| pubmed-article:9755062 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9755062 | lifeskim:mentions | umls-concept:C1704336 | lld:lifeskim |
| pubmed-article:9755062 | lifeskim:mentions | umls-concept:C0538674 | lld:lifeskim |
| pubmed-article:9755062 | lifeskim:mentions | umls-concept:C0037533 | lld:lifeskim |
| pubmed-article:9755062 | lifeskim:mentions | umls-concept:C0018988 | lld:lifeskim |
| pubmed-article:9755062 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
| pubmed-article:9755062 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:9755062 | lifeskim:mentions | umls-concept:C0182953 | lld:lifeskim |
| pubmed-article:9755062 | pubmed:issue | 4 Pt 1 | lld:pubmed |
| pubmed-article:9755062 | pubmed:dateCreated | 1998-11-23 | lld:pubmed |
| pubmed-article:9755062 | pubmed:abstractText | The heat shock protein heme oxygenase-1 (HO-1) is regulated by a variety of physiological and pharmacological factors. In skeletal muscle tissue, HO-1 has been shown to be induced only by exercise and electrical stimulation in vivo. Both hemin and sodium nitroprusside (SNP) are potent inducers of HO-1 in other tissues. In this study, we examined the effects of these two agents on HO-1 induction in L6.G8 rat skeletal myoblast cells. Hemin and SNP increased cellular heme oxygenase activity in both a time- and concentration-dependent manner. Increases in the HO-1 mRNA level and protein expression accompanied changes in heme oxygenase activity. The ability of SNP to induce HO-1 in L6.G8 cells was reduced by coincubation with hydroxocobalamin, a known nitric oxide (NO) scavenger, suggesting that NO itself may be involved in HO-1 gene stimulation. These results indicate that HO-1 expression is sensitive to both hemin and SNP in skeletal myoblast cells and may indicate an important regulatory mechanism of heme catabolism in skeletal muscle tissue. | lld:pubmed |
| pubmed-article:9755062 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9755062 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9755062 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9755062 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9755062 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9755062 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9755062 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9755062 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9755062 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9755062 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9755062 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9755062 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:9755062 | pubmed:issn | 0002-9513 | lld:pubmed |
| pubmed-article:9755062 | pubmed:author | pubmed-author:GreenC JCJ | lld:pubmed |
| pubmed-article:9755062 | pubmed:author | pubmed-author:ClarkJ EJE | lld:pubmed |
| pubmed-article:9755062 | pubmed:author | pubmed-author:MotterliniRR | lld:pubmed |
| pubmed-article:9755062 | pubmed:author | pubmed-author:ForestiRR | lld:pubmed |
| pubmed-article:9755062 | pubmed:author | pubmed-author:VeselyM JMJ | lld:pubmed |
| pubmed-article:9755062 | pubmed:author | pubmed-author:ExonD JDJ | lld:pubmed |
| pubmed-article:9755062 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9755062 | pubmed:volume | 275 | lld:pubmed |
| pubmed-article:9755062 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9755062 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9755062 | pubmed:pagination | C1087-94 | lld:pubmed |
| pubmed-article:9755062 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:9755062 | pubmed:meshHeading | pubmed-meshheading:9755062-... | lld:pubmed |
| pubmed-article:9755062 | pubmed:meshHeading | pubmed-meshheading:9755062-... | lld:pubmed |
| pubmed-article:9755062 | pubmed:meshHeading | pubmed-meshheading:9755062-... | lld:pubmed |
| pubmed-article:9755062 | pubmed:meshHeading | pubmed-meshheading:9755062-... | lld:pubmed |
| pubmed-article:9755062 | pubmed:meshHeading | pubmed-meshheading:9755062-... | lld:pubmed |
| pubmed-article:9755062 | pubmed:meshHeading | pubmed-meshheading:9755062-... | lld:pubmed |
| pubmed-article:9755062 | pubmed:meshHeading | pubmed-meshheading:9755062-... | lld:pubmed |
| pubmed-article:9755062 | pubmed:meshHeading | pubmed-meshheading:9755062-... | lld:pubmed |
| pubmed-article:9755062 | pubmed:meshHeading | pubmed-meshheading:9755062-... | lld:pubmed |
| pubmed-article:9755062 | pubmed:meshHeading | pubmed-meshheading:9755062-... | lld:pubmed |
| pubmed-article:9755062 | pubmed:meshHeading | pubmed-meshheading:9755062-... | lld:pubmed |
| pubmed-article:9755062 | pubmed:meshHeading | pubmed-meshheading:9755062-... | lld:pubmed |
| pubmed-article:9755062 | pubmed:meshHeading | pubmed-meshheading:9755062-... | lld:pubmed |
| pubmed-article:9755062 | pubmed:meshHeading | pubmed-meshheading:9755062-... | lld:pubmed |
| pubmed-article:9755062 | pubmed:meshHeading | pubmed-meshheading:9755062-... | lld:pubmed |
| pubmed-article:9755062 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9755062 | pubmed:articleTitle | Heme oxygenase-1 induction in skeletal muscle cells: hemin and sodium nitroprusside are regulators in vitro. | lld:pubmed |
| pubmed-article:9755062 | pubmed:affiliation | Vascular Biology Unit, Department of Surgical Research, Northwick Park Institute for Medical Research, Harrow, Middlesex, HA1 3UJ, United Kingdom. | lld:pubmed |
| pubmed-article:9755062 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9755062 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9755062 | lld:pubmed |
