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(Received for publication, March 8, 1996, and in revised form, April 19, 1996)
From the Laboratory of Kidney and Electrolyte Metabolism, NHLBI,
National Institutes of Health, Bethesda, Maryland 20892-1598
ABSTRACT Organisms, almost universally, adapt to
hyperosmotic stress through increased accumulation of organic osmolytes
but the molecular mechanisms have only begun to be addressed. Among
mammalian tissues, renal medullary cells are uniquely exposed to
extreme hyperosmotic stress. Sorbitol, synthesized through aldose
reductase, is a predominant osmolyte induced under hyperosmotic
conditions in renal cells. Using a rabbit renal cell line, we
originally demonstrated that hyperosmotic stress induces transcription
of the aldose reductase gene. Recently, we cloned the rabbit aldose
reductase gene, characterized its structure, and found the first
evidence of an osmotic response region in a eukaryotic gene. Now, we
have progressively subdivided this 3221-base pair (bp) region into
discrete fragments in reporter gene constructs. Thereby, we have
functionally defined the smallest sequence able to confer hyperosmotic
response on a downstream gene independent of other putative
cis-elements, that is, a minimal essential osmotic response
element (ORE). The sequence of the ORE is CGGAAAATCAC(C) (bp
INTRODUCTION In nature, one of the most prevalent types of stress is that
caused by prolonged exposure of an organism to a hyperosmotic
environment. Although the cellular responses to hyperosmotic stress are
among the most profound, the molecular mechanisms involved have only
recently begun to be addressed. Thus, contrary to the earnest study of
heat shock at the molecular level, relatively little is known about the
cascade of signals between the initial extracellular stimulus
(hyperosmolality) and the ultimate adaptative response. It is
recognized that, across the evolutionary spectrum, organisms have
developed a universal adaptation process to cope with hyperosmotic
stress; that is, increased accumulation of osmotically active organic
solutes (organic osmolytes) (1). Cells accumulate high concentrations
of organic osmolytes in place of inorganic ions. This is because,
unlike equivalent concentrations of inorganic ions, the organic
osmolytes apparently are not perturbing to cellular macromolecules
(1).
Some of the predominant organic osmolytes are: betaine in bacteria
(e.g. Escherichia coli) (2), glycerol in yeast (e.g.
Saccharomyces cerevisiae) (3, 4), and sorbitol and betaine in
cells of the mammalian renal medulla, the only mammalian tissue
routinely exposed to extreme hyperosmotic stress in normal
physiological conditions (5). In bacteria, where the molecular
mechanisms for accumulation of organic osmolytes have been studied most
extensively, hyperosmotic stress induces transcription of the
proU operon. proU encodes the transport system
involved in accumulation of betaine (2). Osmotic control of
proU transcription is exerted, at least in part, by an
``upstream activating region'' that is currently being characterized
by several groups (reviewed in Ref. 2). In S. cerevisiae,
studies of the In mammalian renal medullary cells under hyperosmotic stress, the
synthesis of sorbitol, catalyzed by aldose reductase
(AR),1 is increased (6). PAP-HT25 cells are
a line of rabbit inner medullary cells (7) that accumulate large
amounts of sorbitol (8) and other organic osmolytes (9) under
hyperosmotic conditions. Using this line, we originally demonstrated
that hyperosmotic stress induces transcription of the AR gene (10),
resulting in increased AR mRNA levels (11), followed by a rise in
AR protein synthesis rate (12) and, ultimately, increased sorbitol
accumulation (13). Recently, we cloned the rabbit AR gene,
characterized its structure, and found the first evidence of an osmotic
response element (ORE) within a eukaryotic gene (14). A 3221 base pair
(bp) fragment of the 5 EXPERIMENTAL PROCEDURES Expression vectors, 007Luc, ARLuc, and B19CAT, were
as described (14). 007Luc is promoterless and contains the luciferase
gene, whereas ARLuc contains the rabbit AR promoter (bp AR fragments longer than 70 bp to be subcloned into expression vectors
were PCR-amplified from genomic clone gAR56-5 (GenBankTM accession
number is U12317[GenBank]) (14) using primers synthesized with appropriate
restriction enzyme sites toward their 5 Transfections were
performed as described previously (14). Briefly, rabbit renal medulla
PAP-HT25 cells (passage 72-80) were grown in isoosmotic medium (300 mosm/kg H2O) (7) in 150-mm dishes (Corning) and
co-transfected with a given luciferase construct (3 µg) and B19CAT
(12-20 µg) using Cell-Phect (Pharmacia Biotech Inc.). From each
transfected 150-mm dish, cells were seeded into six 35-mm dishes and
left overnight. The medium in three of the dishes was changed to fresh
isoosmotic medium (300 mosm/kg H2O); the medium in the
three other dishes was changed to the same medium made hyperosmotic
(500 mosm/kg H2O) with NaCl. Twenty-four hours after
changing the medium, cells were harvested by adding 100 µl of lysis
buffer (Enhanced Luciferase Assay Kit, Analytical Luminescence
Laboratory).
