The Experts below are selected from a list of 131103 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 Protein
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 Protein
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 Protein
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 Protein
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 Protein
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 Protein
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 Protein
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.
Gerald Krystal - One of the best experts on this subject based on the ideXlab platform.
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the 145 kda Protein induced to associate with shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3 4 5 triphosphate 5 phosphatase
Proceedings of the National Academy of Sciences of the United States of America, 1996Co-Authors: Jacqueline E Damen, Philip W. Majerus, P Rosten, R K Humphries, Ann B Jefferson, Gerald KrystalAbstract:A 145-kDa tyrosine-Phosphorylated Protein that becomes associated with Shc in response to multiple cytokines has been purified from the murine hemopoietic cell line B6SUtA1. Amino acid sequence data were used to clone the cDNA encoding this Protein from a B6SUtA1 library. The predicted amino acid sequence encodes a unique Protein containing an N-terminal src homology 2 domain, two consensus sequences that are targets for phosphotyrosine binding domains, a proline-rich region, and two motifs highly conserved among inositol polyphosphate 5-phosphatases. Cell lysates immunoprecipitated with antiserum to this Protein exhibited both phosphatidylinositol 3,4,5-trisphosphate and inositol 1,3,4,5-tetrakisphosphate polyphosphate 5-phosphatase activity. This novel signal transduction intermediate may serve to modulate both Ras and inositol signaling pathways. Based on its properties, we suggest the 145-kDa Protein be called SHIP for SH2-containing inositol phosphatase.
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erythropoietin stimulates the tyrosine phosphorylation of shc and its association with grb2 and a 145 kd tyrosine Phosphorylated Protein
Blood, 1993Co-Authors: Jacqueline E Damen, Ling Liu, Robert L Cutler, Gerald KrystalAbstract:Although the erythropoietin receptor (EpR) lacks a tyrosine kinase consensus sequence within its proline-rich intracellular domain, addition of its ligand to Ep-responsive cells stimulates the rapid and transient tyrosine phosphorylation of a number of cellular Proteins. The characterization of these phosphorylatable substrates, which include 5 major phosphoProteins with molecular masses of approximately 145, 130, 97, 72, and 56 Kd is an essential step in understanding the signal transduction pathways used by Ep. Recently, we and others have shown that the major 72-Kd tyrosine Phosphorylated Protein is the EpR itself. We now report, using both murine DA-3 and human MO7E cell lines engineered to express high levels of biologically responsive EpRs (and designated DA-ER and MO7-ER, respectively), that the major 56-Kd tyrosine Phosphorylated Protein is the recently identified SH2-containing Protein, p52shc. Interestingly, in Ep-stimulated cells, anti-Shc antibodies coprecipitate the major 145-Kd tyrosine Phosphorylated Protein in both DA-ER and MO7-ER cells. Tyrosine phosphorylation of both Proteins is detectable within 30 seconds of incubation with Ep at 37 degrees C, reaches a maximum between 2 and 5 minutes, and declines by 30 minutes. In addition, tyrosine Phosphorylated Shc appears capable of associating with the activated EpR, but this could only be shown in MO7-ER cells. Lastly, as has been shown previously with the tyrosine kinase containing receptors for epidermal growth factor, platelet derived growth factor, and insulin, activation of the EpR leads to the association of p52shc with the 25-Kd polypeptide, Grb2. Taken together, our data suggest that the previously reported increases in rasGTP observed with Ep result, in part, from the tyrosine phosphorylation of Shc and its association with Grb2 and/or a tyrosine Phosphorylated 145-Kd Protein.