The Experts below are selected from a list of 51051 Experts worldwide ranked by ideXlab platform
J T Parsons - One of the best experts on this subject based on the ideXlab platform.
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cd40 signaling pathway anti cd40 monoclonal antibody induces rapid dephosphorylation and phosphorylation of tyrosine phosphorylated Proteins including Protein tyrosine Kinase lyn fyn and syk and the appearance of a 28 kd tyrosine phosphorylated prote
Journal of Experimental Medicine, 1994Co-Authors: M Faris, Felicia Gaskin, J T Parsons, Shu Man FuAbstract:CD40 plays an important role in B cell activation, proliferation, and Ig class switching. The signal transduction pathway mediated by CD40 was studied using monoclonal antibody (mAb) 626.1 to CD40. Burkitt's lymphoma and Epstein-Barr virus-transformed B cell lines and tonsilar B lymphocytes were treated with the anti-CD40 mAb for various lengths of time. The early events triggered by CD40 were examined by monitoring the changes in tyrosine phosphorylation of cellular Proteins with anti-phosphotyrosine mAb. Dephosphorylation of specific Proteins ranging between 50-110 kD and the appearance of a 28-kD tyrosine phosphorylated Protein were seen within 30 s in human B cell lines. The dephosphorylation was reversed and the 28-kD Protein was dephosphorylated in cells stimulated for 1 min. In resting B cells, the appearance of the 28-kD phosphoProtein was observed in 30 s after the addition of the anti-CD40 mAb. The tyrosine phosphorylation of this Protein persisted. The patterns of Protein tyrosine phosphorylation differed from those induced by an anti-immunoglobulin M mAb. The changes in the state of tyrosine phosphorylation induced by the anti-CD40 mAb were obviated by mAb to CD45, a Protein tyrosine phosphatase (PTP) or by the addition of sodium orthovanadate, a broad PTP inhibitor. They were also blocked by Protein tyrosine Kinase (PTK) inhibitors, herbimycin A and genistein, and PKC and Protein serine/threonine Kinase inhibitors, H7 and HA1004. In addition, the alteration in the tyrosine phosphorylation of PTKs Lyn, Fyn, and Syk was directly demonstrated. Engagement of CD40 for 30 s induced a transient decrease in tyrosine phosphorylation of these PTKs. These results indicate that the early events in CD40 signaling involve the complex interaction between PTP and Protein Kinases.
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cd40 signaling pathway anti cd40 monoclonal antibody induces rapid dephosphorylation and phosphorylation of tyrosine phosphorylated Proteins including Protein tyrosine Kinase lyn fyn and syk and the appearance of a 28 kd tyrosine phosphorylated prote
Journal of Experimental Medicine, 1994Co-Authors: M Faris, Felicia Gaskin, J T ParsonsAbstract:CD40 plays an important role in B cell activation, proliferation, and Ig class switching. The signal transduction pathway mediated by CD40 was studied using monoclonal antibody (mAb) 626.1 to CD40. Burkitt's lymphoma and Epstein-Barr virus-transformed B cell lines and tonsilar B lymphocytes were treated with the anti-CD40 mAb for various lengths of time. The early events triggered by CD40 were examined by monitoring the changes in tyrosine phosphorylation of cellular Proteins with anti-phosphotyrosine mAb. Dephosphorylation of specific Proteins ranging between 50-110 kD and the appearance of a 28-kD tyrosine phosphorylated Protein were seen within 30 s in human B cell lines. The dephosphorylation was reversed and the 28-kD Protein was dephosphorylated in cells stimulated for 1 min. In resting B cells, the appearance of the 28-kD phosphoProtein was observed in 30 s after the addition of the anti-CD40 mAb. The tyrosine phosphorylation of this Protein persisted. The patterns of Protein tyrosine phosphorylation differed from those induced by an anti-immunoglobulin M mAb. The changes in the state of tyrosine phosphorylation induced by the anti-CD40 mAb were obviated by mAb to CD45, a Protein tyrosine phosphatase (PTP) or by the addition of sodium orthovanadate, a broad PTP inhibitor. They were also blocked by Protein tyrosine Kinase (PTK) inhibitors, herbimycin A and genistein, and PKC and Protein serine/threonine Kinase inhibitors, H7 and HA1004. In addition, the alteration in the tyrosine phosphorylation of PTKs Lyn, Fyn, and Syk was directly demonstrated. Engagement of CD40 for 30 s induced a transient decrease in tyrosine phosphorylation of these PTKs. These results indicate that the early events in CD40 signaling involve the complex interaction between PTP and Protein Kinases.
