The Experts below are selected from a list of 258 Experts worldwide ranked by ideXlab platform
Jichao Wei - One of the best experts on this subject based on the ideXlab platform.
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Fructose-Bisphosphate Aldolase A Regulates Hypoxic Adaptation in Hepatocellular Carcinoma and Involved with Tumor Malignancy.
Digestive Diseases and Sciences, 2019Co-Authors: Fengxing Jiang, Bin Chen, Mingjun Xin, Jiandong Wang, Jichao WeiAbstract:Background Hypoxia is an important factor in malignant tumors, and glycolysis is a major metabolic contributor in their development. Glycolytic enzymes have gained increasing attention as potential therapeutic targets because they are associated with cancer-specific metabolism. Fructose-Bisphosphate Aldolase A (ALDOA), a key glycolytic enzyme, reportedly is associated with hepatocellular carcinoma (HCC). However, its role in pathogenesis and its clinical significance in HCC remain largely unknown. Aim To explore the increased expression of ALDOA in HCC in correlation with tumor malignancy, and to investigate the potential regulatory role ALDOA plays in HCC progression through its regulation in hypoxia adaptation. Methods and results To better understand ALDOA and its correlation with clinicopathological features of HCC, we analyzed 100 HCC clinical specimens using immunohistochemistry analysis. The results show that the ALDOA expression level is significantly higher in advanced HCC and in HCC with venous invasion. Using in vitro knockdown assays, we showed that higher ALDOA expression was positively associated with cell proliferation, cell cycle, apoptosis, and invasion under both normoxic and hypoxic conditions. Evidence shows that the underlying mechanism is due to the regulatory function of ALDOA in glycolysis, the cell cycle, matrix metalloproteinase-mediated extracellular matrix degradation, and epithelial-mesenchymal transformation. Conclusions Data indicated that ALDOA is significantly upregulated in HCC tissue and is closely related to HCC malignancy. ALDOA is likely to regulate HCC progression by regulating HCC tumor cell proliferation, apoptosis, and invasion in both normoxic and hypoxic condition.
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Fructose-Bisphosphate Aldolase A Regulates Hypoxic Adaptation in Hepatocellular Carcinoma and Involved with Tumor Malignancy.
Digestive diseases and sciences, 2019Co-Authors: Fengxing Jiang, Bin Chen, Mingjun Xin, Jiandong Wang, Jichao WeiAbstract:Hypoxia is an important factor in malignant tumors, and glycolysis is a major metabolic contributor in their development. Glycolytic enzymes have gained increasing attention as potential therapeutic targets because they are associated with cancer-specific metabolism. Fructose-Bisphosphate Aldolase A (ALDOA), a key glycolytic enzyme, reportedly is associated with hepatocellular carcinoma (HCC). However, its role in pathogenesis and its clinical significance in HCC remain largely unknown. To explore the increased expression of ALDOA in HCC in correlation with tumor malignancy, and to investigate the potential regulatory role ALDOA plays in HCC progression through its regulation in hypoxia adaptation. To better understand ALDOA and its correlation with clinicopathological features of HCC, we analyzed 100 HCC clinical specimens using immunohistochemistry analysis. The results show that the ALDOA expression level is significantly higher in advanced HCC and in HCC with venous invasion. Using in vitro knockdown assays, we showed that higher ALDOA expression was positively associated with cell proliferation, cell cycle, apoptosis, and invasion under both normoxic and hypoxic conditions. Evidence shows that the underlying mechanism is due to the regulatory function of ALDOA in glycolysis, the cell cycle, matrix metalloproteinase-mediated extracellular matrix degradation, and epithelial–mesenchymal transformation. Data indicated that ALDOA is significantly upregulated in HCC tissue and is closely related to HCC malignancy. ALDOA is likely to regulate HCC progression by regulating HCC tumor cell proliferation, apoptosis, and invasion in both normoxic and hypoxic condition.
Setsuko Komatsu - One of the best experts on this subject based on the ideXlab platform.
