dc.contributor.author | Reichelt, Melissa E | |
dc.contributor.author | Shanu, Anu | |
dc.contributor.author | Willems, Laura | |
dc.contributor.author | Witting, Paul K | |
dc.contributor.author | Ellis, Natasha A | |
dc.contributor.author | Blackburn, Michael R | |
dc.contributor.author | Headrick, John P | |
dc.date.accessioned | 2017-05-03T11:16:46Z | |
dc.date.available | 2017-05-03T11:16:46Z | |
dc.date.issued | 2009 | |
dc.date.modified | 2010-06-16T05:42:15Z | |
dc.identifier.issn | 1523-0864 | |
dc.identifier.doi | 10.1089/ars.2009.2644 | |
dc.identifier.uri | http://hdl.handle.net/10072/29430 | |
dc.description.abstract | We tested the impact of A1 adenosine receptor (AR) deletion on injury and oxidant damage in mouse hearts subjected to 25 min ischemia/45 min reperfusion (I/R). Wild-type hearts recovered ~50% of contractile function, and released 8.2ᰮ7 IU/g of lactate dehydrogenase (LDH). A1AR deletion worsened dysfunction and LDH efflux (15.2Ხ6 IU/g). Tissue cholesterol and native cholesteryl esters were unchanged, while cholesteryl ester-derived lipid hydroperoxides and hydroxides (CE-O(O)H; a marker of lipid oxidation) increased 3-fold, and a-tocopherylquinone (a-TQ; oxidation product of a-tocopherol (a-TOH)) increased 6-fold. Elevations in a-TQ were augmented 2- to 3-fold by A1AR deletion, whereas CE-O(O)H was unaltered. A1AR deletion also decreased glutathione redox status ([GSH]/[GSSG+GSH]) and enhanced expression of the antioxidant response element heme oxygenase-1 (HO-1) during I/R: 4-fold elevations in HO-1 mRNA and activity were doubled by A1AR deletion. Broad-spectrum AR agonism (10 占2-chloroadenosine; 2-CAD) countered effects of A1AR deletion on oxidant damage, HO-1, and tissue injury, indicating additional ARs (A2A, A2B and/or A3) can mediate similar actions. These data reveal local adenosine engages A1ARs during I/R to selectively limit oxidant damage and enhance outcome. Control of a-TOH/a-TQ levels may contribute to A1AR-dependent cardioprotection. | |
dc.description.peerreviewed | Yes | |
dc.description.publicationstatus | Yes | |
dc.language | English | |
dc.language.iso | eng | |
dc.publisher | Mary Ann Liebert, Inc. | |
dc.publisher.place | United States | |
dc.relation.ispartofstudentpublication | N | |
dc.relation.ispartofpagefrom | 2641 | |
dc.relation.ispartofpageto | 2650 | |
dc.relation.ispartofissue | 11 | |
dc.relation.ispartofjournal | Antioxidants & Redox Signaling | |
dc.relation.ispartofvolume | 11 | |
dc.rights.retention | Y | |
dc.subject.fieldofresearch | Biochemistry and cell biology | |
dc.subject.fieldofresearch | Biochemistry and cell biology not elsewhere classified | |
dc.subject.fieldofresearch | Animal physiology - cell | |
dc.subject.fieldofresearch | Medical biochemistry and metabolomics | |
dc.subject.fieldofresearch | Cardiology (incl. cardiovascular diseases) | |
dc.subject.fieldofresearch | Pharmacology and pharmaceutical sciences | |
dc.subject.fieldofresearchcode | 3101 | |
dc.subject.fieldofresearchcode | 310199 | |
dc.subject.fieldofresearchcode | 310909 | |
dc.subject.fieldofresearchcode | 3205 | |
dc.subject.fieldofresearchcode | 320101 | |
dc.subject.fieldofresearchcode | 3214 | |
dc.title | Endogenous adenosine selectively modulates oxidant stress via the A1 receptor in ischemic hearts | |
dc.type | Journal article | |
dc.type.description | C1 - Articles | |
dc.type.code | C - Journal Articles | |
gro.faculty | Griffith Health, School of Medical Science | |
gro.rights.copyright | © 2009 Mary Ann Liebert, Inc., publishers. Self-archiving of the author-manuscript version is not yet supported by this publisher. Please refer to the journal link for access to the definitive, published version or contact the authors for more information. | |
gro.date.issued | 2009 | |
gro.hasfulltext | No Full Text | |
gro.griffith.author | Headrick, John P. | |