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Proteasome mediates removal of proteins oxidized during myocardial ischemia
Numerous proteins are known to be lost following myocardial ischemia/reperfusion yet little is known about the mediating proteinases. This study examines the hypothesis that proteasome plays a significant role in the removal of proteins oxidized during myocardial ischemia. Proteasome was inhibited b...
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| Published in: | Free radical biology & medicine 2006, Vol.40 (1), p.156-164 |
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| cites | cdi_FETCH-LOGICAL-c447t-cca69c70b28901e5de1b0ad8d06ed957ff89c90cd9286f2ed868693f52ce43623 |
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| container_title | Free radical biology & medicine |
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| creator | Divald, Andras Powell, Saul R. |
| description | Numerous proteins are known to be lost following myocardial ischemia/reperfusion yet little is known about the mediating proteinases. This study examines the hypothesis that proteasome plays a significant role in the removal of proteins oxidized during myocardial ischemia. Proteasome was inhibited by perfusing isolated rat hearts with buffer containing lactacystin, 2 μmol/L, for 10 min, which resulted in 51 and 42% decreases in 20S and 26S proteasome activities that persisted for a minimum of 90 min. Lactacystin pretreatment had minor effects on postischemic recovery of isolated hearts exposed to 30 min global ischemia and 60 min reperfusion. Protein carbonyl content of lactacystin-pretreated ischemic hearts was significantly (
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| doi_str_mv | 10.1016/j.freeradbiomed.2005.09.022 |
| format | article |
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P < 0.05) increased. One band with approximate molecular mass of 50 kDa is known to contain oxidized actin. Actin degradation was quantitated by analysis of 3-methylhistidine which was significantly (
P < 0.05) decreased by 15% following 30 min ischemia and 60 min reperfusion. Pretreatment of ischemic hearts with lactacystin prevented much of the loss (−6.5%) of 3-methylhistidine. Probing immunoprecipitated actin with an antibody specific for ubiquitin revealed no bands containing ubiquitinated homologues of this protein. These observations support the conclusion that proteasome mediates removal of some of the proteins oxidized during myocardial ischemia/reperfusion, and that at least oxidized actin is removed by the 20S proteasome.</description><identifier>ISSN: 0891-5849</identifier><identifier>EISSN: 1873-4596</identifier><identifier>DOI: 10.1016/j.freeradbiomed.2005.09.022</identifier><identifier>PMID: 16337889</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>3-Methylhistidine ; Acetylcysteine - analogs & derivatives ; Acetylcysteine - pharmacology ; Actin ; Actins - metabolism ; Animals ; Cysteine Proteinase Inhibitors - pharmacology ; Free radical ; Heart - physiopathology ; Immunoprecipitation ; Ischemic Preconditioning, Myocardial ; Male ; Methylhistidines - metabolism ; Myocardial ischemia ; Myocardial Ischemia - metabolism ; Myocardial Ischemia - pathology ; Oxidation-Reduction ; Proteasome ; Proteasome Endopeptidase Complex - metabolism ; Proteasome Inhibitors ; Protein oxidation ; Proteins - metabolism ; Rats ; Rats, Sprague-Dawley ; Reperfusion ; Ubiquitin - metabolism</subject><ispartof>Free radical biology & medicine, 2006, Vol.40 (1), p.156-164</ispartof><rights>2005 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c447t-cca69c70b28901e5de1b0ad8d06ed957ff89c90cd9286f2ed868693f52ce43623</citedby><cites>FETCH-LOGICAL-c447t-cca69c70b28901e5de1b0ad8d06ed957ff89c90cd9286f2ed868693f52ce43623</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,4010,27904,27905,27906</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16337889$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Divald, Andras</creatorcontrib><creatorcontrib>Powell, Saul R.