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Identification of rice root proteins regulated by gibberellin using proteome analysis
Plant Cell and Environment, 2005Co-Authors: H. Konishi, Hidemi Kitano, Setsuko KomatsuAbstract:Gibberellin (GA) promoted rice (Oryza sativa L.) root elongation in a concentration-dependent manner with roots grown in 0.1 micromolar GA3 being 13.8% longer than controls. On the other hand, the roots of Tan-ginbozu, a semi-dwarf cultivar were 69.8% shorter in comparison with Nipponbare, a normal cultivar. Treatments with 10 micromolar uniconazole-P and 10 micromolar abscisic acid (ABA) caused decreases in root length in Tan-ginbozu by 44.6 and 79.2%, respectively. To investigate how GA influences rice root growth, proteome analysis techniques were applied. Extracted proteins were separated by two-dimensional polyacrylamide gel electrophoresis and analysed using an automated protein sequencer and mass spectrometer. Sixteen proteins show differences in accumulation levels as a result of treatment with GA3, uniconazole-P and ABA treatment and/or the difference between the semi-dwarf cultivar, Tan-ginbozu, and normal cultivars. Among these proteins, Fructose-Bisphosphate Aldolase (EC 4.1.2.13) increased in roots treated with GA3, occurred in low levels in Tan-ginbozu roots, and decreased in roots treated with uniconazole-P or ABA. Moreover, roots from seedlings grown in 100 micromolar glucose were 9.1% longer than controls. These results indicate that increases in Fructose-Bisphosphate Aldolase activity stimulate the glycolytic pathway and may play an important role in the GA-induced growth of roots.
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Characterization of Fructose-Bisphosphate Aldolase regulated by gibberellin in roots of rice seedling
Plant Molecular Biology, 2004Co-Authors: Hirosato Konishi, Hisakazu Yamane, Masayoshi Maeshima, Setsuko KomatsuAbstract:Fructose-Bisphosphate Aldolase is a glycolytic enzyme whose activity increases in rice roots treated with gibberellin (GA). To investigate the relationship between Aldolase and root growth, GA-induced root Aldolase was characterized. GA_3 promoted an increase in Aldolase accumulation when 0.1 μ M GA_3 was added exogenously to rice roots. Aldolase accumulated abundantly in roots, especially in the apical region. To examine the effect of Aldolase function on root growth, transgenic rice plants expressing antisense Aldolase were constructed. Root growth of Aldolase-antisense transgenic rice was repressed compared with that of the vector control transgenic rice. Although Aldolase activity increased by 25% in vector control rice roots treated with 0.1 μ M GA_3, FBPA activity increased very little by 0.1 μ M GA_3 treatment in the root of Aldolase-antisense transgenic rice. Furthermore, Aldolase co-immunoprecipitated with antibodies against vacuolar H^+-ATPase in rice roots. In the root of OsCDPK13-antisense transgenic rice, Aldolase did not accumulate even after treatment with GA_3. These results suggest that the activation of glycolytic pathway function accelerates root growth and that GA_3-induced root Aldolase may be modulated through OsCDPK13. Aldolase physically associates with vacuolar H-ATPase in roots and may regulate the vacuolar H-ATPase mediated control of cell elongation that determines root length.
Muhammad Akhtar - One of the best experts on this subject based on the ideXlab platform.
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Pcal_0111, a highly thermostable bifunctional Fructose-1,6-Bisphosphate Aldolase/phosphatase from Pyrobaculum calidifontis
Extremophiles, 2017Co-Authors: Iram Aziz, Naeem Rashid, Raza Ashraf, Qamar Bashir, Tadayuki Imanaka, Muhammad AkhtarAbstract:Pyrobaculum calidifontis genome harbors an open reading frame Pcal_0111 annotated as Fructose Bisphosphate Aldolase. Although the gene is annotated as Fructose Bisphosphate Aldolase, it exhibits a high homology with previously reported Fructose-1,6-Bisphosphate Aldolase/phosphatase from Thermoproteus neutrophilus . To examine the biochemical properties of Pcal_0111, we have cloned and expressed the gene in Escherichia coli . Purified recombinant Pcal_0111 catalyzed both phosphatase and Aldolase reactions with specific activity values of 4 U and 1.3 U, respectively. These values are highest among the Fructose 1,6-bisphosphatases/Aldolases characterized from archaea. The enzyme activity increased linearly with the increase in temperature until 100 °C. Recombinant Pcal_0111 is highly stable with a half-life of 120 min at 100 °C. There was no significant change in the circular dichroism spectra of the protein up to 90 °C. The enzyme activity was not affected by AMP but strongly inhibited by ATP with an IC_50 value of 0.75 mM and mildly by ADP. High thermostability and inhibition by ATP make Pcal_0111 a unique Fructose 1,6-bisphosphatase/Aldolase.
