Linked Life Data

6861745

Source:http://linkedlifedata.com/resource/pubmed/id/6861745

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1983-8-11
pubmed:abstractText
Recent evidence has indicated a role for the acetyl derivatives of polyamines, particularly N8-monoacetylspermidine, as activators of L-ornithine decarboxylase in rat hepatoma tissue culture (HTC) cells. This is in contrast with the well-described negative regulatory control of ornithine decarboxylase exerted by their non-acetylated counterparts. Because of the possibility of a rapid extracellular and intracellular catabolism of the acetyl derivatives of polyamines, the metabolism of N8-monoacetylspermidine and its effect on HTC cell ornithine decarboxylase have been investigated, under conditions which eliminate its extracellular catabolism. Differing from previous reports, we demonstrate that N8-monoacetylspermidine does not elevate ornithine decarboxylase activity when added at low concentrations to the culture medium of HTC cells. Higher concentrations decrease ornithine decarboxylase activity in a dose-dependent manner. This effect cannot be unambiguously attributed to the effect of the acetyl derivative itself, because of the presence in situ of a very active N8-monoacetylspermidine deacetylase, which generates spermidine intracellularly.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
133
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
613-6
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Metabolism of N8-monoacetylspermidine in rat hepatoma cells. Investigation of its effect on the activity of L-ornithine decarboxylase.
pubmed:publicationType
Journal Article