Calcium as a mediator between erythropoietin and protein tyrosine phosphatase 1B
Erythropoietin (Epo) is crucial for promoting the survival, proliferation, and differentiation of mammalian erythroid progenitors. The central role played by tyrosine phosphorylation of erythropoietin receptor (EpoR) in Epo-cell activation has focused attention on protein tyrosine phosphatases (PTPs...
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todo:paper_00039861_v505_n2_p242_Callero2023-10-03T13:57:04Z Calcium as a mediator between erythropoietin and protein tyrosine phosphatase 1B Callero, M.A. Vota, D.M. Chamorro, M.E. Wenker, S.D. Vittori, D.C. Nesse, A.B. Calcium Calpain Erythropoietin PTP1B TRPC calcium calpain erythropoietin granulocyte macrophage colony stimulating factor interleukin 3 intracellular calcium sensing protein protein tyrosine phosphatase 1B transient receptor potential channel 3 transient receptor potential channel 6 tyrosine article calcium signaling cell culture cell differentiation cell proliferation controlled study enzyme localization erythroid cell human human cell leukemia cell priority journal protein expression protein function protein phosphorylation protein protein interaction regulatory mechanism Calcium Calpain Cell Differentiation Cell Line Cell Proliferation Erythropoietin Humans Intracellular Space Isoenzymes Molecular Weight Phosphorylation Protein Binding Protein Tyrosine Phosphatase, Non-Receptor Type 1 RNA, Messenger TRPC Cation Channels Tyrosine Mammalia Erythropoietin (Epo) is crucial for promoting the survival, proliferation, and differentiation of mammalian erythroid progenitors. The central role played by tyrosine phosphorylation of erythropoietin receptor (EpoR) in Epo-cell activation has focused attention on protein tyrosine phosphatases (PTPs) as candidates implicated in the pathogenesis of the resistance to therapy with human recombinant Epo. Prototypic member of the PTP family is PTP1B, which has been implicated in the regulation of EpoR signaling pathways. In previous reports we have shown that PTP1B is reciprocally modulated by Epo in undifferentiated UT-7 cell line. However, no information is available with respect to the modulation of this phosphatase in non-Epo depending cells or at late stages of erythroid differentiation. In order to investigate these issues we induced UT-7 cells to differentiate and studied their PTP1B expression pattern. Simultaneous observations were performed in TF-1 cells which can be cultured either with GM-CSF, IL-3 or Epo. We found that Epo induced PTP1B cleaveage in TF-1 and differentiated UT-7 cells. This pattern of PTP1B modulation may be due to an increased TRPC3/TRPC6 expression ratio which could explain the larger and sustained calcium response to Epo and calpain activation in Epo treated TF-1 and differentiated UT-7 cells. © 2010 Elsevier Inc. All rights reserved. Fil:Callero, M.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Vota, D.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Chamorro, M.E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Wenker, S.D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Vittori, D.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Nesse, A.B. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00039861_v505_n2_p242_Callero |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
Calcium Calpain Erythropoietin PTP1B TRPC calcium calpain erythropoietin granulocyte macrophage colony stimulating factor interleukin 3 intracellular calcium sensing protein protein tyrosine phosphatase 1B transient receptor potential channel 3 transient receptor potential channel 6 tyrosine article calcium signaling cell culture cell differentiation cell proliferation controlled study enzyme localization erythroid cell human human cell leukemia cell priority journal protein expression protein function protein phosphorylation protein protein interaction regulatory mechanism Calcium Calpain Cell Differentiation Cell Line Cell Proliferation Erythropoietin Humans Intracellular Space Isoenzymes Molecular Weight Phosphorylation Protein Binding Protein Tyrosine Phosphatase, Non-Receptor Type 1 RNA, Messenger TRPC Cation Channels Tyrosine Mammalia |
spellingShingle |
