (data not shown). Interestingly, dispersed bands
corresponding to glycosylated forms of AQP2 that were detected in
membrane fractions from rat kidney medulla and oocytes expressing rat
AQP2 (20) were not observed. A similar result was obtained by
expressing c-Myc-tagged AQP2 in LLC-PK1 cells (18), indicating that
AQP2 is not properly glycosylated in LLC-PK1 cells. However, in view of
the previous observations that first, glycosylation of AQP2 is not
necessary for proper folding and assembly as well as plasma membrane
expression of AQP2 and second, that the non-glycosylated form of AQP2
possesses a function identical to that of the wild-type AQP2 water
channel (22), it follows that a lack of the glycosylated form of AQP2
expressed in LLC-PK1 cells would have little effect in studying AQP2
function and trafficking. When S256A AQP2 was expressed in LLC-PK1
cells, the identical staining of a band of ~29 kDa shows similar
expression efficiency, provided that the immunoreactivity of the WT and
S256A AQP2 is the same.
Fig. 1. Immunoblot of LLC-PK1 cells transfected with wild type and S256A mutant of AQP2. 10 µl of cell lysate (~1 µg/µl) from LLC-PK1 cells transfected with pcDNA3 vector (mock, lane 1), wild type AQP2 (lane 2), and S256A mutant AQP2 (lane 3) was separated by 10-20% gradient SDS-polyacrylamide gel and blotted. Molecular mass standard (kDa) is indicated on the left.
[View Larger Version of this Image (45K GIF file)]
To examine the functional expression of WT and S256A AQP2 in LLC-PK1
cells, the osmotic water permeability of the plasma membrane of LLC-PK1
cells transfected with constructs was examined by a stopped-flow
light-scattering method (Fig. 2). Light-scattering traces in Fig. 2A show the time course of volume increase in
response to inward osmotic gradient. Interestingly, without cAMP
stimulation LLC-PK1 cells transfected with wild-type AQP2 showed faster
volume shrinkage than did mock-transfected cells. Calculated
Pf was about three times larger than the control,
and the increase of Pf was ~80% inhibited by
preincubation of cells with 50 µM HgCl2 (data
not shown), which is compatible with the characteristics of aquaporin
water channels (23). In contrast to the previous observation (18),
which showed that Pf of LLC-PK1 cells transfected
with AQP2 was similar to that of the control without forskolin or
vasopressin stimulation, our results indicated that AQP2 was
constitutively expressed in LLC-PK1 cell plasma membrane without cAMP
stimulation. This constitutive expression may be partially due to the
larger amount of expressed AQP2 or to the lack of cell polarity in our
experimental condition. Subsequently, we examined the effects of cAMP
on the Pf. Suspended LLC-PK1 cells expressing WT
AQP2 were incubated with 500 µM cpt-cAMP for 30 min at
37 °C, and the Pf was measured. A significant increase in the Pf was observed after this
treatment, showing a regulatory enhancement of Pf in
LLC-PK1 cells expressing WT AQP2. In contrast, when LLC-PK1 cells were
transfected with S256A AQP2, the Pf was comparable
with that of LLC-PK1 cells transfected with WT AQP2 without cAMP
stimulation, but cAMP treatment failed to increase the
Pf. These results suggested that serine 256 is
required for a cAMP-dependent regulatory increase in the
Pf of LLC-PK1 cells expressing AQP2.
Fig. 2. Osmotic water permeability of transfected LLC-PK1 cells measured by stopped-flow light-scattering microfluorimetry. A, representative traces showing the time-dependent increase in scattered light intensity are presented for LLC-PK1 cells transfected with pcDNA3, WT AQP2, or S256A AQP2, after incubation with (+) or without (
) 500 µM cpt-cAMP. Traces are from an average of three to seven experiments. B, mean and S.E. (n = 4 separate sets of transfection and measurements, each consisting of the
average of three to five individual curves) of osmotic water
permeability (Pf) of LLC-PK1 cells transfected with
pcDNA3 (mock), WT AQP2, and S256A AQP2. Cells were incubated with
(+, hatched bar) or without (, open bar) 500 µM cpt-cAMP for 30 min at 37 °C before measurement. The difference of Pf between +cAMP and cAMP in
cells transfected with WT AQP2 was significant (p < 0.05 by Student's t test).