Cell lysates were analyzed for total protein, luciferase activity, and
CAT protein using the following kits as per manufacturers'
instructions. Total protein was determined using the Bio-Rad Protein
Assay Kit (Bio-Rad, using Luciferase activity in relative
light units/µg of cell protein was normalized by CAT protein in
picograms (from the co-transfected B19CAT construct)/µg of cell
protein.
Nuclei were isolated
(17) from PAP-HT25 cells maintained in isoosmotic medium (300 mosm/kg
H2O) and from cells exposed for 18-24 h to the same medium
made hyperosmotic (500 mosm/kg H2O) with NaCl (11). Nuclear
protein extracts were prepared after the method of Frain (18) except
that buffer D contained 650 mM NaCl.
32P-End-labeled double-stranded oligonucleotides (3-5 × 104 cpm containing 10-20 fmol) were incubated with 4 µg of nuclear protein extract, 0.5 µg of poly(dI-dC), and 0-1.7
pmol (0-100-fold molar excess) unlabeled specific competitor
oligonucleotide (AR gene bp RESULTS AND DISCUSSION We first identified a 3221-bp region of DNA (
Effect of hyperosmolality on reporter gene expression in transient
transfectants
Volume 271, Number 31,
Issue of August 2, 1996
pp. 18318-18321
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
COMMUNICATION:
THE ALDOSE REDUCTASE GENE IN HYPEROSMOTIC STRESS*
,
ABSTRACT
INTRODUCTION
EXPERIMENTAL PROCEDURES
RESULTS AND DISCUSSION
FOOTNOTES
Acknowledgments
REFERENCES
1105/1094). A 17-bp fragment (1108/1092) containing the ORE
used as a probe in electrophoretic mobility shift assays suggests
hyperosmotic induction of a slowly migrating band. Isolation of
trans-acting factor(s) and characterization of their
interaction with the ORE should elucidate the basic mechanisms for
regulation of gene expression by hyperosmotic stress.
igh-
smolarity
lycerol (HOG) response have concentrated on the signal
transduction pathway immediately following hyperosmotic stress and
preceding induction of target genes that directly control accumulation
of glycerol (reviewed in Ref. 4). Thus, only one ultimate gene target
in the HOG pathway has been identified. That is GPD1, which
encodes glycerol-3-phosphate dehydrogenase, one of the two enzymes that
catalyze the synthesis of glycerol. Most recently, osmotic stress was
shown to increase glycerol-3-phosphate dehydrogenase activity and
mRNA levels (3). The identification of GPD1 gene regions
that control the osmotic response has not been reported.
-flanking region of the aldose reductase gene
was shown to confer osmotic response to a downstream luciferase gene
with the AR promoter as well as with a heterologous, B19, promoter
(14). Here, we present the identification of the minimal essential ORE
that controls induction of AR transcription by hyperosmotic stress.
