Linked Life Data

8867782

Source:http://linkedlifedata.com/resource/pubmed/id/8867782

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1997-5-1
pubmed:abstractText
Collagenase, a prototypic matrix metalloproteinase, plays a major role in the degradation of the extracellular matrix. The essential amino acid L-tryptophan was recently shown to stimulate the expression of collagenase gene in human dermal fibroblast cultures. In this study, we focused our attention on the mechanisms responsible for activation of collagenase transcription by L-tryptophan. Incubation of fibroblasts with L-tryptophan resulted in a dose- and time-dependent elevation of collagenase and tissue inhibitor of metalloproteinase mRNA levels. The maximum enhancement in collagenae mRNA was approximately 50-fold. This effect was not abolished by cycloheximide, suggesting independence from ongoing protein synthesis. Transient cell transfections with a promoter/reporter gene construct containing 3.8 kb of 5' flanking DNA of the human collagenase gene linked to the chloramphenicol acetyl transferase (CAT) gene or a construct containing three phorbol ester-responsive AP-1 binding sequences (12-O-tetradecanoyl-phorbol-13-acetate-responsive element) in front of the thymidine kinase promoter linked to the CAT gene indicated enhancement of promoter activity by L-tryptophan. Furthermore, electrophoretic DNA mobility shift assays demonstrated enhanced DNA-protein complex formation specific for an AP-1 binding site probe with nuclear extracts prepared from cells incubated with L-tryptophan. These results collectively suggest that activation of collagenase gene expression in dermal fibroblasts by L-tryptophan is mediated through AP-1 binding elements in the collagenase gene promoter that are sufficient for gene response.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0968-8773
pubmed:author
pubmed:issnType
Print
pubmed:volume
41
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
361-8
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:8867782-Binding Sites, pubmed-meshheading:8867782-Cells, Cultured, pubmed-meshheading:8867782-Collagenases, pubmed-meshheading:8867782-Cycloheximide, pubmed-meshheading:8867782-DNA, pubmed-meshheading:8867782-Enzyme Induction, pubmed-meshheading:8867782-Fibroblasts, pubmed-meshheading:8867782-Genes, Reporter, pubmed-meshheading:8867782-Glycoproteins, pubmed-meshheading:8867782-Humans, pubmed-meshheading:8867782-Mercaptoethanol, pubmed-meshheading:8867782-Oxidation-Reduction, pubmed-meshheading:8867782-Promoter Regions, Genetic, pubmed-meshheading:8867782-Protein Synthesis Inhibitors, pubmed-meshheading:8867782-RNA, Messenger, pubmed-meshheading:8867782-Recombinant Fusion Proteins, pubmed-meshheading:8867782-Skin, pubmed-meshheading:8867782-Tissue Inhibitor of Metalloproteinases, pubmed-meshheading:8867782-Transcription, Genetic, pubmed-meshheading:8867782-Transcription Factor AP-1, pubmed-meshheading:8867782-Tryptophan
pubmed:year
1995
pubmed:articleTitle
L-tryptophan induces expression of collagenase gene in human fibroblasts: demonstration of enhanced AP-1 binding and AP-1 binding site-driven promoter activity.
pubmed:affiliation
Department of Medicine, Thomas Jefferson University, Philadelphia, PA 19107-5541, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.