Differential Regulation of Endoplasmic Reticulum Stress by Protein Tyrosine Phosphatase 1B and T Cell Protein Tyrosine Phosphatase

Protein-tyrosine phosphatase 1B (PTP1B) and T cell protein-tyrosine phosphatase (TCPTP) are closely related intracellular phosphatases implicated in the control of glucose homeostasis. PTP1B and TCPTP can function coordinately to regulate protein tyrosine kinase signaling, and PTP1B has been implica...

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Veröffentlicht in:The Journal of biological chemistry 2011-03, Vol.286 (11), p.9225-9235
Hauptverfasser: Bettaieb, Ahmed, Liu, Siming, Xi, Yannan, Nagata, Naoto, Matsuo, Kosuke, Matsuo, Izumi, Chahed, Samah, Bakke, Jesse, Keilhack, Heike, Tiganis, Tony, Haj, Fawaz G.
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container_end_page 9235
container_issue 11
container_start_page 9225
container_title The Journal of biological chemistry
container_volume 286
creator Bettaieb, Ahmed
Liu, Siming
Xi, Yannan
Nagata, Naoto
Matsuo, Kosuke
Matsuo, Izumi
Chahed, Samah
Bakke, Jesse
Keilhack, Heike
Tiganis, Tony
Haj, Fawaz G.
description Protein-tyrosine phosphatase 1B (PTP1B) and T cell protein-tyrosine phosphatase (TCPTP) are closely related intracellular phosphatases implicated in the control of glucose homeostasis. PTP1B and TCPTP can function coordinately to regulate protein tyrosine kinase signaling, and PTP1B has been implicated previously in the regulation of endoplasmic reticulum (ER) stress. In this study, we assessed the roles of PTP1B and TCPTP in regulating ER stress in the endocrine pancreas. PTP1B and TCPTP expression was determined in pancreases from chow and high fat fed mice and the impact of PTP1B and TCPTP over- or underexpression on palmitate- or tunicamycin-induced ER stress signaling assessed in MIN6 insulinoma β cells. PTP1B expression was increased, and TCPTP expression decreased in pancreases of mice fed a high fat diet, as well as in MIN6 cells treated with palmitate. PTP1B overexpression or TCPTP knockdown in MIN6 cells mitigated palmitate- or tunicamycin-induced PERK/eIF2α ER stress signaling, whereas PTP1B deficiency enhanced ER stress. Moreover, PTP1B deficiency increased ER stress-induced cell death, whereas TCPTP deficiency protected MIN6 cells from ER stress-induced death. ER stress coincided with the inhibition of Src family kinases (SFKs), which was exacerbated by PTP1B overexpression and largely prevented by TCPTP knockdown. Pharmacological inhibition of SFKs ameliorated the protective effect of TCPTP deficiency on ER stress-induced cell death. These results demonstrate that PTP1B and TCPTP play nonredundant roles in modulating ER stress in pancreatic β cells and suggest that changes in PTP1B and TCPTP expression may serve as an adaptive response for the mitigation of chronic ER stress.
doi_str_mv 10.1074/jbc.M110.186148
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subjects Animals
Apoptosis
Cell Death
Cell Line, Tumor
Diabetes
Endoplasmic Reticulum (ER)
Endoplasmic Reticulum - enzymology
Endoplasmic Reticulum Stress
Enzyme Inhibitors - pharmacology
Gene Expression Regulation, Enzymologic - drug effects
Gene Expression Regulation, Enzymologic - physiology
Gene Knockdown Techniques
HEK293 Cells
Humans
Insulin-Secreting Cells - enzymology
Mice
Palmitic Acid - pharmacology
Pancreas
Phosphotyrosine
Protein Tyrosine Phosphatase, Non-Receptor Type 1 - genetics
Protein Tyrosine Phosphatase, Non-Receptor Type 1 - metabolism
Protein Tyrosine Phosphatase, Non-Receptor Type 2 - genetics
Protein Tyrosine Phosphatase, Non-Receptor Type 2 - metabolism
Signal Transduction
Signal Transduction - drug effects
Signal Transduction - physiology
Tyrosine Protein Phosphatase (Tyrosine Phosphatase)
Unfolded Protein Response - drug effects
Unfolded Protein Response - physiology
title Differential Regulation of Endoplasmic Reticulum Stress by Protein Tyrosine Phosphatase 1B and T Cell Protein Tyrosine Phosphatase
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