Minor Thiols Cysteine and Cysteinylglycine Regulate the Competition between Glutathione and Protein SH Groups in Human Platelets Subjected to Oxidative Stress
Changes in the concentrations of protein-mixed disulfides (XS-SP) of glutathione (GSH), cysteine (CSH), and cysteinylglycine (CGSH) were studied in human platelets treated with diamide and t-BOOH in timecourse experiments (time range, 1–30 min) in order to understand the contribution of minor thiols...
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| Veröffentlicht in: | Archives of biochemistry and biophysics 2000-08, Vol.380 (1), p.1-10 |
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| creator | Giustarini, Daniela Campoccia, Giuseppe Fanetti, Giuseppe Rossi, Ranieri Giannerini, Fabiola Lusini, Lorenzo Di Simplicio, Paolo |
| description | Changes in the concentrations of protein-mixed disulfides (XS-SP) of glutathione (GSH), cysteine (CSH), and cysteinylglycine (CGSH) were studied in human platelets treated with diamide and t-BOOH in timecourse experiments (time range, 1–30 min) in order to understand the contribution of minor thiols CSH and CGSH to the regulation of glutathione–protein mixed disulfides (GS-SP). Diamide was much more potent than t-BOOH in altering the platelet thiol composition of XS-SP (threshold dose: diamide, 0.03 mM; t-BOOH, 0.5 mM) and caused reversible XS-SP peaks whose magnitude was related to the concentration of free thiols in untreated cells. Thus maximum levels of GS-SP (8 min after 0.4 mM diamide) were about 16-fold higher than those of controls (untreated platelets, GS-SP = 0.374 nmol/109 platelets), whereas those of CS-SP and CGS-SP were only 4-fold increased (untreated platelets, CS-SP = 0.112 nmol/109 platelets; CGS-SP = 0.024 nmol/109 platelets). The greater effects of diamide with respect to t-BOOH were explained on the basis of the activities of fast reactive protein SH groups for diamide and glutathione reductase (GR) and glucose-6-phosphate dehydrogenase (G-6-PDH) for t-BOOH. The addition of cysteine (0.3 mM, at 4 min) after treatment of platelets with 0.4 mM diamide increased the rate of reversal of GS-SP peaks to normal values, but also caused a relevant change in CGS-SP with respect to that of platelets treated with diamide alone. An increased γ-glutamyltranspeptidase activity was found in platelets treated with diamide. Moreover, untreated platelets were found to release and hydrolyze GSH to CGSH and CSH. Ratios of thiols/disulfides (XSH/XSSX) and activities of GR and G-6PDH were also related to a high reducing potential exerted by GSH but not by minor thiols. The lower mass and charge of minor thiols is a likely requisite of the regulation of GS-SP levels in platelets. |
| doi_str_mv | 10.1006/abbi.2000.1847 |
| format | Article |
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Diamide was much more potent than t-BOOH in altering the platelet thiol composition of XS-SP (threshold dose: diamide, 0.03 mM; t-BOOH, 0.5 mM) and caused reversible XS-SP peaks whose magnitude was related to the concentration of free thiols in untreated cells. Thus maximum levels of GS-SP (8 min after 0.4 mM diamide) were about 16-fold higher than those of controls (untreated platelets, GS-SP = 0.374 nmol/109 platelets), whereas those of CS-SP and CGS-SP were only 4-fold increased (untreated platelets, CS-SP = 0.112 nmol/109 platelets; CGS-SP = 0.024 nmol/109 platelets). The greater effects of diamide with respect to t-BOOH were explained on the basis of the activities of fast reactive protein SH groups for diamide and glutathione reductase (GR) and glucose-6-phosphate dehydrogenase (G-6-PDH) for t-BOOH. The addition of cysteine (0.3 mM, at 4 min) after treatment of platelets with 0.4 mM diamide increased the rate of reversal of GS-SP peaks to normal values, but also caused a relevant change in CGS-SP with respect to that of platelets treated with diamide alone. An increased γ-glutamyltranspeptidase activity was found in platelets treated with diamide. Moreover, untreated platelets were found to release and hydrolyze GSH to CGSH and CSH. Ratios of thiols/disulfides (XSH/XSSX) and activities of GR and G-6PDH were also related to a high reducing potential exerted by GSH but not by minor thiols. The lower mass and charge of minor thiols is a likely requisite of the regulation of GS-SP levels in platelets.