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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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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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.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M110.186148</identifier><identifier>PMID: 21216966</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>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</subject><ispartof>The Journal of biological chemistry, 2011-03, Vol.286 (11), p.9225-9235</ispartof><rights>2011 © 2011 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><rights>2011 by The American Society for Biochemistry and Molecular Biology, Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c466t-8aa91a47decc520f92503e6d24feaf14982b50081d2da094e1e9638de48c5dfc3</citedby><cites>FETCH-LOGICAL-c466t-8aa91a47decc520f92503e6d24feaf14982b50081d2da094e1e9638de48c5dfc3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3059022/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3059022/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21216966$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bettaieb, Ahmed</creatorcontrib><creatorcontrib>Liu, Siming</creatorcontrib><creatorcontrib>Xi, Yannan</creatorcontrib><creatorcontrib>Nagata, Naoto</creatorcontrib><creatorcontrib>Matsuo, Kosuke</creatorcontrib><creatorcontrib>Matsuo, Izumi</creatorcontrib><creatorcontrib>Chahed, Samah</creatorcontrib><creatorcontrib>Bakke, Jesse</creatorcontrib><creatorcontrib>Keilhack, Heike</creatorcontrib><creatorcontrib>Tiganis, Tony</creatorcontrib><creatorcontrib>Haj, Fawaz G.</creatorcontrib><title>Differential Regulation of Endoplasmic Reticulum Stress by Protein Tyrosine Phosphatase 1B and T Cell Protein Tyrosine Phosphatase</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><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.</description><subject>Animals</subject><subject>Apoptosis</subject><subject>Cell Death</subject><subject>Cell Line, Tumor</subject><subject>Diabetes</subject><subject>Endoplasmic Reticulum (ER)</subject><subject>Endoplasmic Reticulum - enzymology</subject><subject>Endoplasmic Reticulum Stress</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Gene Expression Regulation, Enzymologic - drug effects</subject><subject>Gene Expression Regulation, Enzymologic - physiology</subject><subject>Gene Knockdown Techniques</subject><subject>HEK293 Cells</subject><subject>Humans</subject><subject>Insulin-Secreting Cells - enzymology</subject><subject>Mice</subject><subject>Palmitic Acid - pharmacology</subject><subject>Pancreas</subject><subject>Phosphotyrosine</subject><subject>Protein Tyrosine Phosphatase, Non-Receptor Type 1 - genetics</subject><subject>Protein Tyrosine Phosphatase, Non-Receptor Type 1 - metabolism</subject><subject>Protein Tyrosine Phosphatase, Non-Receptor Type 2 - genetics</subject><subject>Protein Tyrosine Phosphatase, Non-Receptor Type 2 - metabolism</subject><subject>Signal Transduction</subject><subject>Signal Transduction - drug effects</subject><subject>Signal Transduction - physiology</subject><subject>Tyrosine Protein Phosphatase (Tyrosine Phosphatase)</subject><subject>Unfolded Protein Response - drug effects</subject><subject>Unfolded Protein Response - physiology</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kUFPGzEQhS1EVVLomVvxH1jweL2LfalEU9oigUAQpN4sxx4nRpt1ZG-Qcu0vr6NtET0UX0bWfPNGbx4hx8BOgZ2Ls6e5Pb2B3U-2IOQemQCTdVU38HOfTBjjUCneyAPyIecnVp5Q8J4ccODQqradkF9fg_eYsB-C6eg9LjadGULsafT0sndx3Zm8CrZ0hmA33WZFH4aEOdP5lt6lOGDo6WybYg490rtlzOulGUxGCl-o6R2d0Sl23ZvoEXnnTZfx4596SB6_Xc6mP6rr2-9X04vryoq2HSppjAIjzh1a23Dmiy9WY-u48Gg8CCX5vGFMguPOMCUQULW1dCikbZy39SH5POquN_MVOls8J9PpdQork7Y6mqD_7fRhqRfxWdesUYzzInA2CthiIif0L7PA9C4OXeLQuzj0GEeZ-PR65Qv_9_4FOBkBb6I2ixSyfnzgDGoGqgEpdxJqJLCc5jlg0tkG7C26kNAO2sXw3_W_AZAOprY</recordid><startdate>20110318</startdate><enddate>20110318</enddate><creator>Bettaieb, Ahmed</creator><creator>Liu, Siming</creator><creator>Xi, Yannan</creator><creator>Nagata, Naoto</creator><creator>Matsuo, Kosuke</creator><creator>Matsuo, Izumi</creator><creator>Chahed, Samah</creator><creator>Bakke, Jesse</creator><creator>Keilhack, Heike</creator><creator>Tiganis, Tony</creator><creator>Haj, Fawaz G.