208/+27) in
unique XhoI-HindIII sites immediately upstream of
the luciferase gene. ARLuc was previously demonstrated to exhibit basal
promoter activity (as construct ARLuc6 in Ref. 14). B19CAT contains the
B19 promoter immediately upstream of the chloramphenicol
acetyltransferase (CAT) gene (14, 15). ARL and TKL were constructed to
obtain the ability to subclone AR fragments directionally in vectors
containing either the AR or a heterologous promoter from the polyoma
virus thymidine kinase (TK) gene, respectively, upstream of the
luciferase gene. ARL and TKL vectors were constructed by using PCR
primers synthesized with appropriate restriction enzyme sites toward
their 5 ends. ARL contains the AR promoter (bp 208/+27) flanked
immediately upstream by XhoI, NcoI, and
KpnI sites and immediately downstream by AflII
and HindIII sites. TKL contains the same restriction enzyme
sites flanking the mutant polyoma virus enhancer PYF441 and the
thymidine kinase promoter PCR-amplified as a unit from pSSC-9 (16). The
AR and TK promoters were subcloned directionally into unique
XhoI-HindIII sites in 007Luc to produce ARL and
TKL.
end. Fragments less than 70 bp, inclusive of appropriate restriction enzyme sites, were created by
annealing synthesized sense and antisense oligonucleotides (DNA/RNA
Synthesizer, model 392, Applied Biosystems Inc.). Fragments were
subcloned into the XhoI site of ARLuc, followed by selection
of clones carrying the fragment in the forward direction.
Alternatively, fragments were directionally cloned into the
XhoI-KpnI sites of ARL or TKL. Construct
sequences were verified by primer-directed, double-stranded plasmid
sequencing (Sequenase DNA Sequencing Kit, U. S. Biochemical Corp.). To
confirm osmotic regulation of a heterologous promoter by the ORE, a
17-bp fragment (bp 1108/1092) containing the minimal essential ORE
was subcloned in the forward direction into the
XhoI-KpnI sites of TKL upstream of the TK
promoter.
-globulin as standard). Luciferase
activity was determined using the Enhanced Luciferase Assay Kit and a
Monolight 2010 Luminometer (Analytical Luminescence Laboratory). The
amount of CAT was determined using CAT Elisa Kits (5 Prime 
3 Prime,
Inc. or Boehringer Mannheim) and a Titertek Multiskan plate reader with
a 405-nm filter.
1108/1092) in binding buffer (19) for
30 min at room temperature. Reactions were electrophoresed on a 4%
polyacrylamide gel (80:1, acrylamide:bisacrylamide) in 1 × TAE
buffer at 4 °C (19). Autoradiograms were exposed at 80 °C.
Oligonucleotides were synthesized directly to produce sequence that
corresponds to AR gene bp 1108/1092 (17 bp).
3429/209) that
contained a putative osmotic response element (as construct ARLuc9 in
Ref. 14) (Table I). We have now proceeded to
functionally identify within that fragment the smallest sequence that
could confer osmotic response on a downstream gene independent of other
putative cis-elements that may potentiate the response; that
is, a minimal essential osmotic response element. Instead of
traditional nested deletions, we increasingly subdivided the
3429/209 region into discrete pieces and tested them individually.
This allowed us to examine all fragments for independent osmotic
response as opposed to only those fragments that remain after deletion.
All fragments were synthesized either by PCR amplification (
146 bp)
or directly on a DNA synthesizer and tested for ability to confer
osmotic response to a luciferase gene driven by the rabbit aldose
reductase promoter (208/+27) (14, 20) in transient transfection
assays (Table I). As shown in Table I in the ARLuc constructs, the most
upstream region (3429/2686 and 2705/1152) of the 3221-bp
fragment (3429/209) did not generate osmotic response. However, the
downstream 962 bp (1170/209) retained osmotic response. Within this
962-bp fragment, osmotic response was confined to an upstream 679-bp
fragment (1170/492).
208 to +27), and TKL contains the
thymidine kinase (TK) promoter; all promoters are upstream of the
luciferase gene. DNA fragments from the rabbit AR gene were inserted
upstream of the AR promoter in ARLuc and ARL or upstream of the TK
promoter in TKL; these fragments are shown directly below their
corresponding promoter. Positions of nucleotides that define the AR
gene DNA fragments are numbered with the first nucleotide of exon 1 as
+1. Positive numbers indicate nucleotides downstream of +1; negative
numbers are nucleotides upstream of +1. For constructs demonstrating
hyperosmotic response, the size of the DNA fragment is shown in
parentheses. Tandem repeats of selected fragments are indicated
(e.g. 3X). Cells were co-transfected with a given luciferase
construct and B19CAT. B19CAT contains the B19 promoter upstream of the
CAT gene. Luciferase activity in relative light units/µg of cell
protein was normalized by CAT protein in picograms/µg cell protein
(Luc/CAT). *HYPER/ISO is the ratio of Luc/CAT in hyperosmotic medium
divided by Luc/CAT in isoosmotic medium (mean ± standard error).