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1006/abbi.2000.1847</identifier><identifier>PMID: 10900126</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>antioxidant enzymes ; Antioxidants - metabolism ; Blood Platelets - drug effects ; Blood Platelets - metabolism ; Chromatography, High Pressure Liquid ; cysteine ; Cysteine - metabolism ; cysteinylglycine ; Diamide - pharmacology ; Dipeptides - metabolism ; Disulfides - metabolism ; Dithionitrobenzoic Acid - pharmacology ; Erythrocytes - metabolism ; glutathione ; Glutathione - metabolism ; human platelets ; Humans ; Oxidative Stress ; protein SH groups ; S-thiolation/dethiolation ; Spectrophotometry ; src Homology Domains ; Sulfhydryl Compounds - physiology ; tert-Butylhydroperoxide - pharmacology ; Time Factors</subject><ispartof>Archives of biochemistry and biophysics, 2000-08, Vol.380 (1), p.1-10</ispartof><rights>2000 Academic Press</rights><rights>Copyright 2000 Academic Press.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c340t-cc016486c45d5df59b83d6cf26d62545e106fbac2ffcfce0b636a78b014d79493</citedby><cites>FETCH-LOGICAL-c340t-cc016486c45d5df59b83d6cf26d62545e106fbac2ffcfce0b636a78b014d79493</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1006/abbi.2000.1847$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10900126$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Giustarini, Daniela</creatorcontrib><creatorcontrib>Campoccia, Giuseppe</creatorcontrib><creatorcontrib>Fanetti, Giuseppe</creatorcontrib><creatorcontrib>Rossi, Ranieri</creatorcontrib><creatorcontrib>Giannerini, Fabiola</creatorcontrib><creatorcontrib>Lusini, Lorenzo</creatorcontrib><creatorcontrib>Di Simplicio, Paolo</creatorcontrib><title>Minor Thiols Cysteine and Cysteinylglycine Regulate the Competition between Glutathione and Protein SH Groups in Human Platelets Subjected to Oxidative Stress</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>Changes in the concentrations of protein-mixed disulfides (XS-SP) of glutathione (GSH), cysteine (CSH), and cysteinylglycine (CGSH) were studied in human platelets treated with diamide and t-BOOH in timecourse experiments (time range, 1–30 min) in order to understand the contribution of minor thiols CSH and CGSH to the regulation of glutathione–protein mixed disulfides (GS-SP). Diamide was much more potent than t-BOOH in altering the platelet thiol composition of XS-SP (threshold dose: diamide, 0.03 mM; t-BOOH, 0.5 mM) and caused reversible XS-SP peaks whose magnitude was related to the concentration of free thiols in untreated cells. Thus maximum levels of GS-SP (8 min after 0.4 mM diamide) were about 16-fold higher than those of controls (untreated platelets, GS-SP = 0.374 nmol/109 platelets), whereas those of CS-SP and CGS-SP were only 4-fold increased (untreated platelets, CS-SP = 0.112 nmol/109 platelets; CGS-SP = 0.024 nmol/109 platelets). The greater effects of diamide with respect to t-BOOH were explained on the basis of the activities of fast reactive protein SH groups for diamide and glutathione reductase (GR) and glucose-6-phosphate dehydrogenase (G-6-PDH) for t-BOOH. The addition of cysteine (0.3 mM, at 4 min) after treatment of platelets with 0.4 mM diamide increased the rate of reversal of GS-SP peaks to normal values, but also caused a relevant change in CGS-SP with respect to that of platelets treated with diamide alone. An increased γ-glutamyltranspeptidase activity was found in platelets treated with diamide. Moreover, untreated platelets were found to release and hydrolyze GSH to CGSH and CSH. Ratios of thiols/disulfides (XSH/XSSX) and activities of GR and G-6PDH were also related to a high reducing potential exerted by GSH but not by minor thiols. The lower mass and charge of minor thiols is a likely requisite of the regulation of GS-SP levels in platelets.