</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>5PM</scope></search><sort><creationdate>20110318</creationdate><title>Differential Regulation of Endoplasmic Reticulum Stress by Protein Tyrosine Phosphatase 1B and T Cell Protein Tyrosine Phosphatase</title><author>Bettaieb, Ahmed ; Liu, Siming ; Xi, Yannan ; Nagata, Naoto ; Matsuo, Kosuke ; Matsuo, Izumi ; Chahed, Samah ; Bakke, Jesse ; Keilhack, Heike ; Tiganis, Tony ; Haj, Fawaz G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c466t-8aa91a47decc520f92503e6d24feaf14982b50081d2da094e1e9638de48c5dfc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Animals</topic><topic>Apoptosis</topic><topic>Cell Death</topic><topic>Cell Line, Tumor</topic><topic>Diabetes</topic><topic>Endoplasmic Reticulum (ER)</topic><topic>Endoplasmic Reticulum - enzymology</topic><topic>Endoplasmic Reticulum Stress</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Gene Expression Regulation, Enzymologic - drug effects</topic><topic>Gene Expression Regulation, Enzymologic - physiology</topic><topic>Gene Knockdown Techniques</topic><topic>HEK293 Cells</topic><topic>Humans</topic><topic>Insulin-Secreting Cells - enzymology</topic><topic>Mice</topic><topic>Palmitic Acid - pharmacology</topic><topic>Pancreas</topic><topic>Phosphotyrosine</topic><topic>Protein Tyrosine Phosphatase, Non-Receptor Type 1 - genetics</topic><topic>Protein Tyrosine Phosphatase, Non-Receptor Type 1 - metabolism</topic><topic>Protein Tyrosine Phosphatase, Non-Receptor Type 2 - genetics</topic><topic>Protein Tyrosine Phosphatase, Non-Receptor Type 2 - metabolism</topic><topic>Signal Transduction</topic><topic>Signal Transduction - drug effects</topic><topic>Signal Transduction - physiology</topic><topic>Tyrosine Protein Phosphatase (Tyrosine Phosphatase)</topic><topic>Unfolded Protein Response - drug effects</topic><topic>Unfolded Protein Response - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bettaieb, Ahmed</creatorcontrib><creatorcontrib>Liu, Siming</creatorcontrib><creatorcontrib>Xi, Yannan</creatorcontrib><creatorcontrib>Nagata, Naoto</creatorcontrib><creatorcontrib>Matsuo, Kosuke</creatorcontrib><creatorcontrib>Matsuo, Izumi</creatorcontrib><creatorcontrib>Chahed, Samah</creatorcontrib><creatorcontrib>Bakke, Jesse</creatorcontrib><creatorcontrib>Keilhack, Heike</creatorcontrib><creatorcontrib>Tiganis, Tony</creatorcontrib><creatorcontrib>Haj, Fawaz G.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bettaieb, Ahmed</au><au>Liu, Siming</au><au>Xi, Yannan</au><au>Nagata, Naoto</au><au>Matsuo, Kosuke</au><au>Matsuo, Izumi</au><au>Chahed, Samah</au><au>Bakke, Jesse</au><au>Keilhack, Heike</au><au>Tiganis, Tony</au><au>Haj, Fawaz G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Differential Regulation of Endoplasmic Reticulum Stress by Protein Tyrosine Phosphatase 1B and T Cell Protein Tyrosine Phosphatase</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2011-03-18</date><risdate>2011</risdate><volume>286</volume><issue>11</issue><spage>9225</spage><epage>9235</epage><pages>9225-9235</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>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.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>21216966</pmid><doi>10.1074/jbc.M110.186148</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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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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