M Faris - One of the best experts on this subject based on the ideXlab platform.
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cd40 signaling pathway anti cd40 monoclonal antibody induces rapid dephosphorylation and phosphorylation of tyrosine phosphorylated Proteins including Protein tyrosine Kinase lyn fyn and syk and the appearance of a 28 kd tyrosine phosphorylated prote
Journal of Experimental Medicine, 1994Co-Authors: M Faris, Felicia Gaskin, J T Parsons, Shu Man FuAbstract:CD40 plays an important role in B cell activation, proliferation, and Ig class switching. The signal transduction pathway mediated by CD40 was studied using monoclonal antibody (mAb) 626.1 to CD40. Burkitt's lymphoma and Epstein-Barr virus-transformed B cell lines and tonsilar B lymphocytes were treated with the anti-CD40 mAb for various lengths of time. The early events triggered by CD40 were examined by monitoring the changes in tyrosine phosphorylation of cellular Proteins with anti-phosphotyrosine mAb. Dephosphorylation of specific Proteins ranging between 50-110 kD and the appearance of a 28-kD tyrosine phosphorylated Protein were seen within 30 s in human B cell lines. The dephosphorylation was reversed and the 28-kD Protein was dephosphorylated in cells stimulated for 1 min. In resting B cells, the appearance of the 28-kD phosphoProtein was observed in 30 s after the addition of the anti-CD40 mAb. The tyrosine phosphorylation of this Protein persisted. The patterns of Protein tyrosine phosphorylation differed from those induced by an anti-immunoglobulin M mAb. The changes in the state of tyrosine phosphorylation induced by the anti-CD40 mAb were obviated by mAb to CD45, a Protein tyrosine phosphatase (PTP) or by the addition of sodium orthovanadate, a broad PTP inhibitor. They were also blocked by Protein tyrosine Kinase (PTK) inhibitors, herbimycin A and genistein, and PKC and Protein serine/threonine Kinase inhibitors, H7 and HA1004. In addition, the alteration in the tyrosine phosphorylation of PTKs Lyn, Fyn, and Syk was directly demonstrated. Engagement of CD40 for 30 s induced a transient decrease in tyrosine phosphorylation of these PTKs. These results indicate that the early events in CD40 signaling involve the complex interaction between PTP and Protein Kinases.
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cd40 signaling pathway anti cd40 monoclonal antibody induces rapid dephosphorylation and phosphorylation of tyrosine phosphorylated Proteins including Protein tyrosine Kinase lyn fyn and syk and the appearance of a 28 kd tyrosine phosphorylated prote
Journal of Experimental Medicine, 1994Co-Authors: M Faris, Felicia Gaskin, J T ParsonsAbstract:CD40 plays an important role in B cell activation, proliferation, and Ig class switching. The signal transduction pathway mediated by CD40 was studied using monoclonal antibody (mAb) 626.1 to CD40. Burkitt's lymphoma and Epstein-Barr virus-transformed B cell lines and tonsilar B lymphocytes were treated with the anti-CD40 mAb for various lengths of time. The early events triggered by CD40 were examined by monitoring the changes in tyrosine phosphorylation of cellular Proteins with anti-phosphotyrosine mAb. Dephosphorylation of specific Proteins ranging between 50-110 kD and the appearance of a 28-kD tyrosine phosphorylated Protein were seen within 30 s in human B cell lines. The dephosphorylation was reversed and the 28-kD Protein was dephosphorylated in cells stimulated for 1 min. In resting B cells, the appearance of the 28-kD phosphoProtein was observed in 30 s after the addition of the anti-CD40 mAb. The tyrosine phosphorylation of this Protein persisted. The patterns of Protein tyrosine phosphorylation differed from those induced by an anti-immunoglobulin M mAb. The changes in the state of tyrosine phosphorylation induced by the anti-CD40 mAb were obviated by mAb to CD45, a Protein tyrosine phosphatase (PTP) or by the addition of sodium orthovanadate, a broad PTP inhibitor. They were also blocked by Protein tyrosine Kinase (PTK) inhibitors, herbimycin A and genistein, and PKC and Protein serine/threonine Kinase inhibitors, H7 and HA1004. In addition, the alteration in the tyrosine phosphorylation of PTKs Lyn, Fyn, and Syk was directly demonstrated. Engagement of CD40 for 30 s induced a transient decrease in tyrosine phosphorylation of these PTKs. These results indicate that the early events in CD40 signaling involve the complex interaction between PTP and Protein Kinases.