**HYPER/ISO is the ratio of Luc/CAT in hyperosmotic medium divided by
Luc/CAT in isoosmotic medium expressed relative to the construct
containing the promoter alone (mean ± standard error); these data
are shown only for constructs demonstrating hyperosmotic response.
n is the number of independent transfections.
Construct
*HYPER/ISO
(n)
**HYPER/ISO relative to promoter
ARLuc
(
208/+27)3.5
± 0.64 (8)
1.0
3429/209 (3221 bp)33.1 ± 3.83 (8)
9.4 ± 1.09
3429/26861.9 ± 0.18 (2)
2705/11521.4
± 0.36 (2)
1170/209 (962 bp)21.1
± 0.16 (2)
6.0 ± 0.04
510/2091.7 (1)
1170/492 (679 bp)20.2 ± 4.16 (3)
5.7 ± 1.18
1170/894 (277 bp)9.2 ± 1.52 (3)
2.6 ± 0.43
993/6973.0
± 1.05 (3)
770/4922.9 ± 0.63 (3)
ARL (
208/+27)2.4
± 0.09 (27)
1.0
1170/492 (679 bp)11.5 ± 1.30 (7)
4.8 ± 0.54
1170/894 (277 bp)12.7 ± 2.46 (2)
5.3 ± 1.26
1202/1057 (146 bp)8.1 ± 0.54 (15)
3.4 ± 0.22
1110/957 (154 bp)4.1 ± 0.66 (6)
1.7 ± 0.28
1025/8701.7
± 0.37 (3)
1170/11181.8 ± 0.20 (3)
1117/1071 (47 bp)5.3 ± 1.08 (3)
2.2 ± 0.45
1070/10261.7 ± 0.02 (3)
1144/11011.5
± 0.12 (3)
1100/10512.5 ± 0.18 (3)
1120/10962.3 ± 0.47 (4)
1095/10712.3
± 0.10 (3)
1108/1083 (26 bp)4.5 ± 0.51 (3)
1.9
± 0.17
1108/1083 2X (26 bp 2X)15.1
± 0.55 (3)
6.3 ± 0.23
1108/1092 (17 bp)4.8
± 0.22 (16)
2.0 ± 0.09
1108/1092 3X (17 bp
3X)28.6 ± 2.51 (3)
11.9 ± 1.05
1104/10912.7 ± 0.08 (4)
1104/1091 3X2.9
± 0.12 (3)
TKL
2.3 ± 0.12 (6)
1108/10925.6 ± 0.83 (4)
2.5 ± 0.36
007Luc (promotorless)
2.0
± 0.28 (8)
Initially, for the ARLuc constructs (Table I), the DNA fragments were
cloned into the only available unique restriction enzyme
(XhoI) site immediately upstream of the AR promoter. After
having narrowed down the ORE to 277 bp (1170/894), the construct
ARL was produced by adding, to ARLuc, unique restriction enzyme sites
that would allow us to subclone directionally (see ``Experimental
Procedures''). Since the added bases could affect function, we
subcloned into ARL two of the fragments (1170/492 and 1170/894)
that had osmotic response in ARLuc. Indeed, these fragments continued
to display osmotic response when in the ARL vector (Table I).
Osmotic response was sequentially narrowed down to 47 bp
(1117/1071), 26 bp (1108/1083), and then to 17 bp
(1108/1092). This 17-bp sequence was also able to confer osmotic
response to the TK promoter (Table I, TKL construct 1108/1092).