</description><subject>antioxidant enzymes</subject><subject>Antioxidants - metabolism</subject><subject>Blood Platelets - drug effects</subject><subject>Blood Platelets - metabolism</subject><subject>Chromatography, High Pressure Liquid</subject><subject>cysteine</subject><subject>Cysteine - metabolism</subject><subject>cysteinylglycine</subject><subject>Diamide - pharmacology</subject><subject>Dipeptides - metabolism</subject><subject>Disulfides - metabolism</subject><subject>Dithionitrobenzoic Acid - pharmacology</subject><subject>Erythrocytes - metabolism</subject><subject>glutathione</subject><subject>Glutathione - metabolism</subject><subject>human platelets</subject><subject>Humans</subject><subject>Oxidative Stress</subject><subject>protein SH groups</subject><subject>S-thiolation/dethiolation</subject><subject>Spectrophotometry</subject><subject>src Homology Domains</subject><subject>Sulfhydryl Compounds - physiology</subject><subject>tert-Butylhydroperoxide - pharmacology</subject><subject>Time Factors</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kc1uEzEURq0K1IbCliXyit0Ee-xxZpYogqRSUStS1pZ_7rSuPONge0rzMn3WepQgsWF19V0dH-n6Q-gjJUtKiPiitHbLmpASW746QwtKOlER1vI3aFHWrOpaQS_Qu5QeCaGUi_ocXRSohFos0MsPN4aI7x5c8AmvDymDGwGr0f4NB3_vD2Ze_oT7yasMOD8AXodhD9llF0asIf8BGPHGT1nlojoZbmOYDXi3xZsYpn3CJWynQY34dhZ5yAnvJv0IJoPFOeCbZ2dVdk-AdzlCSu_R2175BB9O8xL9-v7tbr2trm82V-uv15VhnOTKGEIFb4XhjW1s33S6ZVaYvhZW1A1vgBLRa2Xqvje9AaIFE2rVakK5XXW8Y5fo89G7j-H3BCnLwSUD3qsRwpTkitaMsoYVcHkETQwpRejlPrpBxYOkRM6NyLkROTci50bKg08n86QHsP_gxwoK0B4BKPc9OYgyGQejAeti-Rdpg_uf-xVIgJ20</recordid><startdate>20000801</startdate><enddate>20000801</enddate><creator>Giustarini, Daniela</creator><creator>Campoccia, Giuseppe</creator><creator>Fanetti, Giuseppe</creator><creator>Rossi, Ranieri</creator><creator>Giannerini, Fabiola</creator><creator>Lusini, Lorenzo</creator><creator>Di Simplicio, Paolo</creator><general>Elsevier Inc</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>7X8</scope></search><sort><creationdate>20000801</creationdate><title>Minor Thiols Cysteine and Cysteinylglycine Regulate the Competition between Glutathione and Protein SH Groups in Human Platelets Subjected to Oxidative Stress</title><author>Giustarini, Daniela ; Campoccia, Giuseppe ; Fanetti, Giuseppe ; Rossi, Ranieri ; Giannerini, Fabiola ; Lusini, Lorenzo ; Di Simplicio, Paolo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c340t-cc016486c45d5df59b83d6cf26d62545e106fbac2ffcfce0b636a78b014d79493</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>antioxidant enzymes</topic><topic>Antioxidants - metabolism</topic><topic>Blood Platelets - drug effects</topic><topic>Blood Platelets - metabolism</topic><topic>Chromatography, High Pressure Liquid</topic><topic>cysteine</topic><topic>Cysteine - metabolism</topic><topic>cysteinylglycine</topic><topic>Diamide - pharmacology</topic><topic>Dipeptides - metabolism</topic><topic>Disulfides - metabolism</topic><topic>Dithionitrobenzoic Acid - pharmacology</topic><topic>Erythrocytes - metabolism</topic><topic>glutathione</topic><topic>Glutathione - metabolism</topic><topic>human platelets</topic><topic>Humans</topic><topic>Oxidative Stress</topic><topic>protein SH groups</topic><topic>S-thiolation/dethiolation</topic><topic>Spectrophotometry</topic><topic>src Homology Domains</topic><topic>Sulfhydryl Compounds - physiology</topic><topic>tert-Butylhydroperoxide - pharmacology</topic><topic>Time Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Giustarini, Daniela</creatorcontrib><creatorcontrib>Campoccia, Giuseppe</creatorcontrib><creatorcontrib>Fanetti, Giuseppe</creatorcontrib><creatorcontrib>Rossi, Ranieri</creatorcontrib><creatorcontrib>Giannerini, Fabiola</creatorcontrib><creatorcontrib>Lusini, Lorenzo</creatorcontrib><creatorcontrib>Di Simplicio, Paolo</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Giustarini, Daniela</au><au>Campoccia, Giuseppe</au><au>Fanetti, Giuseppe</au><au>Rossi, Ranieri</au><au>Giannerini, Fabiola</au><au>Lusini, Lorenzo</au><au>Di Simplicio, Paolo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Minor Thiols Cysteine and Cysteinylglycine Regulate the Competition between Glutathione and Protein SH Groups in Human Platelets Subjected to Oxidative Stress</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>2000-08-01</date><risdate>2000</risdate><volume>380</volume><issue>1</issue><spage>1</spage><epage>10</epage><pages>1-10</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><abstract>Changes in the concentrations of protein-mixed disulfides (XS-SP) of glutathione (GSH), cysteine (CSH), and cysteinylglycine (CGSH) were studied in human platelets treated with diamide and t-BOOH in timecourse experiments (time range, 1–30 min) in order to understand the contribution of minor thiols CSH and CGSH to the regulation of glutathione–protein mixed disulfides (GS-SP). Diamide was much more potent than t-BOOH in altering the platelet thiol composition of XS-SP (threshold dose: diamide, 0.03 mM; t-BOOH, 0.5 mM) and caused reversible XS-SP peaks whose magnitude was related to the concentration of free thiols in untreated cells. Thus maximum levels of GS-SP (8 min after 0.4 mM diamide) were about 16-fold higher than those of controls (untreated platelets, GS-SP = 0.374 nmol/109 platelets), whereas those of CS-SP and CGS-SP were only 4-fold increased (untreated platelets, CS-SP = 0.112 nmol/109 platelets; CGS-SP = 0.024 nmol/109 platelets). The greater effects of diamide with respect to t-BOOH were explained on the basis of the activities of fast reactive protein SH groups for diamide and glutathione reductase (GR) and glucose-6-phosphate dehydrogenase (G-6-PDH) for t-BOOH. The addition of cysteine (0.3 mM, at 4 min) after treatment of platelets with 0.4 mM diamide increased the rate of reversal of GS-SP peaks to normal values, but also caused a relevant change in CGS-SP with respect to that of platelets treated with diamide alone. An increased γ-glutamyltranspeptidase activity was found in platelets treated with diamide. Moreover, untreated platelets were found to release and hydrolyze GSH to CGSH and CSH. Ratios of thiols/disulfides (XSH/XSSX) and activities of GR and G-6PDH were also related to a high reducing potential exerted by GSH but not by minor thiols. The lower mass and charge of minor thiols is a likely requisite of the regulation of GS-SP levels in platelets.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>10900126</pmid><doi>10.1006/abbi.2000.1847</doi><tpages>10</tpages></addata></record> |
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| subjects | antioxidant enzymes Antioxidants - metabolism Blood Platelets - drug effects Blood Platelets - metabolism Chromatography, High Pressure Liquid cysteine Cysteine - metabolism cysteinylglycine Diamide - pharmacology Dipeptides - metabolism Disulfides - metabolism Dithionitrobenzoic Acid - pharmacology Erythrocytes - metabolism glutathione Glutathione - metabolism human platelets Humans Oxidative Stress protein SH groups S-thiolation/dethiolation Spectrophotometry src Homology Domains Sulfhydryl Compounds - physiology tert-Butylhydroperoxide - pharmacology Time Factors |
| title | Minor Thiols Cysteine and Cysteinylglycine Regulate the Competition between Glutathione and Protein SH Groups in Human Platelets Subjected to Oxidative Stress |
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