Linked Life Data

7663427

Source:http://linkedlifedata.com/resource/pubmed/id/7663427

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1995-10-12
pubmed:abstractText
NF-kappa B transcription factor regulates a wide variety of cellular and viral genes including the human immunodeficiency virus type 1. Here, we demonstrate that dihydrolipoate/alpha-lipoate redox couple which is a cofactor for mitochondrial dehydrogenases reactions, influences the DNA binding activity of NF-kappa B. The elimination of dithiothreitol in the electrophoretic mobility shift assay protocol resulted in the inability to detect DNA binding activity of activated NF-kappa B. The DNA binding activity was restored by the addition of dihydrolipoate in the binding reaction mixture. Inhibition of NF-kappa B DNA binding activity by in vitro exposure to a sulfhydryl oxidizing agent, diamide was also blocked by dihydrolipoate. In contrast, the addition of the oxidized form, alpha-lipoate inhibited the NF-kappa B DNA binding activity. Coincidentally, preincubation of Jurkat cells with dihydrolipoate potentiated and alpha-lipoate inhibited the okadaic acid-induced NF-kappa B activation as detected by assessing its DNA binding activity. These results suggest the redox exchange between lipoate and NF-kappa B molecules. Furthermore, since the inhibition of AP-1 DNA binding activity by diamide was also blocked by dihydrolipoate, this natural reductant may participate in the redox regulation of transcription factors by enhancing the DNA-protein interactions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1039-9712
pubmed:author
pubmed:issnType
Print
pubmed:volume
36
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
241-6
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Redox regulation of NF-kappa B DNA binding activity by dihydrolipoate.
pubmed:affiliation
Department of Molecular & Cell Biology, University of California, Berkeley 94720, USA.
pubmed:publicationType
Journal Article