The Experts below are selected from a list of 36579 Experts worldwide ranked by ideXlab platform
Jonathan W Said - One of the best experts on this subject based on the ideXlab platform.
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Bcl-2 Oncogene Protein is preferentially expressed in Reed-Sternberg cells in Hodgkin's disease of the nodular sclerosis subtype.
American Journal of Clinical Pathology, 1994Co-Authors: Mark A. Lones, Shintaku Ip, Geraldine S Pinkus, Jonathan W SaidAbstract:One hundred three cases of nodular sclerosis (NS) and mixed-cellularity Hodgkin's disease were evaluated for expression of bcl-2 Oncogene Protein, because previous studies have revealed expression of bcl-2 in these subtypes but only rarely in the nodular lymphocyte-predominance subtype. Reed-Sternberg (RS) cells and lacunar variants were positive for lcf-2 in 57 of 86 NS cases and 4 of 77 mixed-cellularity cases. In individual cases of NS, the percentage of RS cells and lacunar variants positive for lcf-2 ranged from minimal (in 5 cases) to 700% positive (mean, 34%). By univariate analysis, expression of the bcl-2 gene product in RS cells was observed in a significantly greater proportion of NS Hodgkin's disease cases than MC cases (P
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bcl 2 Oncogene Protein is preferentially expressed in reed sternberg cells in hodgkin s disease of the nodular sclerosis subtype
American Journal of Clinical Pathology, 1994Co-Authors: Mark A. Lones, I. Peter Shintaku, Geraldine S Pinkus, Jonathan W SaidAbstract:One hundred three cases of nodular sclerosis (NS) and mixed-cellularity Hodgkin's disease were evaluated for expression of bcl-2 Oncogene Protein, because previous studies have revealed expression of bcl-2 in these subtypes but only rarely in the nodular lymphocyte-predominance subtype. Reed-Sternberg (RS) cells and lacunar variants were positive for lcf-2 in 57 of 86 NS cases and 4 of 77 mixed-cellularity cases. In individual cases of NS, the percentage of RS cells and lacunar variants positive for lcf-2 ranged from minimal (in 5 cases) to 700% positive (mean, 34%). By univariate analysis, expression of the bcl-2 gene product in RS cells was observed in a significantly greater proportion of NS Hodgkin's disease cases than MC cases (P<.009), a finding that may have implications on the pathogenesis of this disorder
Kei Satoh - One of the best experts on this subject based on the ideXlab platform.
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Polyinosinic-Polycytidylic Acid Induces the Expression of GRO-α in BEAS-2B Cells
Inflammation, 2005Co-Authors: Koji Yamashita, Tadaatsu Imaizumi, Hidemi Yoshida, Kageaki Taima, Takashi Fujita, Akira Ishikawa, Chikara Oyama, Kei SatohAbstract:Growth-related Oncogene Protein-α (GRO-α)/CXCLl is a chemokine that activates neutrophils and plays an important role in inflammatory reactions. Polyinosinic-polycytidylic acid (poly IC) is a synthetic double-stranded RNA (dsRNA), which is a ligand for Toll-like receptor-3. Poly IC mimics viral infection when applied to cells and induces inflammatory and immune responses. In the present study, we found the induction of GRO-α in BEAS-2B bronchial epithelial cells treated with poly IC. Pretreatment of cells with 2-aminopurine, an inhibitor for dsRNA-dependent Protein kinase (PKR), inhibited the expression of GRO-α-induced by poly IC. Overexpression of interferon-regulatory factor-3 (IRF-3) or retinoic-acid inducible gene-I (RIG-I) enhanced the induction of GRO-α by poly IC. PKR, IRF-3, and RIG-I may be involved in the poly IC-induced expression of GRO-α in BEAS-2B cells. Airway viral infection may elicit GRO-α expression in the bronchial epithelium, which may be implicated in inflammatory and immune reactions.
