The Experts below are selected from a list of 207 Experts worldwide ranked by ideXlab platform
C. J. Bailey - One of the best experts on this subject based on the ideXlab platform.
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Recombinant epidermolytic (exfoliative) toxin A of Staphylococcus aureus is not a superantigen
Medical Microbiology and Immunology, 1992Co-Authors: B. Fleischer, C. J. BaileyAbstract:The epidermolytic (exfoliative) toxins produced by Staphylococcus aureus cause epidermolysis and skin blistering. In addition, they have been implicated to belong to the group of T lymphocyte stimulating molecules known as “superantigens”. Here we show that recombinant epidermolytic toxin A produced in S. aureus is not mitogenic for human and murine T lymphocytes. We discuss the possibility that minute contaminations of highly mitogenic exoproteins may cause the Mitogenicity in several proteins that are reported to be superantigens.
Michael J. Cross - One of the best experts on this subject based on the ideXlab platform.
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the shb adaptor protein binds to tyrosine 766 in the fgfr 1 and regulates the ras mek mapk pathway via frs2 phosphorylation in endothelial cells
Molecular Biology of the Cell, 2002Co-Authors: Michael J. Cross, Peetra U. Magnusson, Daniel Nyqvist, Kristina Holmqvist, Michael Welsh, Lena ClaessonwelshAbstract:Stimulation of fibroblast growth factor receptor-1 (FGFR-1) is known to result in phosphorylation of tyrosine 766 and the recruitment and subsequent activation of phospholipase C-γ (PLC-γ). To assess the role of tyrosine 766 in endothelial cell function, we generated endothelial cells expressing a chimeric receptor, composed of the extracellular domain of the PDGF receptor-α and the intracellular domain of FGFR-1. Mutation of tyrosine 766 to phenylalanine prevented PLC-γ activation and resulted in a reduced phosphorylation of FRS2 and reduced activation of the Ras/MEK/MAPK pathway relative to the wild-type chimeric receptor. However, FGFR-1–mediated MAPK activation was not dependent on PKC activation or intracellular calcium, both downstream mediators of PLC-γ activation. We report that the adaptor protein Shb is also able to bind tyrosine 766 in the FGFR-1, via its SH2 domain, resulting in its subsequent phosphorylation. Overexpression of an SH2 domain mutant Shb caused a dramatic reduction in FGFR-1–mediated FRS2 phosphorylation with concomitant perturbment of the Ras/MEK/MAPK pathway. Expression of the chimeric receptor mutant and the Shb SH2 domain mutant resulted in a similar reduction in FGFR-1–mediated Mitogenicity. We conclude, that Shb binds to tyrosine 766 in the FGFR-1 and regulates FGF-mediated Mitogenicity via FRS2 phosphorylation and the subsequent activation of the Ras/MEK/MAPK pathway.
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The Shb Adaptor Protein Binds to Tyrosine 766 in the FGFR-1 and Regulates the Ras/MEK/MAPK Pathway via FRS2 Phosphorylation in Endothelial Cells
Molecular biology of the cell, 2002Co-Authors: Michael J. Cross, Peetra U. Magnusson, Daniel Nyqvist, Kristina Holmqvist, Michael Welsh, Lena Claesson-welshAbstract:Stimulation of fibroblast growth factor receptor-1 (FGFR-1) is known to result in phosphorylation of tyrosine 766 and the recruitment and subsequent activation of phospholipase C-γ (PLC-γ). To assess the role of tyrosine 766 in endothelial cell function, we generated endothelial cells expressing a chimeric receptor, composed of the extracellular domain of the PDGF receptor-α and the intracellular domain of FGFR-1. Mutation of tyrosine 766 to phenylalanine prevented PLC-γ activation and resulted in a reduced phosphorylation of FRS2 and reduced activation of the Ras/MEK/MAPK pathway relative to the wild-type chimeric receptor. However, FGFR-1–mediated MAPK activation was not dependent on PKC activation or intracellular calcium, both downstream mediators of PLC-γ activation. We report that the adaptor protein Shb is also able to bind tyrosine 766 in the FGFR-1, via its SH2 domain, resulting in its subsequent phosphorylation. Overexpression of an SH2 domain mutant Shb caused a dramatic reduction in FGFR-1–mediated FRS2 phosphorylation with concomitant perturbment of the Ras/MEK/MAPK pathway. Expression of the chimeric receptor mutant and the Shb SH2 domain mutant resulted in a similar reduction in FGFR-1–mediated Mitogenicity. We conclude, that Shb binds to tyrosine 766 in the FGFR-1 and regulates FGF-mediated Mitogenicity via FRS2 phosphorylation and the subsequent activation of the Ras/MEK/MAPK pathway.
