Linked Life Data

8020578

Source:http://linkedlifedata.com/resource/pubmed/id/8020578

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1994-8-1
pubmed:abstractText
We have used pulsed-field gel electrophoresis and electron microscopy to correlate stages of DNA fragmentation with alterations of nuclear structure during apoptosis. DNA fragmentation occurs in two stages. The first is initiated by a previously undescribed endonucleolytic activity that cleaves DNA into 50- to 300-kb fragments. Electron microscopy showed that this degree of cleavage was sufficient to cause the chromatin to undergo condensation. The second stage of fragmentation is catalyzed by the previously described calcium-magnesium endonuclease. The enzyme activity responsible for the initial fragmentation of DNA was found to be distinct from that causing subsequent internucleosomal DNA cleavage based upon its cation requirements, independence of proteolysis and lack of inhibition by zinc. Both activities were found to preexist in nuclei from thymocytes, liver, HL60, and IL2-dependent CTLL cells. Thus, in apoptosis DNA degradation involves two distinct endonucleolytic activities, with only the first activity being essential for cell death.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0014-4827
pubmed:author
pubmed:issnType
Print
pubmed:volume
213
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
100-6
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Endonuclease activities associated with high molecular weight and internucleosomal DNA fragmentation in apoptosis.
pubmed:affiliation
Institute for Biological Sciences, National Research Council of Canada, Ottawa, Ontario.
pubmed:publicationType
Journal Article