Linked Life Data

1898036

Source:http://linkedlifedata.com/resource/pubmed/id/1898036

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1991-10-24
pubmed:abstractText
Chinese hamster ovary cells cultured in vitro were used to assess the role of glutathione metabolism in the induction of the 32-kDa stress protein. Enhanced synthesis of the 32-kDa protein was observed after cells were incubated with CdCl2 or diethylmaleate and protein was subjected to SDS-PAGE followed by fluorography. Concomitantly, in both cell preparations an increase in heme oxygenase activity was observed. Proteins from CdCl2- and diethylmaleate-treated cells were subjected to Western blotting and protein crossreacting with either rabbit antibody to rat liver heme oxygenase-1 (32,000 Mr) or rat testis heme oxygenase-2 (36,000 Mr) quantitated. The analysis indicated that the CdCl2 treatment increased the intensity of the HO-1 band 5.5-fold while the diethylmaleate treatment increased it three-fold relative to control. Neither treatment affected the intensity of HO-2 antibody binding. Incubation of cells with buthionine sulfoximine, under conditions which resulted in greater than or equal to 90% of the intracellular glutathione being depleted, enhanced synthesis of a 32-kDa protein when assayed by SDS-PAGE. This protein exhibited a Mr similar to the 32-kDa protein induced by either CdCl2 or diethylmaleate treatment. Proteins from buthionine sulfoximine and diethylmaleate-treated cells were mixed together and subjected to 2D PAGE. The resulting fluorograph demonstrated that both treatments produced identical patterns. In contrast, incubation of cells in diamide, a thiol oxidizing compound, resulted in enhanced synthesis of the 110-, 90-, and 73-kDa heat shock proteins but not the 32-kDa protein. The data presented have shown that depletion of glutathione by two independent methods, conjugation and inhibition of synthesis, enhances the synthesis of a 32-kDa protein identified as heme oxygenase-1; oxidation of glutathione, on the other hand did not. We interpret this to indicate that glutathione depletion rather than conjugation or oxidation represents one pathway for induction of heme oxygenase-1.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0003-9861
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
288
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
368-73
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:1898036-Animals, pubmed-meshheading:1898036-Antimetabolites, pubmed-meshheading:1898036-Blotting, Western, pubmed-meshheading:1898036-Buthionine Sulfoximine, pubmed-meshheading:1898036-Cadmium, pubmed-meshheading:1898036-Cadmium Chloride, pubmed-meshheading:1898036-Cell Line, pubmed-meshheading:1898036-Cricetinae, pubmed-meshheading:1898036-Cricetulus, pubmed-meshheading:1898036-Electrophoresis, Gel, Two-Dimensional, pubmed-meshheading:1898036-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:1898036-Female, pubmed-meshheading:1898036-Glutathione, pubmed-meshheading:1898036-Heat-Shock Proteins, pubmed-meshheading:1898036-Heme Oxygenase (Decyclizing), pubmed-meshheading:1898036-Kinetics, pubmed-meshheading:1898036-Maleates, pubmed-meshheading:1898036-Methionine Sulfoximine, pubmed-meshheading:1898036-Molecular Weight, pubmed-meshheading:1898036-Ovary
pubmed:year
1991
pubmed:articleTitle
Enhancement of heme oxygenase-1 synthesis by glutathione depletion in Chinese hamster ovary cells.
pubmed:affiliation
Vanderbilt Center for Radiation Oncology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.