[View Larger Version of this Image (23K GIF file)]
To quantitatively determine the surface expression of WT and S256A
AQP2, a cell-surface labeling method using biotin was employed. LLC-PK1
cells transfected with WT or S256A AQP2 were labeled with water-soluble
Sulfo-NHS-LC-Biotin, and biotin-labeled AQP2 was immunoprecipitated and
visualized. AQP2 expressed in the surface plasma membrane was
quantified as biotin-labeled AQP2 (21). As shown in Fig.
3A, biotin-labeled AQP2 was detected without cAMP stimulation in LLC-PK1 cells transfected with WT or S256A AQP2,
indicating constitutive surface expression of AQP2 and the S256A
mutant. After cAMP treatment, surface expression of WT AQP2 increased
by ~80% (Fig. 3B). This result, together with the
observation of a cAMP-dependent increase in the
Pf of LLC-PK1 cells expressing WT AQP2, proved the
existence of cAMP-dependent regulatory trafficking of AQP2
in LLC-PK1 cells as well as the constitutive pathway. However, when
serine 256 was replaced with alanine, surface expression of the mutant
did not increase after cAMP stimulation, suggesting the significant
role of serine 256 in cAMP-dependent regulatory exocytosis
of AQP2.
Fig. 3. Surface expression of AQP2 in transfected LLC-PK1 cells examined by surface biotin labeling. A, cells were transfected with mock (pcDNA3), WT AQP2, or S256A AQP2 and incubated with (+) or without (
) 500 µM
cpt-cAMP for 30 min at 37 °C. The cell surface was then labeled with
Sulfo-NHS-LC-Biotin at 4 °C for 45 min and washed. Biotin-labeled
AQP2 was immunoprecipitated, electrophoresed, and visualized by an
avidin-biotin reaction. The amount of immunoprecipitated AQP2 in each
lane was similar as examined by immunoblot with ECL-enhanced
chemiluminescence (data not shown). Molecular mass standard is shown on
the left. B, means and S.E. of relative intensity
of biotin-labeled WT AQP2 and S256A AQP2 with (+) or without ()
stimulation of cpt-cAMP are shown. Surface expression of AQP2 was
quantified by digital densitometry. Values are calculated relative to
surface expression of WT AQP2 without cAMP stimulation. The number of
individual experiments from the transfection is shown in
parentheses.
[View Larger Version of this Image (29K GIF file)]
Having shown the considerable importance of serine 256 of AQP2, we
studied cAMP-dependent phosphorylation of WT and S256A AQP2
in LLC-PK1 cells to examine the role of channel phosphorylation in the
trafficking process. As shown in Fig. 4, in
vivo phosphorylation of AQP2 was detected without cAMP
stimulation, and cAMP treatment increased the phosphorylation by about
39 ± 8% (mean ± S.D. from three independent experiments).
On the other hand, in vivo phosphorylation of S256A AQP2 was
very limited even after cAMP stimulation, showing that the major
phosphorylation site of AQP2 in LLC-PK1 cells is serine 256 and that
cAMP stimulation increased phosphorylated AQP2. cAMP-independent basal
phosphorylation of WT AQP2 could be either due to basal activity of
intracellular protein kinase A in LLC-PK1 cells or phosphorylation of
AQP2 by other kinases. The slight phosphorylation observed in the S256A
mutant may indicate weak phosphorylation of amino acid residues other
than serine 256 of AQP2. Although phosphopeptide mapping was not done
in this study, when our results are taken together with those of the
previous phosphopeptide analyses of AQP2 in oocytes (11) and in rat
kidney medulla (24), it can be concluded that the major phosphorylation site of AQP2 in LLC-PK1 cells is serine 256.
Fig. 4. In vivo phosphorylation of AQP2 in transfected LLC-PK1 cells. Cells transfected with mock (1, 2), WT AQP2 (3, 4), or S256A AQP2 (5, 6) were labeled with [32P]orthophosphate and incubated with (2, 4, 6) or without (1, 3, 5) 500 µM cpt-cAMP for 30 min at 37 °C. Cell lysates were immunoprecipitated with anti-AQP2 antibody, electrophoresed, and autoradiographed. The molecular mass standard of 29 kDa is indicated on the left. Western blotting of immunoprecipitated AQP2 showed that a comparable amount of AQP2 was immunoprecipitated and loaded.
