MOESM1 of Differences in amino acid frequency in CagA and VacA sequences of Helicobacter pylori distinguish gastric cancer from gastric MALT lymphoma

Additional file 1: Table S1. Accession numbers of the cagA and vacA gene sequences

MOESM4 of Helicobacter pylori virulence genes of minor ethnic groups in North Thailand

Additional file 4. Population of H. pylori Maesot strains by STRUCTURE. The H. pylori strains from 24 Thai, 20 Hmong, 15 Karen and 7 Thai-Chinese were analyzed by STRUCTURE with K from 8–15. Each horizontal bar represent one strain, and the color in a line are proportional to the probabilities that the strain belong to each population. Each color square represented the strain from Thai, Hmong, Karen and Thai-Chinese. The H. pylori Maesot strains were hspEAsia, hpAsia2 and hpEurope. Interestingly, H. pylori Hmong and Thai-Chinese strains were located in hspEAsia while H. pylori Karen strains were belonged to hpAsia2. Thai H. pylori strains were located in three population

Bulletin mensuel de statistique / Institut national de la statistique et des études économiques...

juillet 19771977/07 (N7,A28)

MOESM3 of Differences in amino acid frequency in CagA and VacA sequences of Helicobacter pylori distinguish gastric cancer from gastric MALT lymphoma

Additional file 3: Figure S2. Phylogenetic tree of only 18 GC and 12 MALT strains. The star-like topology of this tree implies that these strains are genetically homogenous, and that their population has no clear structure (NJ-tree; Kimura-2 parameters; MEGA v. 6.0)

Serum starvation induces activation and different localization of extracellular ERK between KLM1 and KLM1-R cells.

<p>(A) KLM1 and KLM1-R cells were cultured in medium with or without FBS or exposed to 10 μg/mL of GEM for 24 h. Cell lysates were resolved by SDS-PAGE and probed with specific antibodies against p-ERK and ERK. (B) and (C) The indicated cells were stained with specific antibodies against p-ERK, Hsp27 and LC3A/B after cells were cultured in medium with or without FBS for 24 h. DAPI: blue and p-ERK: red in (B) and LC3A/B: green and Hsp27: red in (C). Scale bar, 20 μm.</p

Gemcitabine Induces Poly (ADP-Ribose) Polymerase-1 (PARP-1) Degradation through Autophagy in Pancreatic Cancer

<div><p>Poly (ADP-ribose) polymerase-1 (PARP-1) and autophagy play increasingly important roles in DNA damage repair and cell death. Gemcitabine (GEM) remains the first-line chemotherapeutic drug for pancreatic cancer (PC). However, little is known about the relationship between PARP-1 expression and autophagy in response to GEM. Here we demonstrate that GEM induces DNA-damage response and degradation of mono-ADP ribosylated PARP-1 through the autophagy pathway in PC cells, which is rescued by inhibiting autophagy. Hypoxia and serum starvation inhibit autophagic activity due to abrogated GEM-induced mono-ADP-ribosylated PARP-1 degradation. Activation of extracellular regulated protein kinases (ERK) induced by serum starvation shows differences in intracellular localization as well as modulation of autophagy and PARP-1 degradation in GEM-sensitive KLM1 and -resistant KLM1-R cells. Our study has revealed a novel role of autophagy in PARP-1 degradation in response to GEM, and the different impacts of MEK/ERK signaling pathway on autophagy between GEM-sensitive and -resistant PC cells.</p></div

MOESM4 of Helicobacter pylori virulence genes of minor ethnic groups in North Thailand

Additional file 4. Population of H. pylori Maesot strains by STRUCTURE. The H. pylori strains from 24 Thai, 20 Hmong, 15 Karen and 7 Thai-Chinese were analyzed by STRUCTURE with K from 8–15. Each horizontal bar represent one strain, and the color in a line are proportional to the probabilities that the strain belong to each population. Each color square represented the strain from Thai, Hmong, Karen and Thai-Chinese. The H. pylori Maesot strains were hspEAsia, hpAsia2 and hpEurope. Interestingly, H. pylori Hmong and Thai-Chinese strains were located in hspEAsia while H. pylori Karen strains were belonged to hpAsia2. Thai H. pylori strains were located in three population

GEM induces autophagy in PC cells.

<p>(A) The expression of Hsp27 was tested by western blot and the relative intensity was measured by student-<i>t</i> test (n = 3) (B) KLM1 and KLM1-R cells were lysed and resolved by SDS-PAGE and probed with specific antibodies. Actin was used to normalize the loading levels of protein. (C) The indicated cells were treated with 100 μg/mL of GEM for 5 h and the expression of LC3A/B and formation of LC3-positive autophagosomes were examined by confocal microscopy. LC3A/B: green and DAPI: blue. Arrows indicate the autophagosome. Scale bar, 20 μm.</p

GEM down-regulates mono-ADP ribosylated PARP-1 in a caspase-independent manner.

<p>(A) KLM1 and KLM1-R cells were treated by GEM with the indicated concentrations for 24 h. Cell lysates were resolved in SDS-PAGE and probed with specific antibodies. The expression of PARP-1 was confirmed repeatedly by a distinct PARP-1 antibody described in Materials. An arrow head indicated the mono-ADP ribosylated form of PARP-1. Arrows indicated the position area of cleaved caspase-3. (B) The indicated cells were treated as in (A) and then stained using a caspases 3/7 assay kit (A). Caspase 3/7 activity was tested and measured by confocal microscopy and Image J. N.S., non significant. Error bars, SD.</p

Serum starvation suppresses GEM-induced PARP-1 degradation through inhibition of autophagy via the ERK signaling pathway.

<p>(A) KLM1 and KLM1-R cells were exposed to 10 μg/mL of GEM in the presence or absence of 20 μM of U0126 for the indicated time courses. Cell lysates were resolved by SDS-PAGE and probed with specific antibodies against p-ERK and LC3A/B. (B) and (C) KLM1 and KLM1-R cells were cultured in the medium with or without FBS and meanwhile exposed to either or both GEM and U0126 at the indicated concentration. Cell lysates were resolved by SDS-PAGE and probed with specific antibodies. The arrow head indicates the mono-ADP ribosylated form of PARP-1. Arrows indicate the position area of cleaved caspase-3. The expression of PARP-1 was confirmed repeatedly by a distinct PARP-1 antibody described in Materials.</p