Calcium Calpain Erythropoietin PTP1B TRPC calcium calpain erythropoietin granulocyte macrophage colony stimulating factor interleukin 3 intracellular calcium sensing protein protein tyrosine phosphatase 1B transient receptor potential channel 3 transient receptor potential channel 6 tyrosine article calcium signaling cell culture cell differentiation cell proliferation controlled study enzyme localization erythroid cell human human cell leukemia cell priority journal protein expression protein function protein phosphorylation protein protein interaction regulatory mechanism Calcium Calpain Cell Differentiation Cell Line Cell Proliferation Erythropoietin Humans Intracellular Space Isoenzymes Molecular Weight Phosphorylation Protein Binding Protein Tyrosine Phosphatase, Non-Receptor Type 1 RNA, Messenger TRPC Cation Channels Tyrosine Mammalia Callero, M.A. Vota, D.M. Chamorro, M.E. Wenker, S.D. Vittori, D.C. Nesse, A.B. Calcium as a mediator between erythropoietin and protein tyrosine phosphatase 1B |
topic_facet |
Calcium Calpain Erythropoietin PTP1B TRPC calcium calpain erythropoietin granulocyte macrophage colony stimulating factor interleukin 3 intracellular calcium sensing protein protein tyrosine phosphatase 1B transient receptor potential channel 3 transient receptor potential channel 6 tyrosine article calcium signaling cell culture cell differentiation cell proliferation controlled study enzyme localization erythroid cell human human cell leukemia cell priority journal protein expression protein function protein phosphorylation protein protein interaction regulatory mechanism Calcium Calpain Cell Differentiation Cell Line Cell Proliferation Erythropoietin Humans Intracellular Space Isoenzymes Molecular Weight Phosphorylation Protein Binding Protein Tyrosine Phosphatase, Non-Receptor Type 1 RNA, Messenger TRPC Cation Channels Tyrosine Mammalia |
description |
Erythropoietin (Epo) is crucial for promoting the survival, proliferation, and differentiation of mammalian erythroid progenitors. The central role played by tyrosine phosphorylation of erythropoietin receptor (EpoR) in Epo-cell activation has focused attention on protein tyrosine phosphatases (PTPs) as candidates implicated in the pathogenesis of the resistance to therapy with human recombinant Epo. Prototypic member of the PTP family is PTP1B, which has been implicated in the regulation of EpoR signaling pathways. In previous reports we have shown that PTP1B is reciprocally modulated by Epo in undifferentiated UT-7 cell line. However, no information is available with respect to the modulation of this phosphatase in non-Epo depending cells or at late stages of erythroid differentiation. In order to investigate these issues we induced UT-7 cells to differentiate and studied their PTP1B expression pattern. Simultaneous observations were performed in TF-1 cells which can be cultured either with GM-CSF, IL-3 or Epo. We found that Epo induced PTP1B cleaveage in TF-1 and differentiated UT-7 cells. This pattern of PTP1B modulation may be due to an increased TRPC3/TRPC6 expression ratio which could explain the larger and sustained calcium response to Epo and calpain activation in Epo treated TF-1 and differentiated UT-7 cells. © 2010 Elsevier Inc. All rights reserved. |
format |
JOUR |
author |
Callero, M.A. Vota, D.M. Chamorro, M.E. Wenker, S.D. Vittori, D.C. Nesse, A.B. |
author_facet |
Callero, M.A. Vota, D.M. Chamorro, M.E. Wenker, S.D. Vittori, D.C. Nesse, A.B. |
author_sort |
Callero, M.A. |
title |
Calcium as a mediator between erythropoietin and protein tyrosine phosphatase 1B |
title_short |
Calcium as a mediator between erythropoietin and protein tyrosine phosphatase 1B |
title_full |
Calcium as a mediator between erythropoietin and protein tyrosine phosphatase 1B |
title_fullStr |
Calcium as a mediator between erythropoietin and protein tyrosine phosphatase 1B |
title_full_unstemmed |
Calcium as a mediator between erythropoietin and protein tyrosine phosphatase 1B |
title_sort |
calcium as a mediator between erythropoietin and protein tyrosine phosphatase 1b |
url |
http://hdl.handle.net/20.500.12110/paper_00039861_v505_n2_p242_Callero |
work_keys_str_mv |
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1807319005214539776 |