Linked Life Data

12810669

Source:http://linkedlifedata.com/resource/pubmed/id/12810669

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2003-6-17
pubmed:abstractText
A role for allelic variation within the gene for the antioxidant selenoprotein glutathione peroxidase 1 (GPx-1) in the risk or etiology of breast cancer was investigated. By analyzing the frequency of a polymorphism within the GPx-1 gene resulting in a leucine or proline at codon 198, it was determined that the leucine-containing allele was more frequently associated with breast cancer than the proline-containing allele (odds ratio = 1.9; P < 0.05). However, the heterozygosity index for this polymorphism was lower in the breast cancer samples. To determine whether this was because of the loss of heterozygosity (LOH) during tumor development, another polymorphic marker within GPx-1, which is frequently heterozygous in the human population, was analyzed. These studies indicated that LOH at this locus is a frequent event, occurring in approximately 36% of the breast tumor DNAs analyzed. The consequences of the identity of the amino acid at position 198 were investigated by engineering breast carcinoma cells that exclusively express either the leucine- or proline-containing GPx-1 allele and studying the response to increasing concentrations of selenium. These studies indicated that the leucine-containing allele was less responsive to the stimulation of GPx-1 enzyme activity observed during selenium supplementation than the allele differing only by a proline at that position. These studies support a role for GPx-1 allelic identity and LOH as factors of significance to breast cancer development.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0008-5472
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
63
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3347-51
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:12810669-Adenocarcinoma, pubmed-meshheading:12810669-Alanine, pubmed-meshheading:12810669-Alleles, pubmed-meshheading:12810669-Amino Acid Substitution, pubmed-meshheading:12810669-Breast Neoplasms, pubmed-meshheading:12810669-Codon, pubmed-meshheading:12810669-DNA, Neoplasm, pubmed-meshheading:12810669-Enzyme Induction, pubmed-meshheading:12810669-Gene Expression Regulation, Neoplastic, pubmed-meshheading:12810669-Gene Frequency, pubmed-meshheading:12810669-Genetic Predisposition to Disease, pubmed-meshheading:12810669-Genotype, pubmed-meshheading:12810669-Glutathione Peroxidase, pubmed-meshheading:12810669-Leucine, pubmed-meshheading:12810669-Loss of Heterozygosity, pubmed-meshheading:12810669-Neoplasm Proteins, pubmed-meshheading:12810669-Polymorphism, Genetic, pubmed-meshheading:12810669-Proline, pubmed-meshheading:12810669-Recombinant Fusion Proteins, pubmed-meshheading:12810669-Repetitive Sequences, Amino Acid, pubmed-meshheading:12810669-Selenium, pubmed-meshheading:12810669-Structure-Activity Relationship, pubmed-meshheading:12810669-Tumor Cells, Cultured
pubmed:year
2003
pubmed:articleTitle
Role of glutathione peroxidase 1 in breast cancer: loss of heterozygosity and allelic differences in the response to selenium.
pubmed:affiliation
Department of Human Nutrition, University of Illinois at Chicago, Chicago, Illinois 60612, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't