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Helicobacter pylori γ-Glutamyltranspeptidase Induces Cell Cycle Arrest at the G1-S Phase Transition
Kyung-Mi Kim,Seung-Gyu Lee,Jung-Min Kim,Do-Su Kim,Jea-Young Song,Hyung-Lyun Kang,Woo-Kon Lee,Myung-Je Cho,Kwang-Ho Rhee,윤희상,Seung-Chul Baik 한국미생물학회 2010 The journal of microbiology Vol.48 No.3
In our previous study, we showed that Helicobacter pylori γ-glutamyltranspeptidase (GGT) is associated with H. pylori-induced apoptosis through a mitochondrial pathway. To better understand the role of GGT in apoptosis, we examined the effect of GGT on cell cycle regulation in AGS cells. To determine the effect of recombinant GGT (rGGT) on cell cycle distribution and apoptosis, rGGT-treated and untreated AGS cells were analyzed in parallel by flow cytometry using propidium iodide (PI). We found that rGGT inhibited the growth of AGS cells in a time-dependent manner, and that the pre-exposure of cells to a caspase-3 inhibitor (z-DEVD-fmk) effectively blocked GGT-induced apoptosis. Cell cycle analysis showed G1 phase arrest and apoptosis in AGS cells following rGGT treatment. The rGGT-mediated G1 phase arrest was found to be associated with down-regulation of cyclin E, cyclin A, Cdk 4, and Cdk 6, and the up-regulation of the cyclindependent kinase (Cdk) inhibitors p27 and p21. Our results suggest that H. pylori GGT induces cell cycle arrest at the G1-S phase transition.
Kim, Kyung-Mi,Lee, Seung-Gyu,Cho, Young-A,Song, Yun-Gyu,Song, Jea-Young,Kang, Hyung-Lyun,Lee, Woo-Kon,Cho, Myung-Je,Rhee, Kwang-Ho,Baik, Seung-Chul The Korean Society for Microbiology 2010 Journal of Bacteriology and Virology Vol.40 No.3
As part of an initial inquiry into the function of the outer membrane proteins (OMPs) of Helicobacter pylori Korean strain 51, we have conducted an extensive proteome analysis via quadrupole time of flight (Q-TOF) mass spectrometry (MS). Fifty one OMPs of H. pylori were purified using sarcosine and resolved via two-dimensional electrophoresis with immobilized pH gradient strips. The most abundant proteins were observed in the alkaline pI regions (6.0~11.0) at molecular masses between 10~100 KDa. Here, 15 spots were identified, representing 9 types of genes (KHP0852, KHP0853, KHP1353, KHP1017, KHP0172, KHP0076, KHP0617, KHP1069, KHP0614) from the sarcosin-insoluble fraction of H. pylori 51. These may be employed in the characterization of the OMPs of H. pylori 51, which will help to identify new potential target proteins for vaccine development and drug therapy.
Proteomic analysis of Helicobacter pylori J99 Outer Membrane Protein by Tandem Mass Spectrometry
Kim, Kyung-Mi,Lee, Seung-Gyu,Joo, Jung-Soo,Kwon, Young-Chul,Bea, Dong-Won,Song, Jea-Young,Kang, Hyung-Lyun,Lee, Woo-Kon,Cho, Myung-Je,Rhee, Kwang-Ho,Youn, Hee-Shang,Baik, Seung-Chul The Korean Society for Microbiology 2008 Journal of Bacteriology and Virology Vol.38 No.2
The protein identity of sarcosine-insoluble outer membrane proteins (OMPs) of Helicobacter pylori J99 was determined with the basic study of understanding the function of proteins. A sarcosine-insoluble OMPs was resolved by two-dimensional electrophoresis with immobilized pH gradient strips. The most abundant proteins were shown in the alkaline pI regions $(6.0{\sim}11.0)$ with molecular masses of 10 to 100kDa. We have performed an extensive proteome analysis by quadrupole time of flight (Q-TOF) mass spectrometry (MS). Here, of 50 spots processed, 42 spots were identified, which represented 16 genes and we newly detected 8 kinds of proteins (JHP0119, JHP0388, JHP1046, JHP1405, JHP0073, JHP0551, JHP1382, JHP0552) from the sarcosin-insoluble fraction of H. pylori J99. Those may be used to elucidate the characterization of the OMPs of H. pylori J99, which will help identify new potential target proteins for vaccine development and drug therapy.
Proteomic analysis of Helicobacter pylori J99 Outer Membrane Protein by Tandem Mass Spectrometry
Kyung-Mi Kim,Seung-Gyu Lee,Jung-Soo Joo,Young-Chul Kwon,Dong-Won Bea,Jea-Young Song,Hyung-Lyun Kang,Woo-Kon Lee,Myung-Je Cho,Kwang-Ho Rhee,Hee-Shang Youn,Seung-Chul Baik 대한미생물학회 2008 Journal of Bacteriology and Virology Vol.38 No.2
Park, Eun-Hee,Kim, Jung-Min,Kim, Kyung-Mi,Kang, Dawon,Cho, Young-Ah,Choi, Jun-Young,Song, Jea-Young,Kang, Hyung-Lyun,Lee, Woo-Kon,Cho, Myung-Je,Rhee, Kwang-Ho,Seo, Ji-Hyun,Youn, Hee-Shang,Baik, Seung- Canadian Science Publishing 2014 Canadian journal of microbiology Vol.60 No.12
<P> In our previous study, γ-glutamyl transpeptidase (GGT) isolated from Helicobacter pylori induced apoptosis of AGS cells. Here, we investigate Ca<SUP>2+</SUP> effects on GGT-induced apoptosis. The GGT transiently and significantly increased intracellular Ca<SUP>2+</SUP> concentration ([Ca<SUP>2+</SUP>]i) in AGS cells in a dose-dependent manner (P @@<@@ 0.05). The GGT-induced Ca<SUP>2+</SUP> increase resulted from Ca<SUP>2+</SUP> influx and release through the phospholipase C - inositol 1,4,5-trisphosphate (PLC-IP3) pathway. The GGT-induced apoptosis was significantly reduced by treatment with U73122 (a PLC inhibitor) and xestospongin (an IP3 receptor antagonist) (P @@<@@ 0.05). These results indicate that GGT could induce apoptosis of AGS cells by high levels of [Ca<SUP>2+</SUP>]i. </P>