Linked Life Data

1657905

Source:http://linkedlifedata.com/resource/pubmed/id/1657905

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
30
pubmed:dateCreated
1991-12-2
pubmed:abstractText
Interleukin 1 (IL-1) mediates many cellular functions, but the signal transduction mechanisms of its actions are not clearly understood. Here, we have examined the exact participation of cAMP in the IL-1-induced production of the precursors of matrix metalloproteinase (MMPs) and their specific inhibitor, tissue inhibitor of metalloproteinases (TIMP) in human uterine cervical fibroblasts. IL-1 significantly augmented the production of proMMP-1 (vertebrate procollagenase), proMMP-3 (prostromelysin), and TIMP without detectable changes in the intracellular level of cAMP. Dibutyryl cAMP (Bt2cAMP) and the cAMP elevating agent (forskolin) did not replace IL-1 as MMP inducers. On the contrary, the IL-1-mediated induction of proMMP-1 and proMMP-3 was significantly suppressed by treatment of the cells with Bt2cAMP, forskolin, or theophylline. The suppressive effect of Bt2cAMP on the IL-1-induced production of proMMP-1 and -3 was not due to the inhibition of zymogen secretion, but resulted from the decrease in the steady-state levels of proMMP-1 and proMMP-3 mRNAs. In contrast, Bt2cAMP slightly enhanced the IL-1-induced production of TIMP. The synthesis of proMMP-2 (72-kDa progelatinase/type IV procollagenase) was not altered by IL-1 and/or Bt2cAMP. These results suggest, first, that induction of proMMP-1 and -3 synthesis may share similar transduction pathways but they are distinct from those for proMMP-2 and TIMP synthesis and, second, that cAMP does not function as a second messenger in the MMPs' induction upon IL-1 stimulation in human uterine cervical fibroblasts. Thus, it is further suggested that the system that increases the intracellular cAMP level may be involved in negative regulation of proMMP-1 and -3 production.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
266
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
19894-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:1657905-Animals, pubmed-meshheading:1657905-Blotting, Western, pubmed-meshheading:1657905-Bucladesine, pubmed-meshheading:1657905-Cervix Uteri, pubmed-meshheading:1657905-Cyclic AMP, pubmed-meshheading:1657905-Enzyme Precursors, pubmed-meshheading:1657905-Extracellular Matrix, pubmed-meshheading:1657905-Female, pubmed-meshheading:1657905-Fibroblasts, pubmed-meshheading:1657905-Forskolin, pubmed-meshheading:1657905-Glycoproteins, pubmed-meshheading:1657905-Humans, pubmed-meshheading:1657905-Interleukin-1, pubmed-meshheading:1657905-Metalloendopeptidases, pubmed-meshheading:1657905-Rabbits, pubmed-meshheading:1657905-Radioimmunoassay, pubmed-meshheading:1657905-Recombinant Proteins, pubmed-meshheading:1657905-Theophylline, pubmed-meshheading:1657905-Tissue Inhibitor of Metalloproteinases
pubmed:year
1991
pubmed:articleTitle
Cyclic adenosine 3',5'-monophosphate suppresses interleukin 1-induced synthesis of matrix metalloproteinases but not of tissue inhibitor of metalloproteinases in human uterine cervical fibroblasts.
pubmed:affiliation
Department of Biochemistry, Tokyo College of Pharmacy, Japan.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.