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Polyinosinic-Polycytidylic Acid Induces the Expression of GRO-α in BEAS-2B Cells
Inflammation, 2005Co-Authors: Koji Yamashita, Tadaatsu Imaizumi, Hidemi Yoshida, Kageaki Taima, Takashi Fujita, Akira Ishikawa, Chikara Oyama, Kei SatohAbstract:Growth-related Oncogene Protein-α (GRO-α)/CXCLl is a chemokine that activates neutrophils and plays an important role in inflammatory reactions. Polyinosinic-polycytidylic acid (poly IC) is a synthetic double-stranded RNA (dsRNA), which is a ligand for Toll-like receptor-3. Poly IC mimics viral infection when applied to cells and induces inflammatory and immune responses. In the present study, we found the induction of GRO-α in BEAS-2B bronchial epithelial cells treated with poly IC. Pretreatment of cells with 2-aminopurine, an inhibitor for dsRNA-dependent Protein kinase (PKR), inhibited the expression of GRO-α-induced by poly IC. Overexpression of interferon-regulatory factor-3 (IRF-3) or retinoic-acid inducible gene-I (RIG-I) enhanced the induction of GRO-α by poly IC. PKR, IRF-3, and RIG-I may be involved in the poly IC-induced expression of GRO-α in BEAS-2B cells. Airway viral infection may elicit GRO-α expression in the bronchial epithelium, which may be implicated in inflammatory and immune reactions.
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Effect of MG132, a proteasome inhibitor, on the expression of growth related Oncogene Protein-α in human umbilical vein endothelial cells
Cytokine, 2003Co-Authors: Takeo Shibata, Tadaatsu Imaizumi, Hidemi Yoshida, Tomoh Matsumiya, Wakako Tamo, Masaharu Hatakeyama, Hirohumi Munakata, Ikuo Fukuda, Kei SatohAbstract:Abstract Growth related Oncogene Protein-α (GRO-α) is a member of C-X-C chemokine and plays an important role in inflammatory responses. Expression of GRO gene family is regulated by a number of factors at both transcriptional and posttranscriptional levels. In the present study, we have addressed the possible regulation of GRO-α expression by ubiquitin–proteasome system. Cultures of human umbilical vein endothelial cells were treated with a proteasome inhibitor, MG132, and the levels of GRO-α mRNA were analyzed by reverse transcription-polymerase chain reaction or northern blotting. Levels of GRO-α Protein in the cell-conditioned medium were determined by enzyme-linked immunosorbent assay. MG132 alone increased the levels of GRO-α mRNA and Protein; however, it did not affect the GRO-α mRNA induced by lipopolysaccharide (LPS) and inhibited the LPS-induced decrease in IκB levels. Other proteasome inhibitors, MG115 and lactacystin, also induced the expression of GRO-α mRNA. MG132 induced the phosphorylation of p38 MAPK, MEK and JNK. Pretreatment of the cells with SB203580, an inhibitor of p38 MAPK, suppressed the MG132-induced GRO-α expression, but pretreatment of the cells with U0126, PD98059 or SP600125, inhibitors of MEK1/2 or JNK, did not influence the effect of MG132. We conclude that MG132 upregulates GRO-α expression in vascular endothelial cells, at least in part, through the activation of p38 MAPK.
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production of growth related Oncogene Protein α in human umbilical vein endothelial cells stimulated with soluble interleukin 6 receptor α role of signal transducers janus kinase 2 and mitogen activated kinase kinase
Life Sciences, 2002Co-Authors: Tomoh Matsumiya, Tadaatsu Imaizumi, Hidemi Yoshida, Takeo Shibata, Hiroyuki Itaya, Hirotaka Sakaki, Hiroto Kimura, Kei SatohAbstract:Abstract Growth-related Oncogene Protein-α (GRO-α) is a member of the C-X-C chemokine family with a wide variety of biological activities. We studied the production of GRO-α by human umbilical vein endothelial cells (HUVEC) in response to the stimulation with soluble form of interleukin-6 receptor α (sIL-6R). sIL-6R stimulated HUVEC to express GRO-α mRNA and secrete GRO-α Protein in concentration-and time-dependent manners. The sIL-6R-induced GRO-α expression was inhibited by the pretreatment of the cells with AG490, a janus kinase 2 (JAK2) inhibitor, or with U0126, a MAP kinase-ERK kinase (MEK) inhibitor. sIL-6R also induced the phosphorylation of both Src homology 2-Protein tyrosine phosphatase-2 (SHP-2), signal transducer and activator of transcription 3 (STAT3) and MEK. AG490 pretreatment inhibited the MEK phosphorylation but did not affect the STAT3 phosphorylation. We conclude that sIL-6R induces GRO-α expression in HUVEC through the activation of JAK2 and MEK.
Mark A. Lones - One of the best experts on this subject based on the ideXlab platform.
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Bcl-2 Oncogene Protein is preferentially expressed in Reed-Sternberg cells in Hodgkin's disease of the nodular sclerosis subtype.
