Redox-Sensing Release of Human Thioredoxin from T Lymphocytes with Negative Feedback Loops
Thioredoxin (TRX) is released from various types of mammalian cells despite no typical secretory signal sequence. We show here that a redox-active site in TRX is essential for its release from T lymphocytes in response to H2O2 and extracellular TRX regulates its own H2O2-induced release. Human T cel...
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Veröffentlicht in: | The Journal of immunology (1950) 2004-01, Vol.172 (1), p.442-448 |
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description | Thioredoxin (TRX) is released from various types of mammalian cells despite no typical secretory signal sequence. We show here that a redox-active site in TRX is essential for its release from T lymphocytes in response to H2O2 and extracellular TRX regulates its own H2O2-induced release. Human T cell leukemia virus type I-transformed T lymphocytes constitutively release a large amount of TRX. The level of TRX release is augmented upon the addition of H2O2, but suppressed upon the addition of N-acetylcysteine. In the culture supernatant of a Jurkat transfectant expressing the tagged TRX-wild type (WT), the tagged TRX protein is rapidly released at 1 h and kept at a constant level until 6 h after the addition of H2O2. In contrast, another type of transfectant expressing the tagged TRX mutant (C32S/C35S; CS) fails to release the protein. H2O2-induced release of TRX from the transfectant is inhibited by the presence of rTRX-WT in a dose-dependent manner. Preincubation of the transfectant with rTRX-WT for 1 h at 37 degrees C, but not 0 degrees C, results in a significant suppression of the TRX release, reactive oxygen species, and caspase-3 activity induced by H2O2, respectively. Confocal microscopy and Western blot analysis show that extracellular rTRX-WT added to the culture does not obviously enter T lymphocytes until 24 h. These results collectively suggest that the oxidative stress-induced TRX release from T lymphocytes depends on a redox-sensitive event and may be regulated by negative feedback loops using reactive oxygen species-mediated signal transductions. |
doi_str_mv | 10.4049/jimmunol.172.1.442 |
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We show here that a redox-active site in TRX is essential for its release from T lymphocytes in response to H2O2 and extracellular TRX regulates its own H2O2-induced release. Human T cell leukemia virus type I-transformed T lymphocytes constitutively release a large amount of TRX. The level of TRX release is augmented upon the addition of H2O2, but suppressed upon the addition of N-acetylcysteine. In the culture supernatant of a Jurkat transfectant expressing the tagged TRX-wild type (WT), the tagged TRX protein is rapidly released at 1 h and kept at a constant level until 6 h after the addition of H2O2. In contrast, another type of transfectant expressing the tagged TRX mutant (C32S/C35S; CS) fails to release the protein. H2O2-induced release of TRX from the transfectant is inhibited by the presence of rTRX-WT in a dose-dependent manner. Preincubation of the transfectant with rTRX-WT for 1 h at 37 degrees C, but not 0 degrees C, results in a significant suppression of the TRX release, reactive oxygen species, and caspase-3 activity induced by H2O2, respectively. Confocal microscopy and Western blot analysis show that extracellular rTRX-WT added to the culture does not obviously enter T lymphocytes until 24 h. These results collectively suggest that the oxidative stress-induced TRX release from T lymphocytes depends on a redox-sensitive event and may be regulated by negative feedback loops using reactive oxygen species-mediated signal transductions.</description><identifier>ISSN: 0022-1767</identifier><identifier>EISSN: 1550-6606</identifier><identifier>DOI: 10.4049/jimmunol.172.1.442</identifier><identifier>PMID: 14688353</identifier><language>eng</language><publisher>United States: Am Assoc Immnol</publisher><subject>Apoptosis - genetics ; Apoptosis - physiology ; Binding Sites - genetics ; Binding Sites - physiology ; Cell Line, Transformed ; Extracellular Fluid - metabolism ; Extracellular Fluid - physiology ; Feedback, Physiological - genetics ; Feedback, Physiological - physiology ; Human T-lymphotropic virus 1 - physiology ; Humans ; Hydrogen Peroxide - antagonists & inhibitors ; Hydrogen Peroxide - pharmacology ; Jurkat Cells ; Oxidation-Reduction ; Oxidative Stress - genetics ; Oxidative Stress - physiology ; Recombinant Proteins - pharmacology ; Signal Transduction - genetics ; Signal Transduction - physiology ; T-Lymphocytes - drug effects ; T-Lymphocytes - metabolism ; Thioredoxins - genetics ; Thioredoxins - metabolism ; Transfection</subject><ispartof>The Journal of immunology (1950), 2004-01, Vol.172 (1), p.442-448</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c405t-49e3ec09aa66b6f144bd86ca0c0974121de8333efbc2fcd91596d3ff79ec187b3</citedby><cites>FETCH-LOGICAL-c405t-49e3ec09aa66b6f144bd86ca0c0974121de8333efbc2fcd91596d3ff79ec187b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14688353$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kondo, Norihiko</creatorcontrib><creatorcontrib>Ishii, Yasuyuki</creatorcontrib><creatorcontrib>Kwon, Yong-Won</creatorcontrib><creatorcontrib>Tanito, Masaki</creatorcontrib><creatorcontrib>Horita, Hiroyuki</creatorcontrib><creatorcontrib>Nishinaka, Yumiko</creatorcontrib><creatorcontrib>Nakamura, Hajime</creatorcontrib><creatorcontrib>Yodoi, Junji</creatorcontrib><title>Redox-Sensing Release of Human Thioredoxin from T Lymphocytes with Negative Feedback Loops</title><title>The Journal of immunology (1950)</title><addtitle>J Immunol</addtitle><description>Thioredoxin (TRX) is released from various types of mammalian cells despite no typical secretory signal sequence. We show here that a redox-active site in TRX is essential for its release from T lymphocytes in response to H2O2 and extracellular TRX regulates its own H2O2-induced release. Human T cell leukemia virus type I-transformed T lymphocytes constitutively release a large amount of TRX. The level of TRX release is augmented upon the addition of H2O2, but suppressed upon the addition of N-acetylcysteine. In the culture supernatant of a Jurkat transfectant expressing the tagged TRX-wild type (WT), the tagged TRX protein is rapidly released at 1 h and kept at a constant level until 6 h after the addition of H2O2. In contrast, another type of transfectant expressing the tagged TRX mutant (C32S/C35S; CS) fails to release the protein. H2O2-induced release of TRX from the transfectant is inhibited by the presence of rTRX-WT in a dose-dependent manner. Preincubation of the transfectant with rTRX-WT for 1 h at 37 degrees C, but not 0 degrees C, results in a significant suppression of the TRX release, reactive oxygen species, and caspase-3 activity induced by H2O2, respectively. Confocal microscopy and Western blot analysis show that extracellular rTRX-WT added to the culture does not obviously enter T lymphocytes until 24 h. These results collectively suggest that the oxidative stress-induced TRX release from T lymphocytes depends on a redox-sensitive event and may be regulated by negative feedback loops using reactive oxygen species-mediated signal transductions.</description><subject>Apoptosis - genetics</subject><subject>Apoptosis - physiology</subject><subject>Binding Sites - genetics</subject><subject>Binding Sites - physiology</subject><subject>Cell Line, Transformed</subject><subject>Extracellular Fluid - metabolism</subject><subject>Extracellular Fluid - physiology</subject><subject>Feedback, Physiological - genetics</subject><subject>Feedback, Physiological - physiology</subject><subject>Human T-lymphotropic virus 1 - physiology</subject><subject>Humans</subject><subject>Hydrogen Peroxide - antagonists & inhibitors</subject><subject>Hydrogen Peroxide - pharmacology</subject><subject>Jurkat Cells</subject><subject>Oxidation-Reduction</subject><subject>Oxidative Stress - genetics</subject><subject>Oxidative Stress - physiology</subject><subject>Recombinant Proteins - pharmacology</subject><subject>Signal Transduction - genetics</subject><subject>Signal Transduction - physiology</subject><subject>T-Lymphocytes - drug effects</subject><subject>T-Lymphocytes - metabolism</subject><subject>Thioredoxins - genetics</subject><subject>Thioredoxins - metabolism</subject><subject>Transfection</subject><issn>0022-1767</issn><issn>1550-6606</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkLFu2zAQhokiQeOkfYEOAadsUkmKoqSxCOq6gJEAjrN0ISjqaDERRVeUovrtSyMuPHY64PD9_-E-hL5QknLCq68v1rmp911KC5bSlHP2AS1onpNECCIu0IIQxhJaiOIKXYfwQggRhPGP6IpyUZZZni3Qrw00_k_yBH2w_Q5voAMVAHuDV5NTPd621g9HxPbYDN7hLV4f3L71-jBCwLMdW_wAOzXaN8BLgKZW-hWvvd-HT-jSqC7A59O8Qc_L79v7VbJ-_PHz_ts60ZzkY8IryECTSikhamEo53VTCq1I3BWcMtpAmWUZmFozo5uK5pVoMmOKCjQtizq7QXfvvfvB_54gjNLZoKHrVA9-CrKMb8dM9V-QVoxFZXkE2TuoBx_CAEbuB-vUcJCUyKN6-U-9jOollVF9DN2e2qfaQXOOnFyfz7d21852ABmc6rqIUznP87npL7zhj6Y</recordid><startdate>20040101</startdate><enddate>20040101</enddate><creator>Kondo, Norihiko</creator><creator>Ishii, Yasuyuki</creator><creator>Kwon, Yong-Won</creator><creator>Tanito, Masaki</creator><creator>Horita, Hiroyuki</creator><creator>Nishinaka, Yumiko</creator><creator>Nakamura, Hajime</creator><creator>Yodoi, Junji</creator><general>Am Assoc Immnol</general><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>7T5</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>20040101</creationdate><title>Redox-Sensing Release of Human Thioredoxin from T Lymphocytes with Negative Feedback Loops</title><author>Kondo, Norihiko ; Ishii, Yasuyuki ; Kwon, Yong-Won ; Tanito, Masaki ; Horita, Hiroyuki ; Nishinaka, Yumiko ; Nakamura, Hajime ; Yodoi, Junji</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c405t-49e3ec09aa66b6f144bd86ca0c0974121de8333efbc2fcd91596d3ff79ec187b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Apoptosis - genetics</topic><topic>Apoptosis - physiology</topic><topic>Binding Sites - genetics</topic><topic>Binding Sites - physiology</topic><topic>Cell Line, Transformed</topic><topic>Extracellular Fluid - metabolism</topic><topic>Extracellular Fluid - physiology</topic><topic>Feedback, Physiological - genetics</topic><topic>Feedback, Physiological - physiology</topic><topic>Human T-lymphotropic virus 1 - physiology</topic><topic>Humans</topic><topic>Hydrogen Peroxide - antagonists & inhibitors</topic><topic>Hydrogen Peroxide - pharmacology</topic><topic>Jurkat Cells</topic><topic>Oxidation-Reduction</topic><topic>Oxidative Stress - genetics</topic><topic>Oxidative Stress - physiology</topic><topic>Recombinant Proteins - pharmacology</topic><topic>Signal Transduction - genetics</topic><topic>Signal Transduction - physiology</topic><topic>T-Lymphocytes - drug effects</topic><topic>T-Lymphocytes - metabolism</topic><topic>Thioredoxins - genetics</topic><topic>Thioredoxins - metabolism</topic><topic>Transfection</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kondo, Norihiko</creatorcontrib><creatorcontrib>Ishii, Yasuyuki</creatorcontrib><creatorcontrib>Kwon, Yong-Won</creatorcontrib><creatorcontrib>Tanito, Masaki</creatorcontrib><creatorcontrib>Horita, Hiroyuki</creatorcontrib><creatorcontrib>Nishinaka, Yumiko</creatorcontrib><creatorcontrib>Nakamura, Hajime</creatorcontrib><creatorcontrib>Yodoi, Junji</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Immunology Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of immunology (1950)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kondo, Norihiko</au><au>Ishii, Yasuyuki</au><au>Kwon, Yong-Won</au><au>Tanito, Masaki</au><au>Horita, Hiroyuki</au><au>Nishinaka, Yumiko</au><au>Nakamura, Hajime</au><au>Yodoi, Junji</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Redox-Sensing Release of Human Thioredoxin from T Lymphocytes with Negative Feedback Loops</atitle><jtitle>The Journal of immunology (1950)</jtitle><addtitle>J Immunol</addtitle><date>2004-01-01</date><risdate>2004</risdate><volume>172</volume><issue>1</issue><spage>442</spage><epage>448</epage><pages>442-448</pages><issn>0022-1767</issn><eissn>1550-6606</eissn><abstract>Thioredoxin (TRX) is released from various types of mammalian cells despite no typical secretory signal sequence. We show here that a redox-active site in TRX is essential for its release from T lymphocytes in response to H2O2 and extracellular TRX regulates its own H2O2-induced release. Human T cell leukemia virus type I-transformed T lymphocytes constitutively release a large amount of TRX. The level of TRX release is augmented upon the addition of H2O2, but suppressed upon the addition of N-acetylcysteine. In the culture supernatant of a Jurkat transfectant expressing the tagged TRX-wild type (WT), the tagged TRX protein is rapidly released at 1 h and kept at a constant level until 6 h after the addition of H2O2. In contrast, another type of transfectant expressing the tagged TRX mutant (C32S/C35S; CS) fails to release the protein. H2O2-induced release of TRX from the transfectant is inhibited by the presence of rTRX-WT in a dose-dependent manner. Preincubation of the transfectant with rTRX-WT for 1 h at 37 degrees C, but not 0 degrees C, results in a significant suppression of the TRX release, reactive oxygen species, and caspase-3 activity induced by H2O2, respectively. Confocal microscopy and Western blot analysis show that extracellular rTRX-WT added to the culture does not obviously enter T lymphocytes until 24 h. These results collectively suggest that the oxidative stress-induced TRX release from T lymphocytes depends on a redox-sensitive event and may be regulated by negative feedback loops using reactive oxygen species-mediated signal transductions.</abstract><cop>United States</cop><pub>Am Assoc Immnol</pub><pmid>14688353</pmid><doi>10.4049/jimmunol.172.1.442</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Apoptosis - genetics Apoptosis - physiology Binding Sites - genetics Binding Sites - physiology Cell Line, Transformed Extracellular Fluid - metabolism Extracellular Fluid - physiology Feedback, Physiological - genetics Feedback, Physiological - physiology Human T-lymphotropic virus 1 - physiology Humans Hydrogen Peroxide - antagonists & inhibitors Hydrogen Peroxide - pharmacology Jurkat Cells Oxidation-Reduction Oxidative Stress - genetics Oxidative Stress - physiology Recombinant Proteins - pharmacology Signal Transduction - genetics Signal Transduction - physiology T-Lymphocytes - drug effects T-Lymphocytes - metabolism Thioredoxins - genetics Thioredoxins - metabolism Transfection |
title | Redox-Sensing Release of Human Thioredoxin from T Lymphocytes with Negative Feedback Loops |
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