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Fig 1. TRPM4 expression and effect of activation on IL-1α and IL-6 production in
keratinocytes. Western blot analysis of TRPM4 in keratinocytes (A). The cell lysate from
hTRPM4-expressing HEK293T cells was used as an hTRPM4 control (A). Effects of
TRPM4 activation on IL-1α (B) and IL-6 (C) protein production in NHEKs. NHEKs were
treated with 20 ng/mL TNFα and 100 nM BTP2 for 48 hours. The concentrations of IL1α in the cell lysate and IL-6 in the supernatant were determined. Relative production
levels were calculated by setting the control value to 1.0. Results are presented as means
± standard errors of the means of six replicates; *p < 0.05, ***p < 0.001, ****p < 0.0001,
one-way analysis of variance with Dunnett’s test. Treatment with 100 nM of the TRPM4
agonist BTP2 significantly reduced IL-1α and IL-6 protein expression in NHEKs.
Fig 2. Effect of TRPM4 knockout on IL-1A and IL-6 gene expression in HaCaT cells.
Western blot analysis of TRPM4 in TRPM4-deficient HaCaT keratinocytes (A). The cell
lysate from hTRPM4-expressing HEK293T cells was used as an hTRPM4 control (A).
Effects of TRPM4 activation on IL-1A (B, D) and IL-6 (C, E) gene expression in HaCaT
cells. HaCaT cells and TRPM4 deficient HaCaT cells were treated with 20 ng/mL TNFα
and BTP2 for 3 hours. mRNA levels were analyzed by quantitative real-time PCR.
Expression of target genes was normalized to the expression of reference gene, GAPDH.
Relative expression levels were calculated by setting the control value to 1.0. Results are
presented as means ± standard errors of the means of six (B, C) or five (D, E) replicates;
*p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001, one-way analysis of variance with
Dunnett’s test. TNFα (20 nM) was applied to induce cytokine production. Treatment with
the TRPM4 agonist BTP2 significantly reduced IL-1A and IL-6 mRNA levels in HaCaT
cells (B, C). This suppression was not observed in the TRPM4-deficient HaCaT cells (D,
23
E).
Fig 3. Effect of TRPM4 knockout on IL-1α and IL-6 production in HaCaT cells.
Effects of TRPM4 activation on IL-1α (A, C) and IL-6 (B, D) protein production in
HaCaT cells (A, B) and in TRPM4-deficient HaCaT cells (C, D). HaCaT cells and
TRPM4 deficient HaCaT cells were treated with 20 ng/mL TNFα and 100 nM BTP2 for
48 hours. The concentrations of IL-1α in the cell lysate and IL-6 in the supernatant were
determined. Relative production levels were calculated by setting the control value to 1.0.
Results are presented as means ± standard errors of the means of six replicates; **p <
0.01, ****p < 0.0001, one-way analysis of variance with Dunnett’s test. Treatment with
100 nM of the TRPM4 agonist BTP2 significantly reduced IL-1α and IL-6 protein
expression in HaCaT cells (A, B). This suppression was not observed in the TRPM4deficient HaCaT cells (C, D).
Fig 4. Effect of aluminum potassium sulfate on IL-1α and IL-6 production and
intracellular Ca2+ concentration. Effects of aluminum potassium sulfate on IL-1α (A)
and IL-6 (B) protein production in HaCaT cells. HaCaT cells were treated with 20 ng/mL
TNFα and 1 mM aluminum potassium sulfate for 48 hours. The concentrations of IL-1α
in the cell lysate and IL-6 in the supernatant were determined. Relative production levels
were calculated by setting the control value to 1.0. Results are presented as means ±
standard errors of the means of six replicates; ****p < 0.0001, one-way analysis of
variance with Dunnett’s test. Treatment with 1 mM aluminum potassium sulfate
significantly reduced IL-1α and IL-6 protein expression in HaCaT cells (A, B).
Representative Ca2+ traces from hTRPM4-expressing HEK293T cells treated with or
24
without 10 µM U73122 (C). Thapsigargin (1 µM) was added to deplete stored Ca2+ to
open plasma membrane store-operated Ca2+ channels, and addition of external Ca2+ (2
mM) caused Ca2+ influx through store-operated channels. Ca2+ signals were normalized
to ionomycin (C). Average Ca2+ responses of hTRPM4-expressing HEK293T cells
normalized to ionomycin were decreased with 10 µM U73122 or 1 mM aluminum
potassium sulfate treatment after depletion of stored Ca2+ by thapsigargin (D). Means ±
standard errors of the means; **p < 0.01, ****p < 0.0001, control versus treatment; oneway analysis of variance with Dunnett’s test.
Fig 5. Direct activation of TRPM4 by aluminum potassium sulfate. Representative
traces of the inside-out patches excised from HEK293T cells expressing hTRPM4 or
mock plasmid-transfected cells. Bath application of 3 µM Ca2+ activated the current in
HEK293T cells expressing hTRPM4 (A). Application of 1 mM aluminum potassium
sulfate in pipette solution activated the current in HEK293T cells expressing hTRPM4
(B) but not in mock plasmid-transfected cells (C). Bath application of 9-phenanthrol (100
µM) suppressed the current evoked by intercellular Ca2+ (A) and aluminum potassium
sulfate (B). Bath application of 1 mM aluminum potassium sulfate activated the current
in HEK293T cells expressing hTRPM4; the current was inhibited by 9-phenanthrol (100
µM) (D).
25
Supporting Information
S1 Fig. Generation of HaCaT cell clones with targeted deletions in TRPM4 using
CRISPR/Cas9. (A) Schematic representation of the gene structure around the target site.
(B) Sequence of the TRPM4-deficient clone.
26
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