[View Larger Version of this Image (29K GIF file)]
DISCUSSION
Expression of AQP2 deficient of serine 256 (a consensus phosphorylation site for protein kinase A) in LLC-PK1 cells revealed that serine 256 is required for cAMP-dependent regulatory exocytosis of AQP2. Assessments by functional assay and surface biotin labeling confirmed translocation of WT AQP2 to the plasma membrane upon cAMP stimulation. In contrast, cAMP-dependent regulatory exocytosis of an AQP2 mutant with alanine in place of serine 256 (S256A) was not significant. In addition, in vivo phosphorylation of WT AQP2 expressed in LLC-PK1 cells was shown to occur and was enhanced by cAMP stimulation, while phosphorylation of S256A AQP2 was minimal. Taken together, our results indicated that phosphorylation of AQP2 at serine 256 may be required for regulatory exocytosis of AQP2.
Although it has been well known that functions of many channel proteins are modulated through protein phosphorylation (12), our results provide the interesting notion that the translocation of the channel protein may be regulated by phosphorylation of the channel itself. Our finding suggests that the major passenger of the vesicle trafficking system may be a site of the regulation. This postulation is compatible with the previous prediction that AQP2 itself is a crucial component of a regulated vesicle-recycling system (18). There have been numerous reports showing cAMP-dependent regulatory trafficking of secretory vesicles and membrane proteins (25, 26); however, most of them have suggested that vesicle-associated proteins are sites of regulation (14, 27). It has been shown that trafficking of the cystic fibrosis transmembrane regulator is regulated by cAMP (15, 28, 29), but regulatory effects of cystic fibrosis transmembrane regulator phosphorylation on exo/endocytosis of the cystic fibrosis transmembrane regulator have not been known.
According to the shuttle hypothesis (10), phosphorylation of AQP2 at serine 256 may be required for vesicle trafficking processes including transferring, docking, and fusing of AQP2-containing endosomes toward the plasma membrane (14). From accumulated observations, it is conceived that the AQP2 recycling system is composed of cytoskeletal components (30-33), vesicle fusion proteins (34, 35), and the AQP2 water channel. Vasopressin-responsive modification of actin (32, 36) and phosphorylation of several of the vesicle-associated proteins (37) have been shown. In our experiments, the increment in 32P labeling of WT AQP2 was not proportional to the increment in channel surface expression, and apparent phosphorylation of WT AQP2 without cAMP stimulation was observed (Fig. 4). These observations may indicate that phosphorylation of AQP2 is not sufficient for exocytosis to occur. Thus, rather than being the initial regulatory effect on the translocation machinery, phosphorylation of AQP2 may be one of a series of regulatory processes. At the least, our results confirm that the phosphorylation of AQP2 plays a significant role in a series of the translocation signaling processes.
When transfected cells were examined immunohistochemically, results are qualitatively consistent with the conclusions from the data on water permeability and surface biotinylation, and after cAMP stimulation, a slight increment in basolateral staining was observed (data not shown) as in the previous study (18). In addition, constitutive surface expression of AQP2 and smaller cAMP-dependent changes were noticed, indicating that the dynamics of AQP2 trafficking in LLC-PK1 cells may be slightly different from those in natural collecting duct cells. However, in preliminary experiments with a cell line derived from OMCD cells (38), results were similar to those observed in LLC-PK1 cells, suggesting that although there may be some limitations, observations in LLC-PK1 cells are relevant to the collecting duct cells.
We found that the appearance of AQP2 in plasma membrane and an increment in Pf are well correlated in WT and mutant channels, suggesting that normal and mutant channels have the same permeability and that phosphorylation of serine 256 of AQP2 did not significantly change single channel water permeability in contrast to the previous study in oocytes (11). Thus, it can be concluded that the number of AQP2 channels, rather than single channel water permeability, is critical for vasopressin regulation of water permeability in collecting duct cells.
FOOTNOTES
To whom correspondence and reprint requests should be addressed:
Second Dept. of Internal Medicine, School of Medicine, Tokyo Medical
and Dental University, 1-5-45 Yushima, Bunkyo-ku, Tokyo 113, Japan.
Tel.: 81-3-5803-5216; Fax: 81-3-5803-0132; E-mail: kfushimi.med2{at}med.tmd.ac.jp.
1 The abbreviations used are: AQP2, aquaporin-2; WT, wild type; PBS, phosphate-buffered saline; DMEM, Dulbecco's modified Eagle's medium; cpt-cAMP, 8-(4-chlorophenylthio)-cAMP; Pf, osmotic water permeability; PAGE, polyacrylamide gel electrophoresis.