Shu Man Fu - One of the best experts on this subject based on the ideXlab platform.
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cd40 signaling pathway anti cd40 monoclonal antibody induces rapid dephosphorylation and phosphorylation of tyrosine phosphorylated Proteins including Protein tyrosine Kinase lyn fyn and syk and the appearance of a 28 kd tyrosine phosphorylated prote
Journal of Experimental Medicine, 1994Co-Authors: M Faris, Felicia Gaskin, J T Parsons, Shu Man FuAbstract:CD40 plays an important role in B cell activation, proliferation, and Ig class switching. The signal transduction pathway mediated by CD40 was studied using monoclonal antibody (mAb) 626.1 to CD40. Burkitt's lymphoma and Epstein-Barr virus-transformed B cell lines and tonsilar B lymphocytes were treated with the anti-CD40 mAb for various lengths of time. The early events triggered by CD40 were examined by monitoring the changes in tyrosine phosphorylation of cellular Proteins with anti-phosphotyrosine mAb. Dephosphorylation of specific Proteins ranging between 50-110 kD and the appearance of a 28-kD tyrosine phosphorylated Protein were seen within 30 s in human B cell lines. The dephosphorylation was reversed and the 28-kD Protein was dephosphorylated in cells stimulated for 1 min. In resting B cells, the appearance of the 28-kD phosphoProtein was observed in 30 s after the addition of the anti-CD40 mAb. The tyrosine phosphorylation of this Protein persisted. The patterns of Protein tyrosine phosphorylation differed from those induced by an anti-immunoglobulin M mAb. The changes in the state of tyrosine phosphorylation induced by the anti-CD40 mAb were obviated by mAb to CD45, a Protein tyrosine phosphatase (PTP) or by the addition of sodium orthovanadate, a broad PTP inhibitor. They were also blocked by Protein tyrosine Kinase (PTK) inhibitors, herbimycin A and genistein, and PKC and Protein serine/threonine Kinase inhibitors, H7 and HA1004. In addition, the alteration in the tyrosine phosphorylation of PTKs Lyn, Fyn, and Syk was directly demonstrated. Engagement of CD40 for 30 s induced a transient decrease in tyrosine phosphorylation of these PTKs. These results indicate that the early events in CD40 signaling involve the complex interaction between PTP and Protein Kinases.
Felicia Gaskin - One of the best experts on this subject based on the ideXlab platform.
