The Experts below are selected from a list of 1419 Experts worldwide ranked by ideXlab platform
Hidekazu Suzuki - One of the best experts on this subject based on the ideXlab platform.
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helicobacter pylori vaca acting through receptor protein tyrosine phosphatase α is crucial for caga phosphorylation in human Duodenum Carcinoma cell line az 521
Disease Models & Mechanisms, 2016Co-Authors: Masayuki Nakano, Yoshio Yamaoka, Kinnosuke Yahiro, Eiki Yamasaki, Hisao Kurazono, Junko Akada, Takuro Niidome, Masanori Hatakeyama, Hidekazu SuzukiAbstract:Helicobacter pylori, a major cause of gastroduodenal diseases, produces vacuolating cytotoxin (VacA) and cytotoxin-associated gene A (CagA), which seem to be involved in virulence. VacA exhibits pleiotropic actions in gastroduodenal disorders via its specific receptors. Recently, we found that VacA induced the phosphorylation of cellular Src kinase (Src) at Tyr418 in AZ-521 cells. Silencing of receptor protein tyrosine phosphatase (RPTP)α, a VacA receptor, reduced VacA-induced Src phosphorylation. Src is responsible for tyrosine phosphorylation of CagA at its Glu-Pro-Ile-Tyr-Ala (EPIYA) variant C (EPIYA-C) motif in Helicobacter pylori-infected gastric epithelial cells, resulting in binding of CagA to SHP-2 phosphatase. Challenging AZ-521 cells with wild-type H. pylori induced phosphorylation of CagA, but this did not occur when challenged with a vacA gene-disrupted mutant strain. CagA phosphorylation was observed in cells infected with a vacA gene-disrupted mutant strain after addition of purified VacA, suggesting that VacA is required for H. pylori-induced CagA phosphorylation. Following siRNA-mediated RPTPα knockdown in AZ-521 cells, infection with wild-type H. pylori and treatment with VacA did not induce CagA phosphorylation. Taken together, these results support our conclusion that VacA mediates CagA phosphorylation through RPTPα in AZ-521 cells. These data indicate the possibility that Src phosphorylation induced by VacA is mediated through RPTPα, resulting in activation of Src, leading to CagA phosphorylation at Tyr972 in AZ-521 cells.
Yoshio Yamaoka - One of the best experts on this subject based on the ideXlab platform.
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helicobacter pylori vaca acting through receptor protein tyrosine phosphatase α is crucial for caga phosphorylation in human Duodenum Carcinoma cell line az 521
Disease Models & Mechanisms, 2016Co-Authors: Masayuki Nakano, Yoshio Yamaoka, Kinnosuke Yahiro, Eiki Yamasaki, Hisao Kurazono, Junko Akada, Takuro Niidome, Masanori Hatakeyama, Hidekazu SuzukiAbstract:Helicobacter pylori, a major cause of gastroduodenal diseases, produces vacuolating cytotoxin (VacA) and cytotoxin-associated gene A (CagA), which seem to be involved in virulence. VacA exhibits pleiotropic actions in gastroduodenal disorders via its specific receptors. Recently, we found that VacA induced the phosphorylation of cellular Src kinase (Src) at Tyr418 in AZ-521 cells. Silencing of receptor protein tyrosine phosphatase (RPTP)α, a VacA receptor, reduced VacA-induced Src phosphorylation. Src is responsible for tyrosine phosphorylation of CagA at its Glu-Pro-Ile-Tyr-Ala (EPIYA) variant C (EPIYA-C) motif in Helicobacter pylori-infected gastric epithelial cells, resulting in binding of CagA to SHP-2 phosphatase. Challenging AZ-521 cells with wild-type H. pylori induced phosphorylation of CagA, but this did not occur when challenged with a vacA gene-disrupted mutant strain. CagA phosphorylation was observed in cells infected with a vacA gene-disrupted mutant strain after addition of purified VacA, suggesting that VacA is required for H. pylori-induced CagA phosphorylation. Following siRNA-mediated RPTPα knockdown in AZ-521 cells, infection with wild-type H. pylori and treatment with VacA did not induce CagA phosphorylation. Taken together, these results support our conclusion that VacA mediates CagA phosphorylation through RPTPα in AZ-521 cells. These data indicate the possibility that Src phosphorylation induced by VacA is mediated through RPTPα, resulting in activation of Src, leading to CagA phosphorylation at Tyr972 in AZ-521 cells.
Masayuki Nakano - One of the best experts on this subject based on the ideXlab platform.