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A. L. Stevens, S. Breton, C. E. Gustafson, R. Bouley, R. D. Nelson, D. E. Kohan, and D. Brown Aquaporin 2 is a vasopressin-independent, constitutive apical membrane protein in rat vas deferens Am J Physiol Cell Physiol, April 1, 2000; 278(4): C791 - C802. [Abstract] [Full Text] [PDF]
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M. Zelenina, B. M. Christensen, J. Palmer, A. C. Nairn, S. Nielsen, and A. Aperia Prostaglandin E2 interaction with AVP: effects on AQP2 phosphorylation and distribution Am J Physiol Renal Physiol, March 1, 2000; 278(3): F388 - F394. [Abstract] [Full Text] [PDF]
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Y. Yamashita, K. Hirai, Y. Katayama, K. Fushimi, S. Sasaki, and F. Marumo Mutations in sixth transmembrane domain of AQP2 inhibit its translocation induced by vasopression Am J Physiol Renal Physiol, March 1, 2000; 278(3): F395 - F405. [Abstract] [Full Text] [PDF]
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 S. C.D. van IJzendoorn and D. Hoekstra Polarized Sphingolipid Transport from the Subapical Compartment Changes during Cell Polarity Development Mol. Biol. Cell, March 1, 2000; 11(3): 1093 - 1101. [Abstract] [Full Text]
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D. Brown Targeting of membrane transporters in renal epithelia: when cell biology meets physiology Am J Physiol Renal Physiol, February 1, 2000; 278(2): F192 - F201. [Abstract] [Full Text] [PDF]
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C. E. Gustafson, T. Katsura, M. McKee, R. Bouley, J. E. Casanova, and D. Brown Recycling of AQP2 occurs through a temperature- and bafilomycin-sensitive trans-Golgi-associated compartment Am J Physiol Renal Physiol, February 1, 2000; 278(2): F317 - F326. [Abstract] [Full Text] [PDF]
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G Valenti, G Procino, M Carmosino, A Frigeri, R Mannucci, I Nicoletti, and M Svelto The phosphatase inhibitor okadaic acid induces AQP2 translocation independently from AQP2 phosphorylation in renal collecting duct cells J. Cell Sci., January 6, 2000; 113(11): 1985 - 1992. [Abstract] [PDF]
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B. M. Christensen, M. Zelenina, A. Aperia, and S. Nielsen Localization and regulation of PKA-phosphorylated AQP2 in response to V2-receptor agonist/antagonist treatment Am J Physiol Renal Physiol, January 1, 2000; 278(1): F29 - F42. [Abstract] [Full Text] [PDF]
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I. Shinbo, K. Fushimi, M. Kasahara, K. Yamauchi, S. Sasaki, and F. Marumo Functional analysis of aquaporin-2 mutants associated with nephrogenic diabetes insipidus by yeast expression Am J Physiol Renal Physiol, November 1, 1999; 277(5): F734 - F741. [Abstract] [Full Text] [PDF]
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A. Rodriguez, I. Martinez, A. Chung, C. H. Berlot, and N. W. Andrews cAMP Regulates Ca2+-dependent Exocytosis of Lysosomes and Lysosome-mediated Cell Invasion by Trypanosomes J. Biol. Chem., June 11, 1999; 274(24): 16754 - 16759. [Abstract] [Full Text] [PDF]
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 T. Ma and A S Verkman Aquaporin water channels in gastrointestinal physiology J. Physiol., June 1, 1999; 517(2): 317 - 326. [Abstract] [Full Text] [PDF]
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S. NIELSEN, T.-H. KWON, B. M. CHRISTENSEN, D. PROMENEUR, J. FRØKI&Aelig;R, and D. MARPLES Physiology and Pathophysiology of Renal Aquaporins J. Am. Soc. Nephrol., March 1, 1999; 10(3): 647 - 663. [Abstract] [Full Text]
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E. Klussmann, K. Maric, B. Wiesner, M. Beyermann, and W. Rosenthal Protein Kinase A Anchoring Proteins Are Required for Vasopressin-mediated Translocation of Aquaporin-2 into Cell Membranes of Renal Principal Cells J. Biol. Chem., February 19, 1999; 274(8): 4934 - 4938. [Abstract] [Full Text] [PDF]