American Journal of Clinical Pathology, 1994Co-Authors: Mark A. Lones, Shintaku Ip, Geraldine S Pinkus, Jonathan W SaidAbstract:One hundred three cases of nodular sclerosis (NS) and mixed-cellularity Hodgkin's disease were evaluated for expression of bcl-2 Oncogene Protein, because previous studies have revealed expression of bcl-2 in these subtypes but only rarely in the nodular lymphocyte-predominance subtype. Reed-Sternberg (RS) cells and lacunar variants were positive for lcf-2 in 57 of 86 NS cases and 4 of 77 mixed-cellularity cases. In individual cases of NS, the percentage of RS cells and lacunar variants positive for lcf-2 ranged from minimal (in 5 cases) to 700% positive (mean, 34%). By univariate analysis, expression of the bcl-2 gene product in RS cells was observed in a significantly greater proportion of NS Hodgkin's disease cases than MC cases (P
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bcl 2 Oncogene Protein is preferentially expressed in reed sternberg cells in hodgkin s disease of the nodular sclerosis subtype
American Journal of Clinical Pathology, 1994Co-Authors: Mark A. Lones, I. Peter Shintaku, Geraldine S Pinkus, Jonathan W SaidAbstract:One hundred three cases of nodular sclerosis (NS) and mixed-cellularity Hodgkin's disease were evaluated for expression of bcl-2 Oncogene Protein, because previous studies have revealed expression of bcl-2 in these subtypes but only rarely in the nodular lymphocyte-predominance subtype. Reed-Sternberg (RS) cells and lacunar variants were positive for lcf-2 in 57 of 86 NS cases and 4 of 77 mixed-cellularity cases. In individual cases of NS, the percentage of RS cells and lacunar variants positive for lcf-2 ranged from minimal (in 5 cases) to 700% positive (mean, 34%). By univariate analysis, expression of the bcl-2 gene product in RS cells was observed in a significantly greater proportion of NS Hodgkin's disease cases than MC cases (P<.009), a finding that may have implications on the pathogenesis of this disorder
Tomoh Matsumiya - One of the best experts on this subject based on the ideXlab platform.
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Effect of MG132, a proteasome inhibitor, on the expression of growth related Oncogene Protein-α in human umbilical vein endothelial cells
Cytokine, 2003Co-Authors: Takeo Shibata, Tadaatsu Imaizumi, Hidemi Yoshida, Tomoh Matsumiya, Wakako Tamo, Masaharu Hatakeyama, Hirohumi Munakata, Ikuo Fukuda, Kei SatohAbstract:Abstract Growth related Oncogene Protein-α (GRO-α) is a member of C-X-C chemokine and plays an important role in inflammatory responses. Expression of GRO gene family is regulated by a number of factors at both transcriptional and posttranscriptional levels. In the present study, we have addressed the possible regulation of GRO-α expression by ubiquitin–proteasome system. Cultures of human umbilical vein endothelial cells were treated with a proteasome inhibitor, MG132, and the levels of GRO-α mRNA were analyzed by reverse transcription-polymerase chain reaction or northern blotting. Levels of GRO-α Protein in the cell-conditioned medium were determined by enzyme-linked immunosorbent assay. MG132 alone increased the levels of GRO-α mRNA and Protein; however, it did not affect the GRO-α mRNA induced by lipopolysaccharide (LPS) and inhibited the LPS-induced decrease in IκB levels. Other proteasome inhibitors, MG115 and lactacystin, also induced the expression of GRO-α mRNA. MG132 induced the phosphorylation of p38 MAPK, MEK and JNK. Pretreatment of the cells with SB203580, an inhibitor of p38 MAPK, suppressed the MG132-induced GRO-α expression, but pretreatment of the cells with U0126, PD98059 or SP600125, inhibitors of MEK1/2 or JNK, did not influence the effect of MG132. We conclude that MG132 upregulates GRO-α expression in vascular endothelial cells, at least in part, through the activation of p38 MAPK.
