| pubmed-article:8135806 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8135806 | lifeskim:mentions | umls-concept:C0034693 | lld:lifeskim |
| pubmed-article:8135806 | lifeskim:mentions | umls-concept:C0227525 | lld:lifeskim |
| pubmed-article:8135806 | lifeskim:mentions | umls-concept:C1518440 | lld:lifeskim |
| pubmed-article:8135806 | lifeskim:mentions | umls-concept:C0256926 | lld:lifeskim |
| pubmed-article:8135806 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:8135806 | pubmed:dateCreated | 1994-4-21 | lld:pubmed |
| pubmed-article:8135806 | pubmed:abstractText | Immunocytochemical studies have revealed that one of the major heat shock proteins, HSP72, is induced in livers of rats that have been pretreated with phenobarbital and then administered halothane in a hypoxic gas mixture of 10% oxygen. To determine the sub-cellular localization of HSP72 in the livers of these rats 24 hr after halothane administration, cytoplasmic and nuclear fractions were prepared and separated by PAGE electrophoresis. Western blotting with a mouse monoclonal anti-HSP70 IgG antibody, which recognizes both the constitutive (HSP73) and inducible (HSP72) forms, revealed that HSP72 was induced and translocated into the nucleus in only those rats exposed to halothane under hypoxia following phenobarbital pretreatment. Nuclear translocation of HSP72 under the latter conditions was confirmed by immunocytochemical staining using gold-conjugated secondary antibodies followed by digital laser microscopy with Nomarski optics. Neither phenobarbital pretreatment alone nor phenobarbital plus hypoxia treatment induced HSP72. No alteration in amount of HSP73 was observed under any of these conditions. | lld:pubmed |
| pubmed-article:8135806 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8135806 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8135806 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8135806 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8135806 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8135806 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8135806 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8135806 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8135806 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8135806 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:8135806 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:8135806 | pubmed:author | pubmed-author:Van DykeR ARA | lld:pubmed |
| pubmed-article:8135806 | pubmed:author | pubmed-author:TrudellJ RJR | lld:pubmed |
| pubmed-article:8135806 | pubmed:author | pubmed-author:MarshH MHM | lld:pubmed |
| pubmed-article:8135806 | pubmed:author | pubmed-author:LiuW JWJ | lld:pubmed |
| pubmed-article:8135806 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8135806 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:8135806 | pubmed:volume | 199 | lld:pubmed |
| pubmed-article:8135806 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8135806 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8135806 | pubmed:pagination | 647-52 | lld:pubmed |
| pubmed-article:8135806 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:8135806 | pubmed:meshHeading | pubmed-meshheading:8135806-... | lld:pubmed |
| pubmed-article:8135806 | pubmed:meshHeading | pubmed-meshheading:8135806-... | lld:pubmed |
| pubmed-article:8135806 | pubmed:meshHeading | pubmed-meshheading:8135806-... | lld:pubmed |
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| pubmed-article:8135806 | pubmed:meshHeading | pubmed-meshheading:8135806-... | lld:pubmed |
| pubmed-article:8135806 | pubmed:meshHeading | pubmed-meshheading:8135806-... | lld:pubmed |
| pubmed-article:8135806 | pubmed:meshHeading | pubmed-meshheading:8135806-... | lld:pubmed |
| pubmed-article:8135806 | pubmed:meshHeading | pubmed-meshheading:8135806-... | lld:pubmed |
| pubmed-article:8135806 | pubmed:meshHeading | pubmed-meshheading:8135806-... | lld:pubmed |
| pubmed-article:8135806 | pubmed:meshHeading | pubmed-meshheading:8135806-... | lld:pubmed |
| pubmed-article:8135806 | pubmed:meshHeading | pubmed-meshheading:8135806-... | lld:pubmed |
| pubmed-article:8135806 | pubmed:meshHeading | pubmed-meshheading:8135806-... | lld:pubmed |
| pubmed-article:8135806 | pubmed:meshHeading | pubmed-meshheading:8135806-... | lld:pubmed |
| pubmed-article:8135806 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:8135806 | pubmed:articleTitle | Nuclear translocation of heat shock protein 72 in liver cells of halothane-exposed rats. | lld:pubmed |
| pubmed-article:8135806 | pubmed:affiliation | Department of Anesthesia, Stanford School of Medicine, CA 94305-5117. | lld:pubmed |
| pubmed-article:8135806 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8135806 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8135806 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
