Linked Life Data

9101240

Source:http://linkedlifedata.com/resource/pubmed/id/9101240

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1997-7-8
pubmed:abstractText
Transfection of a pSV2 human copper-zinc superoxide dismutase expression vector into murine fibroblasts resulted in stable transgenic clones producing increased amounts of copper-zinc superoxide dismutase. Two classes of transfectants were observed and were characterized by the presence or absence of an increase in endogenous glutathione peroxidase activity. In addition, increases and decreases in individual clones in the activities of manganese superoxide dismutase, glutathione reductase, and NADPH-reductase were detected. In general, these alterations in enzyme activity correlated to the cellular glutathione peroxidase/copper-zinc superoxide dismutase ratio. Parameters of cellular physiological functions were also altered, including cell division time, FGF and EGF response, fibronectin content, paraquat resistance, hydrogen peroxide release into media, and sensitivity to radiation. Some of these cellular parameters were also bidirectional and reflected the cellular glutathione peroxidase/copper-zinc superoxide dismutase ratio. Our results indicate that small deviations from the normal physiological copper-zinc superoxide dismutase/seleno-glutathione peroxidase ratios can have pronounced effects on other antioxidant enzymes, growth rate, growth factor response, and expression of proteins normally not associated with oxygen metabolism.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0891-5849
pubmed:author
pubmed:issnType
Print
pubmed:volume
18
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
497-506
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Transfection with human copper-zinc superoxide dismutase induces bidirectional alterations in other antioxidant enzymes, proteins, growth factor response, and paraquat resistance.
pubmed:affiliation
University of California, San Diego 92103-8320, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.