</creatorcontrib><title>Proteasome mediates removal of proteins oxidized during myocardial ischemia</title><title>Free radical biology & medicine</title><addtitle>Free Radic Biol Med</addtitle><description>Numerous proteins are known to be lost following myocardial ischemia/reperfusion yet little is known about the mediating proteinases. This study examines the hypothesis that proteasome plays a significant role in the removal of proteins oxidized during myocardial ischemia. Proteasome was inhibited by perfusing isolated rat hearts with buffer containing lactacystin, 2 μmol/L, for 10 min, which resulted in 51 and 42% decreases in 20S and 26S proteasome activities that persisted for a minimum of 90 min. Lactacystin pretreatment had minor effects on postischemic recovery of isolated hearts exposed to 30 min global ischemia and 60 min reperfusion. Protein carbonyl content of lactacystin-pretreated ischemic hearts was significantly (
P < 0.05) increased. One band with approximate molecular mass of 50 kDa is known to contain oxidized actin. Actin degradation was quantitated by analysis of 3-methylhistidine which was significantly (
P < 0.05) decreased by 15% following 30 min ischemia and 60 min reperfusion. Pretreatment of ischemic hearts with lactacystin prevented much of the loss (−6.5%) of 3-methylhistidine. Probing immunoprecipitated actin with an antibody specific for ubiquitin revealed no bands containing ubiquitinated homologues of this protein. These observations support the conclusion that proteasome mediates removal of some of the proteins oxidized during myocardial ischemia/reperfusion, and that at least oxidized actin is removed by the 20S proteasome.</description><subject>3-Methylhistidine</subject><subject>Acetylcysteine - analogs & derivatives</subject><subject>Acetylcysteine - pharmacology</subject><subject>Actin</subject><subject>Actins - metabolism</subject><subject>Animals</subject><subject>Cysteine Proteinase Inhibitors - pharmacology</subject><subject>Free radical</subject><subject>Heart - physiopathology</subject><subject>Immunoprecipitation</subject><subject>Ischemic Preconditioning, Myocardial</subject><subject>Male</subject><subject>Methylhistidines - metabolism</subject><subject>Myocardial ischemia</subject><subject>Myocardial Ischemia - metabolism</subject><subject>Myocardial Ischemia - pathology</subject><subject>Oxidation-Reduction</subject><subject>Proteasome</subject><subject>Proteasome Endopeptidase Complex - metabolism</subject><subject>Proteasome Inhibitors</subject><subject>Protein oxidation</subject><subject>Proteins - metabolism</subject><subject>Rats</subject><subject>Rats, Sprague-Dawley</subject><subject>Reperfusion</subject><subject>Ubiquitin - metabolism</subject><issn>0891-5849</issn><issn>1873-4596</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><recordid>eNqNkEtLxDAQx4Mouj6-ghQEb62TtE0TPImsDxT0oOeQJlPN0m406S6un94suwjePM3h_5iZHyFnFAoKlF_Mii4gBm1b5we0BQOoC5AFMLZDJlQ0ZV7Vku-SCQhJ81pU8oAcxjgDgKouxT45oLwsGyHkhDw8Bz-ijqkpS2VOjxizgINf6j7zXfaxlt08Zv7LWfeNNrOL4OZv2bDyRocU6DMXzTsOTh-TvU73EU-284i83kxfru_yx6fb--urx9xUVTPmxmguTQMtExIo1hZpC9oKCxytrJuuE9JIMFYywTuGVnDBZdnVzGBVclYekfNNbzruc4FxVEM6Aftez9EvomqASi4YTcbLjdEEH2PATn0EN-iwUhTUmqWaqT8s1ZqlAqkSy5Q-3a5ZtGvtN7uFlwzTjQHTs0uHQUXjcG4SxoBmVNa7fy36AfTljr0</recordid><startdate>2006</startdate><enddate>2006</enddate><creator>Divald, Andras</creator><creator>Powell, Saul R.