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cd40 signaling pathway anti cd40 monoclonal antibody induces rapid dephosphorylation and phosphorylation of tyrosine phosphorylated Proteins including Protein tyrosine Kinase lyn fyn and syk and the appearance of a 28 kd tyrosine phosphorylated prote
Journal of Experimental Medicine, 1994Co-Authors: M Faris, Felicia Gaskin, J T Parsons, Shu Man FuAbstract:CD40 plays an important role in B cell activation, proliferation, and Ig class switching. The signal transduction pathway mediated by CD40 was studied using monoclonal antibody (mAb) 626.1 to CD40. Burkitt's lymphoma and Epstein-Barr virus-transformed B cell lines and tonsilar B lymphocytes were treated with the anti-CD40 mAb for various lengths of time. The early events triggered by CD40 were examined by monitoring the changes in tyrosine phosphorylation of cellular Proteins with anti-phosphotyrosine mAb. Dephosphorylation of specific Proteins ranging between 50-110 kD and the appearance of a 28-kD tyrosine phosphorylated Protein were seen within 30 s in human B cell lines. The dephosphorylation was reversed and the 28-kD Protein was dephosphorylated in cells stimulated for 1 min. In resting B cells, the appearance of the 28-kD phosphoProtein was observed in 30 s after the addition of the anti-CD40 mAb. The tyrosine phosphorylation of this Protein persisted. The patterns of Protein tyrosine phosphorylation differed from those induced by an anti-immunoglobulin M mAb. The changes in the state of tyrosine phosphorylation induced by the anti-CD40 mAb were obviated by mAb to CD45, a Protein tyrosine phosphatase (PTP) or by the addition of sodium orthovanadate, a broad PTP inhibitor. They were also blocked by Protein tyrosine Kinase (PTK) inhibitors, herbimycin A and genistein, and PKC and Protein serine/threonine Kinase inhibitors, H7 and HA1004. In addition, the alteration in the tyrosine phosphorylation of PTKs Lyn, Fyn, and Syk was directly demonstrated. Engagement of CD40 for 30 s induced a transient decrease in tyrosine phosphorylation of these PTKs. These results indicate that the early events in CD40 signaling involve the complex interaction between PTP and Protein Kinases.
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cd40 signaling pathway anti cd40 monoclonal antibody induces rapid dephosphorylation and phosphorylation of tyrosine phosphorylated Proteins including Protein tyrosine Kinase lyn fyn and syk and the appearance of a 28 kd tyrosine phosphorylated prote
Journal of Experimental Medicine, 1994Co-Authors: M Faris, Felicia Gaskin, J T ParsonsAbstract:CD40 plays an important role in B cell activation, proliferation, and Ig class switching. The signal transduction pathway mediated by CD40 was studied using monoclonal antibody (mAb) 626.1 to CD40. Burkitt's lymphoma and Epstein-Barr virus-transformed B cell lines and tonsilar B lymphocytes were treated with the anti-CD40 mAb for various lengths of time. The early events triggered by CD40 were examined by monitoring the changes in tyrosine phosphorylation of cellular Proteins with anti-phosphotyrosine mAb. Dephosphorylation of specific Proteins ranging between 50-110 kD and the appearance of a 28-kD tyrosine phosphorylated Protein were seen within 30 s in human B cell lines. The dephosphorylation was reversed and the 28-kD Protein was dephosphorylated in cells stimulated for 1 min. In resting B cells, the appearance of the 28-kD phosphoProtein was observed in 30 s after the addition of the anti-CD40 mAb. The tyrosine phosphorylation of this Protein persisted. The patterns of Protein tyrosine phosphorylation differed from those induced by an anti-immunoglobulin M mAb. The changes in the state of tyrosine phosphorylation induced by the anti-CD40 mAb were obviated by mAb to CD45, a Protein tyrosine phosphatase (PTP) or by the addition of sodium orthovanadate, a broad PTP inhibitor. They were also blocked by Protein tyrosine Kinase (PTK) inhibitors, herbimycin A and genistein, and PKC and Protein serine/threonine Kinase inhibitors, H7 and HA1004. In addition, the alteration in the tyrosine phosphorylation of PTKs Lyn, Fyn, and Syk was directly demonstrated. Engagement of CD40 for 30 s induced a transient decrease in tyrosine phosphorylation of these PTKs. These results indicate that the early events in CD40 signaling involve the complex interaction between PTP and Protein Kinases.
Hyuna Seong - One of the best experts on this subject based on the ideXlab platform.
