Linked Life Data

2732003

Source:http://linkedlifedata.com/resource/pubmed/id/2732003

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1989-7-20
pubmed:abstractText
Variations in catalase, glutathione peroxidase (GP) and adenylate cyclase (AC) activity in murine erythroleukemic (MEL) cells were studied during multiplication and dimethylsulfoxide (DMSO)-induced differentiation. The results demonstrated that, although DMSO favors the incorporation of 3H-thymidine into DNA of treated cells, it slows down cell multiplication. Increased incorporation was also observed in superoxide dismutase (SOD)-treated cells. DMSO also determined an early and significant drop in AC activity and a late fall in catalase activity, whereas there was no significant variation in GP activity in parallel with the decreased cell multiplication that accompanied cell differentiation. We hypothesize that DMSO and SOD favor 3H-thymidine incorporation by neutralizing the reactive forms of oxygen and that the reduction in catalase and AC activity is closely related to the mitotic activity of MEL cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0020-7136
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
43
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1145-8
pubmed:dateRevised
2007-7-24
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Effects of dimethylsulfoxide on Friend erythroleukemic cell proliferation and on the activity of enzymes involved in this process.
pubmed:affiliation
Institute of General Pathology, University of Perugia, Italy.
pubmed:publicationType
Journal Article, Comparative Study