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production of growth related Oncogene Protein α in human umbilical vein endothelial cells stimulated with soluble interleukin 6 receptor α role of signal transducers janus kinase 2 and mitogen activated kinase kinase
Life Sciences, 2002Co-Authors: Tomoh Matsumiya, Tadaatsu Imaizumi, Hidemi Yoshida, Takeo Shibata, Hiroyuki Itaya, Hirotaka Sakaki, Hiroto Kimura, Kei SatohAbstract:Abstract Growth-related Oncogene Protein-α (GRO-α) is a member of the C-X-C chemokine family with a wide variety of biological activities. We studied the production of GRO-α by human umbilical vein endothelial cells (HUVEC) in response to the stimulation with soluble form of interleukin-6 receptor α (sIL-6R). sIL-6R stimulated HUVEC to express GRO-α mRNA and secrete GRO-α Protein in concentration-and time-dependent manners. The sIL-6R-induced GRO-α expression was inhibited by the pretreatment of the cells with AG490, a janus kinase 2 (JAK2) inhibitor, or with U0126, a MAP kinase-ERK kinase (MEK) inhibitor. sIL-6R also induced the phosphorylation of both Src homology 2-Protein tyrosine phosphatase-2 (SHP-2), signal transducer and activator of transcription 3 (STAT3) and MEK. AG490 pretreatment inhibited the MEK phosphorylation but did not affect the STAT3 phosphorylation. We conclude that sIL-6R induces GRO-α expression in HUVEC through the activation of JAK2 and MEK.
Takeo Shibata - One of the best experts on this subject based on the ideXlab platform.
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Effect of MG132, a proteasome inhibitor, on the expression of growth related Oncogene Protein-α in human umbilical vein endothelial cells
Cytokine, 2003Co-Authors: Takeo Shibata, Tadaatsu Imaizumi, Hidemi Yoshida, Tomoh Matsumiya, Wakako Tamo, Masaharu Hatakeyama, Hirohumi Munakata, Ikuo Fukuda, Kei SatohAbstract:Abstract Growth related Oncogene Protein-α (GRO-α) is a member of C-X-C chemokine and plays an important role in inflammatory responses. Expression of GRO gene family is regulated by a number of factors at both transcriptional and posttranscriptional levels. In the present study, we have addressed the possible regulation of GRO-α expression by ubiquitin–proteasome system. Cultures of human umbilical vein endothelial cells were treated with a proteasome inhibitor, MG132, and the levels of GRO-α mRNA were analyzed by reverse transcription-polymerase chain reaction or northern blotting. Levels of GRO-α Protein in the cell-conditioned medium were determined by enzyme-linked immunosorbent assay. MG132 alone increased the levels of GRO-α mRNA and Protein; however, it did not affect the GRO-α mRNA induced by lipopolysaccharide (LPS) and inhibited the LPS-induced decrease in IκB levels. Other proteasome inhibitors, MG115 and lactacystin, also induced the expression of GRO-α mRNA. MG132 induced the phosphorylation of p38 MAPK, MEK and JNK. Pretreatment of the cells with SB203580, an inhibitor of p38 MAPK, suppressed the MG132-induced GRO-α expression, but pretreatment of the cells with U0126, PD98059 or SP600125, inhibitors of MEK1/2 or JNK, did not influence the effect of MG132. We conclude that MG132 upregulates GRO-α expression in vascular endothelial cells, at least in part, through the activation of p38 MAPK.
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production of growth related Oncogene Protein α in human umbilical vein endothelial cells stimulated with soluble interleukin 6 receptor α role of signal transducers janus kinase 2 and mitogen activated kinase kinase
Life Sciences, 2002Co-Authors: Tomoh Matsumiya, Tadaatsu Imaizumi, Hidemi Yoshida, Takeo Shibata, Hiroyuki Itaya, Hirotaka Sakaki, Hiroto Kimura, Kei SatohAbstract:Abstract Growth-related Oncogene Protein-α (GRO-α) is a member of the C-X-C chemokine family with a wide variety of biological activities. We studied the production of GRO-α by human umbilical vein endothelial cells (HUVEC) in response to the stimulation with soluble form of interleukin-6 receptor α (sIL-6R). sIL-6R stimulated HUVEC to express GRO-α mRNA and secrete GRO-α Protein in concentration-and time-dependent manners. The sIL-6R-induced GRO-α expression was inhibited by the pretreatment of the cells with AG490, a janus kinase 2 (JAK2) inhibitor, or with U0126, a MAP kinase-ERK kinase (MEK) inhibitor. sIL-6R also induced the phosphorylation of both Src homology 2-Protein tyrosine phosphatase-2 (SHP-2), signal transducer and activator of transcription 3 (STAT3) and MEK. AG490 pretreatment inhibited the MEK phosphorylation but did not affect the STAT3 phosphorylation. We conclude that sIL-6R induces GRO-α expression in HUVEC through the activation of JAK2 and MEK.
