Linked Life Data

12868489

Source:http://linkedlifedata.com/resource/pubmed/id/12868489

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2003-7-18
pubmed:abstractText
Phospholipid hydroperoxide glutathione peroxidase (PhGPx) is an antioxidant enzyme that reduces cellular phospholipid hydroperoxides (PLOOHs) to alcohols. Cellular peroxide tone has been implicated in cell growth and differentiation. By reducing the PLOOH level in the cell membrane, PhGPx regulates the peroxide tone and thereby might be involved in cell growth. We hypothesized that overexpression of PhGPx in human breast cancer cells would decrease their growth rate. We stably transfected MCF-7 cells (Wt) with L-PhGPx and measured cell doubling time, plating efficiency, and cell cycle phase transit times. P-4 cells (8-fold increase in PhGPx activity) showed a 2-fold increase in doubling time; doubling time increased directly with PhGPx activity (r = 0.95). The higher the PhGPx activity, the lower the plating efficiency (r = -0.86). The profile of other antioxidant enzymes was unchanged. Overexpression of PhGPx lowered the steady-state level of PLOOH (by > 60%). Results from bromodeoxyuridine pulse-chase experiments and flow cytometry indicate that PhGPx induced a delay in MCF-7 proliferation that was primarily due to a slower progression from G1 to S. These results support the hypothesis that PhGPx plays a regulatory role in the progression of MCF-7 cells from G1 to S possibly by regulating the steady-state levels of PLOOH. These data suggest that PhGPx can lower the peroxide tone, which might change the cellular redox environment resulting in a delay in G1 transit. Thus, PhGPx could be an important factor in cell growth.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1071-5762
pubmed:author
pubmed:issnType
Print
pubmed:volume
37
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
621-30
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:12868489-Antioxidants, pubmed-meshheading:12868489-Blotting, Western, pubmed-meshheading:12868489-Bromodeoxyuridine, pubmed-meshheading:12868489-Catalase, pubmed-meshheading:12868489-Cell Cycle, pubmed-meshheading:12868489-Cell Differentiation, pubmed-meshheading:12868489-Cell Line, Tumor, pubmed-meshheading:12868489-Flow Cytometry, pubmed-meshheading:12868489-G1 Phase, pubmed-meshheading:12868489-Glutathione, pubmed-meshheading:12868489-Glutathione Peroxidase, pubmed-meshheading:12868489-Glutathione Reductase, pubmed-meshheading:12868489-Humans, pubmed-meshheading:12868489-Immunoblotting, pubmed-meshheading:12868489-Lipid Metabolism, pubmed-meshheading:12868489-Lipid Peroxides, pubmed-meshheading:12868489-Models, Chemical, pubmed-meshheading:12868489-Oxidation-Reduction, pubmed-meshheading:12868489-Protein Biosynthesis, pubmed-meshheading:12868489-Superoxide Dismutase, pubmed-meshheading:12868489-Time Factors, pubmed-meshheading:12868489-Transfection
pubmed:year
2003
pubmed:articleTitle
Phospholipid hydroperoxide glutathione peroxidase induces a delay in G1 of the cell cycle.
pubmed:affiliation
Free Radical and Radiation Biology and The Holden Comprehensive Cancer Center, The University of Iowa, Iowa City, IA 52242-1101, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.