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J. Frokiaer, D. Marples, H. Valtin, J. F. Morris, M. A. Knepper, and S. Nielsen Low aquaporin-2 levels in polyuric DI +/+ severe mice with constitutively high cAMP-phosphodiesterase activity Am J Physiol Renal Physiol, February 1, 1999; 276(2): F179 - F190. [Abstract] [Full Text] [PDF]
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G. Nishimoto, M. Zelenina, D. Li, M. Yasui, A. Aperia, S. Nielsen, and A. C. Nairn Arginine vasopressin stimulates phosphorylation of aquaporin-2 in rat renal tissue Am J Physiol Renal Physiol, February 1, 1999; 276(2): F254 - F259. [Abstract] [Full Text] [PDF]
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T.-H. Kwon, J. Frokiaer, M. A. Knepper, and S. Nielsen Reduced AQP1, -2, and -3 levels in kidneys of rats with CRF induced by surgical reduction in renal mass Am J Physiol Renal Physiol, November 1, 1998; 275(5): F724 - F741. [Abstract] [Full Text] [PDF]
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K. Maric, A. Oksche, and W. Rosenthal Aquaporin-2 expression in primary cultured rat inner medullary collecting duct cells Am J Physiol Renal Physiol, November 1, 1998; 275(5): F796 - F801. [Abstract] [Full Text] [PDF]
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F. F. Bolander Jr. Transduction pathways involved in rapid hormone receptor regulation in the mammary epithelium Am J Physiol Endocrinol Metab, October 1, 1998; 275(4): E553 - E557. [Abstract] [Full Text] [PDF]
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D. Brown, T. Katsura, and C. E. Gustafson Cellular mechanisms of aquaporin trafficking Am J Physiol Renal Physiol, September 1, 1998; 275(3): F328 - F331. [Abstract] [Full Text] [PDF]
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G. G. MacGregor, J. Z. Xu, C. M. McNicholas, G. Giebisch, and S. C. Hebert Partially active channels produced by PKA site mutation of the cloned renal K+ channel, ROMK2 (kir1.2) Am J Physiol Renal Physiol, September 1, 1998; 275(3): F415 - F422. [Abstract] [Full Text] [PDF]
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G. Valenti, G. Procino, U. Liebenhoff, A. Frigeri, P. A. Benedetti, G. Ahnert-Hilger, B. Nurnberg, M. Svelto, and W. Rosenthal A Heterotrimeric G Protein of the Gi Family Is Required for cAMP-triggered Trafficking of Aquaporin 2 in Kidney Epithelial Cells J. Biol. Chem., August 28, 1998; 273(35): 22627 - 22634. [Abstract] [Full Text] [PDF]
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 T. Ma, B. Yang, M. A. Matthay, and A. S. Verkman Evidence against a Role of Mouse, Rat, and Two Cloned Human T1alpha Isoforms as a Water Channel or a Regulator of Aquaporin-type Water Channels Am. J. Respir. Cell Mol. Biol., July 1, 1998; 19(1): 143 - 149. [Abstract] [Full Text]
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I. Johansson, M. Karlsson, V. K. Shukla, M. J. Chrispeels, C. Larsson, and P. Kjellbom Water Transport Activity of the Plasma Membrane Aquaporin PM28A Is Regulated by Phosphorylation PLANT CELL, March 1, 1998; 10(3): 451 - 460. [Abstract] [Full Text] [PDF]
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H. Kipp, N. Pichetshote, and I. M. Arias Transporters on Demand. INTRAHEPATIC POOLS OF CANALICULAR ATP BINDING CASSETTE TRANSPORTERS IN RAT LIVER J. Biol. Chem., March 2, 2001; 276(10): 7218 - 7224. [Abstract] [Full Text] [PDF]
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M. H. Levin, P. M. Haggie, L. Vetrivel, and A. S. Verkman Diffusion in the Endoplasmic Reticulum of an Aquaporin-2 Mutant Causing Human Nephrogenic Diabetes Insipidus J. Biol. Chem., June 8, 2001; 276(24): 21331 - 21336. [Abstract] [Full Text] [PDF]
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P. M. T. Deen, B. W. M. Van Balkom, P. J. M. Savelkoul, E.-J. Kamsteeg, M. Van Raak, M. L. Jennings, T. R. Muth, V. Rajendran, and M. J. Caplan Aquaporin-2: COOH terminus is necessary but not sufficient for routing to the apical membrane Am J Physiol Renal Physiol, February 1, 2002; 282(2): F330 - F340. [Abstract] [Full Text] [PDF]
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