</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>2006</creationdate><title>Proteasome mediates removal of proteins oxidized during myocardial ischemia</title><author>Divald, Andras ; Powell, Saul R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c447t-cca69c70b28901e5de1b0ad8d06ed957ff89c90cd9286f2ed868693f52ce43623</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>3-Methylhistidine</topic><topic>Acetylcysteine - analogs & derivatives</topic><topic>Acetylcysteine - pharmacology</topic><topic>Actin</topic><topic>Actins - metabolism</topic><topic>Animals</topic><topic>Cysteine Proteinase Inhibitors - pharmacology</topic><topic>Free radical</topic><topic>Heart - physiopathology</topic><topic>Immunoprecipitation</topic><topic>Ischemic Preconditioning, Myocardial</topic><topic>Male</topic><topic>Methylhistidines - metabolism</topic><topic>Myocardial ischemia</topic><topic>Myocardial Ischemia - metabolism</topic><topic>Myocardial Ischemia - pathology</topic><topic>Oxidation-Reduction</topic><topic>Proteasome</topic><topic>Proteasome Endopeptidase Complex - metabolism</topic><topic>Proteasome Inhibitors</topic><topic>Protein oxidation</topic><topic>Proteins - metabolism</topic><topic>Rats</topic><topic>Rats, Sprague-Dawley</topic><topic>Reperfusion</topic><topic>Ubiquitin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Divald, Andras</creatorcontrib><creatorcontrib>Powell, Saul R.</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>Free radical biology & medicine</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Divald, Andras</au><au>Powell, Saul R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Proteasome mediates removal of proteins oxidized during myocardial ischemia</atitle><jtitle>Free radical biology & medicine</jtitle><addtitle>Free Radic Biol Med</addtitle><date>2006</date><risdate>2006</risdate><volume>40</volume><issue>1</issue><spage>156</spage><epage>164</epage><pages>156-164</pages><issn>0891-5849</issn><eissn>1873-4596</eissn><abstract>Numerous proteins are known to be lost following myocardial ischemia/reperfusion yet little is known about the mediating proteinases. This study examines the hypothesis that proteasome plays a significant role in the removal of proteins oxidized during myocardial ischemia. Proteasome was inhibited by perfusing isolated rat hearts with buffer containing lactacystin, 2 μmol/L, for 10 min, which resulted in 51 and 42% decreases in 20S and 26S proteasome activities that persisted for a minimum of 90 min. Lactacystin pretreatment had minor effects on postischemic recovery of isolated hearts exposed to 30 min global ischemia and 60 min reperfusion. Protein carbonyl content of lactacystin-pretreated ischemic hearts was significantly (
P < 0.05) increased. One band with approximate molecular mass of 50 kDa is known to contain oxidized actin. Actin degradation was quantitated by analysis of 3-methylhistidine which was significantly (
P < 0.05) decreased by 15% following 30 min ischemia and 60 min reperfusion. Pretreatment of ischemic hearts with lactacystin prevented much of the loss (−6.5%) of 3-methylhistidine. Probing immunoprecipitated actin with an antibody specific for ubiquitin revealed no bands containing ubiquitinated homologues of this protein. These observations support the conclusion that proteasome mediates removal of some of the proteins oxidized during myocardial ischemia/reperfusion, and that at least oxidized actin is removed by the 20S proteasome.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>16337889</pmid><doi>10.1016/j.freeradbiomed.2005.09.022</doi><tpages>9</tpages></addata></record> |
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| subjects | 3-Methylhistidine Acetylcysteine - analogs & derivatives Acetylcysteine - pharmacology Actin Actins - metabolism Animals Cysteine Proteinase Inhibitors - pharmacology Free radical Heart - physiopathology Immunoprecipitation Ischemic Preconditioning, Myocardial Male Methylhistidines - metabolism Myocardial ischemia Myocardial Ischemia - metabolism Myocardial Ischemia - pathology Oxidation-Reduction Proteasome Proteasome Endopeptidase Complex - metabolism Proteasome Inhibitors Protein oxidation Proteins - metabolism Rats Rats, Sprague-Dawley Reperfusion Ubiquitin - metabolism |
| title | Proteasome mediates removal of proteins oxidized during myocardial ischemia |
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