Linked Life Data

15816840

Source:http://linkedlifedata.com/resource/pubmed/id/15816840

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2005-4-8
pubmed:abstractText
When human cells sustain a DNA double-strand break (dsb), histone H2AX in chromatin surrounding the DNA break is phosphorylated, marking repair foci. The number of phosphorylated histone H2AX (gammaH2AX) foci approximates the number of dsb present in the cell's nuclear DNA. We observed 0.4 gammaH2AX foci per nucleus in primary human melanocytes. In contrast, in four melanoma cell lines, we detected 7-17 gammaH2AX foci per nucleus, a 17-42 times increase in the basal level of gammaH2AX foci in melanoma cells relative to melanocytes (MC). Thus, untreated melanoma cells express significantly greater numbers of gammaH2AX foci than do untreated MC. Detection and rejoining of ionizing radiation-induced DNA dsb proceeded as rapidly in melanoma cells as in MC. Melanoma cells, however, reduced the number of radiation-induced gammaH2AX foci down only to pre-irradiation levels. Co-localization of the majority of gammaH2AX foci with ataxia telangiectasia mutated, BRCA1, 53BP1, and Nbs1 foci in untreated melanoma cells indicated that the additional foci in melanoma cells were associated with a DNA change that the cells interpret as DNA dsb. Co-localization of gammaH2AX foci with the telomere replication factor 1 protein in untreated melanoma cells indicates that the additional foci in untreated melanoma cells are associated with dysfunctional telomeres that induce a DNA damage stress response.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0022-202X
pubmed:author
pubmed:issnType
Print
pubmed:volume
124
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
807-17
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Melanoma cells express elevated levels of phosphorylated histone H2AX foci.
pubmed:affiliation
Department of Radiation Oncology, University of Utah Health Sciences Center, Salt Lake City, Utah 85132, USA. ray.warters@hsc.utah.edu
pubmed:publicationType
Journal Article, In Vitro, 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