Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1992-1-3
pubmed:abstractText
Manganese superoxide dismutase (MnSOD) is a nuclear encoded mitochondrial matrix enzyme that functions to scavenge superoxide radicals. The human MnSOD cDNA under the transcriptional control of a human beta-actin promoter was introduced into mouse C3H10T1/2 cells by cotransfection with a recombinant plasmid containing the NeoR selectable marker. C3H10T1/2 transformants (C3H-SOD) were obtained that expressed high levels of authentic enzymatically active human MnSOD. Overexpression of the MnSOD gene did not affect the protein levels of CuZnSOD, catalase (CAT), or glutathione peroxidase (GPX) in the transformants. Treatment of cells with paraquat was less toxic to the C3H-SOD cells than to the control cells. These results are consistent with the possibility that superoxide radicals are mediators of paraquat cytotoxicity.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
293
pubmed:geneSymbol
MnSOD
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
199-203
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Overproduction of human Mn-superoxide dismutase modulates paraquat-mediated toxicity in mammalian cells.
pubmed:affiliation
Department of Radiology, Bowman Gray School of Medicine, Winston-Salem, North Carolina 27103.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't