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pcal_0111 a highly thermostable bifunctional Fructose 1 6 Bisphosphate Aldolase phosphatase from pyrobaculum calidifontis
Extremophiles, 2017Co-Authors: Iram Aziz, Naeem Rashid, Raza Ashraf, Qamar Bashir, Tadayuki Imanaka, Muhammad AkhtarAbstract:Pyrobaculum calidifontis genome harbors an open reading frame Pcal_0111 annotated as Fructose Bisphosphate Aldolase. Although the gene is annotated as Fructose Bisphosphate Aldolase, it exhibits a high homology with previously reported Fructose-1,6-Bisphosphate Aldolase/phosphatase from Thermoproteus neutrophilus. To examine the biochemical properties of Pcal_0111, we have cloned and expressed the gene in Escherichia coli. Purified recombinant Pcal_0111 catalyzed both phosphatase and Aldolase reactions with specific activity values of 4 U and 1.3 U, respectively. These values are highest among the Fructose 1,6-bisphosphatases/Aldolases characterized from archaea. The enzyme activity increased linearly with the increase in temperature until 100 °C. Recombinant Pcal_0111 is highly stable with a half-life of 120 min at 100 °C. There was no significant change in the circular dichroism spectra of the protein up to 90 °C. The enzyme activity was not affected by AMP but strongly inhibited by ATP with an IC50 value of 0.75 mM and mildly by ADP. High thermostability and inhibition by ATP make Pcal_0111 a unique Fructose 1,6-bisphosphatase/Aldolase.
Fengxing Jiang - One of the best experts on this subject based on the ideXlab platform.
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Fructose-Bisphosphate Aldolase A Regulates Hypoxic Adaptation in Hepatocellular Carcinoma and Involved with Tumor Malignancy.
Digestive Diseases and Sciences, 2019Co-Authors: Fengxing Jiang, Bin Chen, Mingjun Xin, Jiandong Wang, Jichao WeiAbstract:Background Hypoxia is an important factor in malignant tumors, and glycolysis is a major metabolic contributor in their development. Glycolytic enzymes have gained increasing attention as potential therapeutic targets because they are associated with cancer-specific metabolism. Fructose-Bisphosphate Aldolase A (ALDOA), a key glycolytic enzyme, reportedly is associated with hepatocellular carcinoma (HCC). However, its role in pathogenesis and its clinical significance in HCC remain largely unknown. Aim To explore the increased expression of ALDOA in HCC in correlation with tumor malignancy, and to investigate the potential regulatory role ALDOA plays in HCC progression through its regulation in hypoxia adaptation. Methods and results To better understand ALDOA and its correlation with clinicopathological features of HCC, we analyzed 100 HCC clinical specimens using immunohistochemistry analysis. The results show that the ALDOA expression level is significantly higher in advanced HCC and in HCC with venous invasion. Using in vitro knockdown assays, we showed that higher ALDOA expression was positively associated with cell proliferation, cell cycle, apoptosis, and invasion under both normoxic and hypoxic conditions. Evidence shows that the underlying mechanism is due to the regulatory function of ALDOA in glycolysis, the cell cycle, matrix metalloproteinase-mediated extracellular matrix degradation, and epithelial-mesenchymal transformation. Conclusions Data indicated that ALDOA is significantly upregulated in HCC tissue and is closely related to HCC malignancy. ALDOA is likely to regulate HCC progression by regulating HCC tumor cell proliferation, apoptosis, and invasion in both normoxic and hypoxic condition.
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Fructose-Bisphosphate Aldolase A Regulates Hypoxic Adaptation in Hepatocellular Carcinoma and Involved with Tumor Malignancy.
Digestive diseases and sciences, 2019Co-Authors: Fengxing Jiang, Bin Chen, Mingjun Xin, Jiandong Wang, Jichao WeiAbstract:Hypoxia is an important factor in malignant tumors, and glycolysis is a major metabolic contributor in their development. Glycolytic enzymes have gained increasing attention as potential therapeutic targets because they are associated with cancer-specific metabolism. Fructose-Bisphosphate Aldolase A (ALDOA), a key glycolytic enzyme, reportedly is associated with hepatocellular carcinoma (HCC). However, its role in pathogenesis and its clinical significance in HCC remain largely unknown. To explore the increased expression of ALDOA in HCC in correlation with tumor malignancy, and to investigate the potential regulatory role ALDOA plays in HCC progression through its regulation in hypoxia adaptation. To better understand ALDOA and its correlation with clinicopathological features of HCC, we analyzed 100 HCC clinical specimens using immunohistochemistry analysis. The results show that the ALDOA expression level is significantly higher in advanced HCC and in HCC with venous invasion. Using in vitro knockdown assays, we showed that higher ALDOA expression was positively associated with cell proliferation, cell cycle, apoptosis, and invasion under both normoxic and hypoxic conditions. Evidence shows that the underlying mechanism is due to the regulatory function of ALDOA in glycolysis, the cell cycle, matrix metalloproteinase-mediated extracellular matrix degradation, and epithelial–mesenchymal transformation. Data indicated that ALDOA is significantly upregulated in HCC tissue and is closely related to HCC malignancy. ALDOA is likely to regulate HCC progression by regulating HCC tumor cell proliferation, apoptosis, and invasion in both normoxic and hypoxic condition.