Osmotic response had been gradually decreasing with the size of the
fragment, as seen in the only other sequence identified as containing a
eukaryotic osmotic response element (19). To better evaluate osmotic
response, we created tandem repeats of the 26- and 17-bp fragments,
hypothesizing that this would magnify the response. As shown in Table
I, tandem repeats of sequence containing the ORE (1108/1083 two
times and 1108/1092 three times) markedly increased osmotic
response. In constrast, tandem repeats (1104/1091 three times) of a
fragment having no osmotic response (1104/1091) were unable to
evoke the response. We conclude that the sequence 1108/1092 alone
can confer osmotic response. The gradual drop in magnitude with
decreasing fragment size suggests the possibility that other
cis-elements may potentiate the osmotic response.
By gradually eliminating base pairs from the 17-bp fragment
(1108/1092) we continued to functionally define the minimal
essential osmotic response element. As shown in Fig. 1,
upstream bp 1108 to 1106 are unnecessary for osmotic response.
However removal of bp 1105 eliminates osmotic response, thereby
defining the upstream end of the ORE to be bp 1105. Relative to the
downstream end of the element, construct 1108/1094 retained osmotic
response (Fig. 1). In addition, we had observed previously that when we
subdivided the 47-bp fragment (1117/1071) into two pieces (Table I,
ARL constructs 1120/1096 and 1095/1071), thereby splitting
between bp 1096 and 1095, all osmotic response was lost. We
concluded that bp 1095 was essential. If bp 1094, a cytidine (C),
is substituted by an adenosine (A), osmotic response is unaffected.
However, ARL construct 1108/1095 showed a Hyper/Iso response equal
to 3.5 ± 0.25 (1.5 ± 0.10 relative to ARL, Fig. 1). We
conclude that bp 1094 may be necessary, but it need not be a
pyrimidine, and that the minimal essential ORE is defined by bp
1105/1094.
Fig. 1. The aldose reductase minimal essential osmotic response element (ORE). Transfected PAP-HT25 cells were maintained in isoosmotic medium (Iso) (300 mosm/kg H2O) or exposed to hyperosmotic medium (Hyper) (500 mosm/kg H2O) for 18-24 h. Values are expressed as the ratio of Hyper divided by Iso. ARL contains the rabbit AR promoter (bp
208/+27) upstream of the
luciferase gene. DNA fragments from the rabbit AR gene were inserted
upstream of the AR promoter in ARL. Positions of nucleotides that
define the AR gene DNA fragments are numbered with the first nucleotide
of exon 1 as +1. Negative numbers are nucleotides upstream
of +1. As indicated by an underline, bp 1102 was mutated
from an A to a G and bp 1094 was mutated from a C to an A. Cells were
co-transfected with a given luciferase construct and B19CAT. B19CAT
contains the B19 promoter upstream of the CAT gene. Luciferase activity
in relative light units/µg of cell protein was normalized by CAT
protein in picograms/µg of cell protein (Luc/CAT).
*Hyper/Iso is the ratio of Luc/CAT in hyperosmotic medium
divided by Luc/CAT in isoosmotic medium (mean ± standard error).
**Hyper/Iso is the ratio of Luc/CAT in hyperosmotic medium
divided by Luc/CAT in isoosmotic medium expressed relative to ARL
(Hyper/Iso = 2.4 ± 0.09 and Table I) (mean ± standard
error); these data are shown only for constructs demonstrating
hyperosmotic response. [n] is the number of independent
transfections.
We noted, particularly because of the concentration of purines at the
5 end of the ORE, the similarity between a nucleotide (nt) sequence
(nt 1104/1095; GGAAAATCAC) within it and the consensus sequence for
the NF-
B element (GGG(A/G)NN(C/T)(C/T)(C/A/T)C) (21). However, the
sequence 1104/1095 does not fit the NF-B consensus at nucleotide
1102 where all currently recognized NF-B elements have a guanosine
(G) at the corresponding nucleotide (21). To determine whether the ORE
would retain osmotic response if its sequence were modified to include
an NF-B element consensus, we substituted base 1102, an adenosine
(A), by a guanosine (G) (underlined in Fig. 1) as in an
NF-B element. Osmotic response was lost (Fig. 1); we conclude that,
at least based on cis-element sequence, the ORE does not
contain an NF-B element.
The same experiment provided information relative to a putative ORE
consensus. As shown below, the ORE shares six consecutive base pairs
(1104/1099, GGAAAA) in common with TonE, the only other sequence
identified as containing a eukaryotic osmotic response element (19).