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coordinate activation of redox dependent ask1 tgf β signaling by a multiProtein complex mpk38 ask1 smads zpr9 and trx improves glucose and lipid metabolism in mice
Antioxidants & Redox Signaling, 2016Co-Authors: Hyuna Seong, Ravi ManoharanAbstract:Abstract Aims: To explore the molecular connections between redox-dependent apoptosis signal-regulating Kinase 1 (ASK1) and transforming growth factor-β (TGF-β) signaling pathways and to examine the physiological processes in which coordinated regulation of these two signaling pathways plays a critical role. Results: We provide evidence that the ASK1 and TGF-β signaling pathways are interconnected by a multiProtein complex harboring murine Protein serine–threonine Kinase 38 (MPK38), ASK1, Sma- and Mad-related Proteins (SMADs), zinc-finger-like Protein 9 (ZPR9), and thioredoxin (TRX) and demonstrate that the activation of either ASK1 or TGF-β activity is sufficient to activate both the redox-dependent ASK1 and TGF-β signaling pathways. Physiologically, the restoration of the downregulated activation levels of ASK1 and TGF-β signaling in genetically and diet-induced obese mice by adenoviral delivery of SMAD3 or ZPR9 results in the amelioration of adiposity, hyperglycemia, hyperlipidemia, and impaired ketoge...
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Murine Protein Serine-Threonine Kinase 38 activates p53 function through Ser15 phosphorylation.
Journal of Biological Chemistry, 2012Co-Authors: Hyuna Seong, Hyunjung HaAbstract:Murine Protein Serine-Threonine Kinase 38 (MPK38) is a member of the AMP-activated Protein Kinase-related serine/threonine Kinase family. In this study, we show that MPK38 physically associates with p53 via the carboxyl-terminal domain of MPK38 and the central DNA-binding domain of p53. This interaction is increased by 5-fluorouracil or doxorubicin treatment and is responsible for Ser15 phosphorylation of p53. Ectopic expression of wild-type Mpk38, but not Kinase-dead Mpk38, stimulates p53-mediated transcription in a dose-dependent manner and up-regulates p53 targets, including p53, p21, MDM2, and BAX. Consistently, knockdown of MPK38 shows an opposite trend, inhibiting p53-mediated transcription. MPK38 functionally enhances p53-mediated apoptosis and cell cycle arrest in a Kinase-dependent manner by stimulating p53 nuclear translocation. We also demonstrate that MPK38-mediated p53 activation is induced by removing MDM2, a negative regulator of p53, from the p53-MDM2 complex as well as by stabilization of interaction between p53 and its positive regulators, including NM23-H1, serine/threonine Kinase receptor-associated Protein, and 14-3-3. This leads to the enhancement of p53 stability. Together, these results suggest that MPK38 may act as a novel regulator for promoting p53 activity through direct phosphorylation of p53 at Ser15.
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murine Protein serine threonine Kinase 38 stimulates tgf β signaling in a Kinase dependent manner via direct phosphorylation of smad Proteins
Journal of Biological Chemistry, 2010Co-Authors: Hyuna Seong, Haiyoung JungAbstract:The present study demonstrated that murine Protein serine/threonine Kinase 38 (MPK38) coimmunoprecipitates with Smad Proteins (Smad2, -3, -4, and -7) and that this association is mediated by the catalytic Kinase domain of MPK38. The association between MPK38 and Smad2, -3, and -4 was significantly increased by TGF-β or ASK1 signals, whereas these signals decreased association of MPK38 with Smad7. MPK38 stimulated TGF-β-induced transcription required for TGF-β-mediated biological functions, such as apoptosis and cell growth arrest, in a Kinase-dependent manner. Knockdown of endogenous MPK38 showed an opposite effect, inhibiting TGF-β signaling. MPK38-mediated phosphorylation of Smad Proteins (Ser245 of Smad2, Ser204 of Smad3, Ser343 of Smad4, and Thr96 of Smad7) was also found to be crucial to the positive regulation of TGF-β signaling induced by MPK38. In addition, MPK38 enhanced nuclear translocation of Smad3, as well as redistribution of Smad7 from the nucleus to the cytoplasm, in response to TGF-β. Together, these results indicate that MPK38 functions as a stimulator of TGF-β signaling through direct interaction with and phosphorylation of Smad Proteins.