Bin Chen - One of the best experts on this subject based on the ideXlab platform.
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Fructose-Bisphosphate Aldolase A Regulates Hypoxic Adaptation in Hepatocellular Carcinoma and Involved with Tumor Malignancy.
Digestive Diseases and Sciences, 2019Co-Authors: Fengxing Jiang, Bin Chen, Mingjun Xin, Jiandong Wang, Jichao WeiAbstract:Background Hypoxia is an important factor in malignant tumors, and glycolysis is a major metabolic contributor in their development. Glycolytic enzymes have gained increasing attention as potential therapeutic targets because they are associated with cancer-specific metabolism. Fructose-Bisphosphate Aldolase A (ALDOA), a key glycolytic enzyme, reportedly is associated with hepatocellular carcinoma (HCC). However, its role in pathogenesis and its clinical significance in HCC remain largely unknown. Aim To explore the increased expression of ALDOA in HCC in correlation with tumor malignancy, and to investigate the potential regulatory role ALDOA plays in HCC progression through its regulation in hypoxia adaptation. Methods and results To better understand ALDOA and its correlation with clinicopathological features of HCC, we analyzed 100 HCC clinical specimens using immunohistochemistry analysis. The results show that the ALDOA expression level is significantly higher in advanced HCC and in HCC with venous invasion. Using in vitro knockdown assays, we showed that higher ALDOA expression was positively associated with cell proliferation, cell cycle, apoptosis, and invasion under both normoxic and hypoxic conditions. Evidence shows that the underlying mechanism is due to the regulatory function of ALDOA in glycolysis, the cell cycle, matrix metalloproteinase-mediated extracellular matrix degradation, and epithelial-mesenchymal transformation. Conclusions Data indicated that ALDOA is significantly upregulated in HCC tissue and is closely related to HCC malignancy. ALDOA is likely to regulate HCC progression by regulating HCC tumor cell proliferation, apoptosis, and invasion in both normoxic and hypoxic condition.
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Fructose-Bisphosphate Aldolase A Regulates Hypoxic Adaptation in Hepatocellular Carcinoma and Involved with Tumor Malignancy.
Digestive diseases and sciences, 2019Co-Authors: Fengxing Jiang, Bin Chen, Mingjun Xin, Jiandong Wang, Jichao WeiAbstract:Hypoxia is an important factor in malignant tumors, and glycolysis is a major metabolic contributor in their development. Glycolytic enzymes have gained increasing attention as potential therapeutic targets because they are associated with cancer-specific metabolism. Fructose-Bisphosphate Aldolase A (ALDOA), a key glycolytic enzyme, reportedly is associated with hepatocellular carcinoma (HCC). However, its role in pathogenesis and its clinical significance in HCC remain largely unknown. To explore the increased expression of ALDOA in HCC in correlation with tumor malignancy, and to investigate the potential regulatory role ALDOA plays in HCC progression through its regulation in hypoxia adaptation. To better understand ALDOA and its correlation with clinicopathological features of HCC, we analyzed 100 HCC clinical specimens using immunohistochemistry analysis. The results show that the ALDOA expression level is significantly higher in advanced HCC and in HCC with venous invasion. Using in vitro knockdown assays, we showed that higher ALDOA expression was positively associated with cell proliferation, cell cycle, apoptosis, and invasion under both normoxic and hypoxic conditions. Evidence shows that the underlying mechanism is due to the regulatory function of ALDOA in glycolysis, the cell cycle, matrix metalloproteinase-mediated extracellular matrix degradation, and epithelial–mesenchymal transformation. Data indicated that ALDOA is significantly upregulated in HCC tissue and is closely related to HCC malignancy. ALDOA is likely to regulate HCC progression by regulating HCC tumor cell proliferation, apoptosis, and invasion in both normoxic and hypoxic condition.
