(A)- 指摘項目No.29
論文#2のFigure 1Aの上から1段目と2段目のAMPKとpAMPKの画像は、
論文#8のFigure 1(A)の上から1段目と2段目のAMPKとpAMPKの画像と、
類似しており、画像の流用（データの捏造）が疑われます。
(A)- 指摘項目No.30
論文#2のFigure 1Aの上から6段目のp-Aktの画像は、
論文#8のFigure 1(A)の上から6段目のp-Aktの画像と、
類似しており、画像の流用（データの捏造）が疑われます。
(A)- 指摘項目No.31
論文#2のFigure 1Aの上から7段目のeNOSの画像は、
論文#8のFigure 1(A)の上から7段目のeNOSの画像を左右逆に加工した画像と同一であり、
画像の流用（データの捏造）が疑われます。
(A)- 指摘項目No.32
論文#2のFigure 4Aの最上段のIkB-αの一番左の１列分の画像(0 minの画像）は、
同論文#2のFigure 4Cの最下段のGST-IkB-αの一番左の１列分の画像(AGE-の画像）の縦横比を変更したものに、
類似しており、画像の流用（データの捏造）が疑われます。
(A)- 指摘項目No.33
論文#2のFigure 4Aの最上段のIkB-αの左から2,3,4列目の3列分は、
同論文#2のFigure 4BのIkB-αの画像の右３列分（Fenofibrate 0, 30, 100 μMの画像）の画像と類似しています（画像サイズを加工しています）。
さらに、この３列分の画像は、
論文#6のFigure 2(B)の最上段のp-Aktの画像の左３列分（0, 5, 15 minの画像）と
類似しており、画像の流用（データの捏造）が疑われます。
(A)- 指摘項目No.34
論文#2のFigure 4BのIkB-αの画像の一番左の列の画像（Contの画像）は、
論文#6のFigure 2(B)の一番上のp-Aktの画像の左から４列目の画像（30 minの画像）と
類似しており、画像の流用（データの捏造）が疑われます。
↓上記論文#2のFigure 1
© 2010 Elsevier Inc. All rights reserved.
Metabolism Clinical and Experimental xx (2010)
Fig. 1. A, Fenofibrate activates AMPK in microvascular endothelial cells.
Human glomerular microvascular endothelial cells were treated with
100 μmol/L fenofibrate for the indicated periods before lysis, after which
cell lysates were probed with antibodies specific for AMPK, ACC, Akt,
or eNOS, or their phosphorylated forms. B, Peroxisome proliferator–
activated receptor α antagonist MK886 did not affect fenofibrateinduced
AMPK activation, and PPARα agonist WY14643 scarcely
activated AMPK in HGMEC. C, Fenofibrate activates AMPK in
microvascular endothelial cells but not in hepatic cells. HepG2 cells
and HGMEC were treated with fenofibrate, WY14643, or bezafibrate for
15 minutes and analyzed with antibodies specific for AMPK or ACC.
Lower figure in Fig. 1C shows that fenofibrate did not activate AMPK
during indicated period in HepG2. Fe indicates fenofibrate (100 μmol/L);
MK, MK886 (100 μmol/L); WY, WY14643 (100 μmol/L); Be,
bezafibrate (100 μmol/L).
↓上記論文#2のFigure 4
© 2010 Elsevier Inc. All rights reserved.
Metabolism Clinical and Experimental xx (2010)
Fig. 4. A, Human glomerular microvascular endothelial cells were incubated
with AGE-BSA for 0 to 180 minutes. The cells were lysed and subjected to
Western blot analysis using anti-IκBα and anti–phospho-IκBα antibodies.
B, The effect of fenofibrate on IκB-α degradation in human umbilical vein
endothelial cells. Cells were incubated for 30 minutes with fenofibrate (30
and 100 μmol/L), followed by AGE-BSA for 15 minutes. Cells were then
lysed and subjected to Western blot analysis using anti-IκBα antibody. C,
The effect of fenofibrate on IKK activity in HGMEC. Cells were incubated
for 30 minutes with fenofibrate (30 and 100 μmol/L), followed by AGEBSA
for 15 minutes. Cells were then lysed and immunoprecipitated with
anti-IKKα/β antibody and used for kinase assay using recombinant IκB-α as
a substrate. Note that equal band densities for IKKα/β- and IκB-α were
observed. Similar results in 3 independent experiments were obtained, and
representative photographs are shown.
↓上記論文#6のFigure 2
© 2008 The Authors
Journal Compilation © 2008 Blackwell Publishing Ltd
Diabetes, Obesity and Metabolism, 11, 2009, 143–149
Fig. 2 (A) Effect of two specific PI3K inhibitors, wortmannin
(WT) and LY294002 (LY), on glimepiride-induced
nitric oxide (NO) production. Human umbilical vein endothelial
cells (HUVEC) were preincubated with WT
(100 nmol/l) or LY294002 (20 mmol/l) for 30 min, after
which the cells were incubated with glimepiride (10 mmol/
l) for 60 min, and released NO was measured. Results represent
the mean s.d. **p < 0.01 vs. glimepiride; n &#188; 3.
##p < 0.01 vs. basal; n &#188; 3. (B) Effect of glimepiride on
phosphorylation of Akt and endothelial NO synthase
(eNOS). HUVEC were incubated with glimepiride
(10 mmol/l) for the indicated times, and cell lysate samples
were prepared and subjected to Western blot analysis
using an antiphospho-Akt antibody and an antiphosphoeNOS
antibody.
↓上記論文#8のFigure 1 (A)(B)
© 2008 Elsevier Inc. All rights reserved.
Life Sciences 82 (2008) 884–891
Fig. 1. (A) Fenofibrate activates AMPK in vascular endothelial cells. HUVEC were treated with 100 μmol/L fenofibrate for the indicated time periods before lysis,
after which cell lysates were probed with antibodies specific for AMPK, ACC, Akt, or eNOS, or their phosphorylated forms. (B) WY14643 (100 μmol/L) activates
AMPK in HUVEC. (C) The chemiluminescence intensity for fenofibrate- and WY14643-induced phosphorylated AMPK from three independent experiments was
quantified. Each point represents the mean±SEM (n=3).
↓上記論文#8のFigure 5
© 2008 Elsevier Inc. All rights reserved.
Life Sciences 82 (2008) 884–891
Fig. 5. (A) HUVEC were incubated with TNFα for 0–180 min. The cells were
lysed and subjected to Western blot analysis using anti-IκB-α and anti-phospho-
IκB-α antibodies. (B) The effect of fenofibrate on IκB-α degradation in HUVEC.
Cells were incubated for 30 min with fenofibrate (30 and 100 μM), followed by
TNFα for 30 min. Cells were then lysed and subjected to Western blot analysis
using anti-IκB-α antibody. (C) The effect of fenofibrate on IKK activity in
HUVEC. Cells were incubated for 30 min with metformin (30 and 100 μM),
followed by TNFα for 15min. Cells were then lysed and immunoprecipitated with
anti-IKKα/β antibody and used for kinase assay using recombinant IκB-α as a
substrate. Note that equal band densities for IKKα/β- and IκB-α were observed.
Three independent experiments for (A) and (B) and two independent experiments
for (C) were performed. Similar results were obtained in each experiment and
representative photos were shown.