B. Fleischer - One of the best experts on this subject based on the ideXlab platform.
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Recombinant epidermolytic (exfoliative) toxin A of Staphylococcus aureus is not a superantigen
Medical Microbiology and Immunology, 1992Co-Authors: B. Fleischer, C. J. BaileyAbstract:The epidermolytic (exfoliative) toxins produced by Staphylococcus aureus cause epidermolysis and skin blistering. In addition, they have been implicated to belong to the group of T lymphocyte stimulating molecules known as “superantigens”. Here we show that recombinant epidermolytic toxin A produced in S. aureus is not mitogenic for human and murine T lymphocytes. We discuss the possibility that minute contaminations of highly mitogenic exoproteins may cause the Mitogenicity in several proteins that are reported to be superantigens.
Lena Claesson-welsh - One of the best experts on this subject based on the ideXlab platform.
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The Shb Adaptor Protein Binds to Tyrosine 766 in the FGFR-1 and Regulates the Ras/MEK/MAPK Pathway via FRS2 Phosphorylation in Endothelial Cells
Molecular biology of the cell, 2002Co-Authors: Michael J. Cross, Peetra U. Magnusson, Daniel Nyqvist, Kristina Holmqvist, Michael Welsh, Lena Claesson-welshAbstract:Stimulation of fibroblast growth factor receptor-1 (FGFR-1) is known to result in phosphorylation of tyrosine 766 and the recruitment and subsequent activation of phospholipase C-γ (PLC-γ). To assess the role of tyrosine 766 in endothelial cell function, we generated endothelial cells expressing a chimeric receptor, composed of the extracellular domain of the PDGF receptor-α and the intracellular domain of FGFR-1. Mutation of tyrosine 766 to phenylalanine prevented PLC-γ activation and resulted in a reduced phosphorylation of FRS2 and reduced activation of the Ras/MEK/MAPK pathway relative to the wild-type chimeric receptor. However, FGFR-1–mediated MAPK activation was not dependent on PKC activation or intracellular calcium, both downstream mediators of PLC-γ activation. We report that the adaptor protein Shb is also able to bind tyrosine 766 in the FGFR-1, via its SH2 domain, resulting in its subsequent phosphorylation. Overexpression of an SH2 domain mutant Shb caused a dramatic reduction in FGFR-1–mediated FRS2 phosphorylation with concomitant perturbment of the Ras/MEK/MAPK pathway. Expression of the chimeric receptor mutant and the Shb SH2 domain mutant resulted in a similar reduction in FGFR-1–mediated Mitogenicity. We conclude, that Shb binds to tyrosine 766 in the FGFR-1 and regulates FGF-mediated Mitogenicity via FRS2 phosphorylation and the subsequent activation of the Ras/MEK/MAPK pathway.
Lena Claessonwelsh - One of the best experts on this subject based on the ideXlab platform.
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the shb adaptor protein binds to tyrosine 766 in the fgfr 1 and regulates the ras mek mapk pathway via frs2 phosphorylation in endothelial cells
Molecular Biology of the Cell, 2002Co-Authors: Michael J. Cross, Peetra U. Magnusson, Daniel Nyqvist, Kristina Holmqvist, Michael Welsh, Lena ClaessonwelshAbstract:Stimulation of fibroblast growth factor receptor-1 (FGFR-1) is known to result in phosphorylation of tyrosine 766 and the recruitment and subsequent activation of phospholipase C-γ (PLC-γ). To assess the role of tyrosine 766 in endothelial cell function, we generated endothelial cells expressing a chimeric receptor, composed of the extracellular domain of the PDGF receptor-α and the intracellular domain of FGFR-1. Mutation of tyrosine 766 to phenylalanine prevented PLC-γ activation and resulted in a reduced phosphorylation of FRS2 and reduced activation of the Ras/MEK/MAPK pathway relative to the wild-type chimeric receptor. However, FGFR-1–mediated MAPK activation was not dependent on PKC activation or intracellular calcium, both downstream mediators of PLC-γ activation. We report that the adaptor protein Shb is also able to bind tyrosine 766 in the FGFR-1, via its SH2 domain, resulting in its subsequent phosphorylation. Overexpression of an SH2 domain mutant Shb caused a dramatic reduction in FGFR-1–mediated FRS2 phosphorylation with concomitant perturbment of the Ras/MEK/MAPK pathway. Expression of the chimeric receptor mutant and the Shb SH2 domain mutant resulted in a similar reduction in FGFR-1–mediated Mitogenicity. We conclude, that Shb binds to tyrosine 766 in the FGFR-1 and regulates FGF-mediated Mitogenicity via FRS2 phosphorylation and the subsequent activation of the Ras/MEK/MAPK pathway.