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helicobacter pylori vaca acting through receptor protein tyrosine phosphatase α is crucial for caga phosphorylation in human Duodenum Carcinoma cell line az 521
Disease Models & Mechanisms, 2016Co-Authors: Masayuki Nakano, Yoshio Yamaoka, Kinnosuke Yahiro, Eiki Yamasaki, Hisao Kurazono, Junko Akada, Takuro Niidome, Masanori Hatakeyama, Hidekazu SuzukiAbstract:Helicobacter pylori, a major cause of gastroduodenal diseases, produces vacuolating cytotoxin (VacA) and cytotoxin-associated gene A (CagA), which seem to be involved in virulence. VacA exhibits pleiotropic actions in gastroduodenal disorders via its specific receptors. Recently, we found that VacA induced the phosphorylation of cellular Src kinase (Src) at Tyr418 in AZ-521 cells. Silencing of receptor protein tyrosine phosphatase (RPTP)α, a VacA receptor, reduced VacA-induced Src phosphorylation. Src is responsible for tyrosine phosphorylation of CagA at its Glu-Pro-Ile-Tyr-Ala (EPIYA) variant C (EPIYA-C) motif in Helicobacter pylori-infected gastric epithelial cells, resulting in binding of CagA to SHP-2 phosphatase. Challenging AZ-521 cells with wild-type H. pylori induced phosphorylation of CagA, but this did not occur when challenged with a vacA gene-disrupted mutant strain. CagA phosphorylation was observed in cells infected with a vacA gene-disrupted mutant strain after addition of purified VacA, suggesting that VacA is required for H. pylori-induced CagA phosphorylation. Following siRNA-mediated RPTPα knockdown in AZ-521 cells, infection with wild-type H. pylori and treatment with VacA did not induce CagA phosphorylation. Taken together, these results support our conclusion that VacA mediates CagA phosphorylation through RPTPα in AZ-521 cells. These data indicate the possibility that Src phosphorylation induced by VacA is mediated through RPTPα, resulting in activation of Src, leading to CagA phosphorylation at Tyr972 in AZ-521 cells.
Weiming Kang - One of the best experts on this subject based on the ideXlab platform.
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investigation of tumor related anemia in 10 218 patients with cancer in the digestive system
Chinese Journal of Gastrointestinal Surgery, 2011Co-Authors: Weiming KangAbstract:Objective To study the prevalence of tumor related anemia in patients with cancer in the digestive system. Methods A total of of 10 218 inpatients were diagnosed with cancer in the digestive system at the Peking Union Hospital from Janary 2000 to June 2009, which included esophageal cancer(n=1118), gastric cancer(n=2418), Carcinoma of Duodenum(n=134), Carcinoma of small intestine(n=85), hepatocellular cancer(n= 1508), cholangioCarcinoma (n=546), pancreatic cancer (n=1242), colon cancer (n=1582), and rectal cancer (n=1585). Patients with hemolytic anemia or hepatorenal dysfunction were excluded. Data pertaining to sex, age and hemoglobin were obtained by chart review. Results According to the China criteria of anemia, the overall anemia rate was 27.5% (2813/10 218). The prevalence of anemia was 64.7% for small bowel cancer, 60.5% for duodenal cancer, 42.6% for colon cancer, 36.6% for cholangioCarcinoma, 33.3% for gastric cancer, 22.6% for pancreatic cancer, 20.4% for rectal cancer, 18.7% for hepatocellular cancer, and 10.0% for esophageal cancer. Anemia was more common in older patients in those with gastric cancer, cholangioCarcinoma, pancreatic cancer, colon cancer and rectal cancer. There were more male anemic patients in those with cancer in the small intestine or cholangioCarcinoma. However, females were more commonly seen in those with hepatocellular cancer or pancreatic cancer. Conclusions Anemia is common in patients with cancer in the digestive system. The prevalence of anemia is higher in patients with cancer in the Duodenum Carcinoma or small intestine, followed by colon cancer and gastric cancer, and then esophageal cancer. Anemia may be associated with age or gender in some types of cancer in the digestive system. Key words: Digestive system neoplasms; Anemia; Hemoglobin; Gender; Age
Kinnosuke Yahiro - One of the best experts on this subject based on the ideXlab platform.
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helicobacter pylori vaca acting through receptor protein tyrosine phosphatase α is crucial for caga phosphorylation in human Duodenum Carcinoma cell line az 521
Disease Models & Mechanisms, 2016Co-Authors: Masayuki Nakano, Yoshio Yamaoka, Kinnosuke Yahiro, Eiki Yamasaki, Hisao Kurazono, Junko Akada, Takuro Niidome, Masanori Hatakeyama, Hidekazu SuzukiAbstract:Helicobacter pylori, a major cause of gastroduodenal diseases, produces vacuolating cytotoxin (VacA) and cytotoxin-associated gene A (CagA), which seem to be involved in virulence. VacA exhibits pleiotropic actions in gastroduodenal disorders via its specific receptors. Recently, we found that VacA induced the phosphorylation of cellular Src kinase (Src) at Tyr418 in AZ-521 cells. Silencing of receptor protein tyrosine phosphatase (RPTP)α, a VacA receptor, reduced VacA-induced Src phosphorylation. Src is responsible for tyrosine phosphorylation of CagA at its Glu-Pro-Ile-Tyr-Ala (EPIYA) variant C (EPIYA-C) motif in Helicobacter pylori-infected gastric epithelial cells, resulting in binding of CagA to SHP-2 phosphatase. Challenging AZ-521 cells with wild-type H. pylori induced phosphorylation of CagA, but this did not occur when challenged with a vacA gene-disrupted mutant strain. CagA phosphorylation was observed in cells infected with a vacA gene-disrupted mutant strain after addition of purified VacA, suggesting that VacA is required for H. pylori-induced CagA phosphorylation. Following siRNA-mediated RPTPα knockdown in AZ-521 cells, infection with wild-type H. pylori and treatment with VacA did not induce CagA phosphorylation. Taken together, these results support our conclusion that VacA mediates CagA phosphorylation through RPTPα in AZ-521 cells. These data indicate the possibility that Src phosphorylation induced by VacA is mediated through RPTPα, resulting in activation of Src, leading to CagA phosphorylation at Tyr972 in AZ-521 cells.