TonE regulates the hyperosmotic response of the dog renal
Na+- and Cl
-coupled betaine transporter
responsible for accumulation of betaine, another organic osmolyte
(22, 23, 24). In TonE, when five of the 6 bases (GAAAA) were simultaneously
substituted by TCCCC, osmotic response was lost (19).
|
1102 in the ORE), an adenosine (A), with
another purine, a guanosine (G), eliminates osmotic response.
Identification of other osmotic response elements should better define
a eukaryotic osmotic response consensus, if there is one.
To test for interaction of the ORE with putative osmotically induced
transcription factors, we performed electrophoretic mobility shift
assays of the ORE in the presence of nuclear protein extracts prepared
either from cells maintained in isoosmotic medium or cells exposed to
hyperosmotic medium for 18-24 h. We used bp 1108/1092 as the
probe. This fragment had been shown to confer osmotic response to the
luciferase gene in transfection analyses (Table I). A slowly migrating
but narrow band (arrow) was observed predominantly with
extracts from hyperosmotically treated cells in the presence of 0.5 µg of poly(dI-dC) (Fig. 2, lane 6). As
shown in Fig. 2, a 50-fold molar excess of unlabeled (cold) probe
reduces and a 100-fold molar excess virtually eliminates the narrow
slowly migrating band (lanes 7 and 8,
respectively). An additional, faster migrating and very broad band also
remains in the presence of poly(dI-dC) but is eliminated by a 100-fold
molar excess of the specific competitor (bp 1108/1092). This band
is also present in lanes containing extract from isoosmotically treated
cells but to a lesser degree than that seen in lanes containing extract
from hyperosmotically treated cells. These mobility shift assays
represent exploratory evidence that hyperosmotic stress results in the
induction of putative trans-acting factor(s) that associate
with the aldose reductase ORE. Isolation of these
trans-acting factor(s) and characterization of their
interaction with the ORE should elucidate the basic mechanisms for
regulation of gene expression by hyperosmotic stress.
Fig. 2. Electrophoretic mobility shift assay of the AR ORE in the presence of specific competitor. A radiolabeled 17-bp oligonucleotide corresponding to bp
1108/1092 in the aldose
reductase gene was used. The oligonucleotide was incubated with 4 µg
of nuclear protein extract from PAP-HT25 cells maintained in isoosmotic
medium (Iso, lanes 1-4) (300 mosm/kg H2O) or
exposed to hyperosmotic medium (Hyper, lanes 5-8) (500 mosm/kg H2O) in the presence (+) (lanes 2-4,
6-8) and absence () (lanes 1 and 5) of
500 ng of poly(dI-dC) (dIC). Incubations were also in the
presence (lanes 3, 4, 7, 8) or absence () (lanes 1, 2, 5, 6) of 50- or 100-fold molar excess of unlabeled specific
competitor oligonucleotide (cold 1108/1092). Lane 9,
radiolabeled oligonucleotide (bp 1108/1092) alone.
FOOTNOTES
To whom correspondence should be addressed: National Institutes of
Health, Bldg. 10, Rm. 6N307, 10 Center Dr. MSC 1598, Bethesda, MD
20892-1598. Tel.: 301-496-1559; Fax: 301-402-1443; E-mail:
jdf{at}helix.nih.gov.
§ On sabbatical leave from Department of Physiology, University of Otago, Dunedin, New Zealand. Dr. Jennifer J. Bedford's sabbatical leave was supported by the Health Research Council of New Zealand and the New Zealand Lottery Grants Board.
1 The abbreviations used are: AR, aldose reductase; ORE, osmotic response element; CAT, chloramphenicol acetyltransferase; bp, base pair(s); nt, nucleotide(s); TK, thymidine kinase; PCR, polymerase chain reaction.
Acknowledgments
We thank Drs. Jarvis Reed and Michael M. Gottesman, National Cancer Institute, for the gift of pSSC-9 and Dr. Mark M. Garner, FMC Bioproducts, and Dr. Hyug-Moo Kwon, Division of Nephrology, The Johns Hopkins University School of Medicine, for valuable advice regarding the electrophoretic mobility shift assays.
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