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http://purl.uniprot.org/citations/12177784http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12177784http://www.w3.org/2000/01/rdf-schema#comment"Incubation of human dermal fibroblasts in keratinocyte-conditioned culture medium led to a 5.7-fold increase in the level of matrix metalloproteinase-1. Virtually all of the matrix metalloproteinase-1 - inducing activity could be related to agonists acting through members of the epidermal growth factor receptor family or to agonists acting through the interleukin-1 receptor. The same keratinocyte-conditioned medium also induced a modest increase in fibroblast proliferation (approximately 1.8-fold). Growth-stimulating activity could be attributed to epidermal growth factor receptor (but not interleukin-1 receptor) function. In fibroblasts exposed to keratinocyte-conditioned medium, mitogen-activated protein kinase signalling through both the extracellular signal-related kinase pathway and p38 pathway occurred. When recombinant epidermal growth factor or recombinant interleukin-1beta were used as a control, they induced mitogen-activated protein kinase signalling consistent with the combined effects of epidermal growth factor receptor - specific and interleukin-1 receptor - specific agonists in keratinocyte-conditioned medium. Recombinant epidermal growth factor stimulated both matrix metalloproteinase-1 induction and proliferation while recombinant interleukin-1beta stimulated matrix metalloproteinase-1 elaboration but not fibroblast growth. An inhibitor of extracellular signal-related kinase pathway signalling (U0126) blocked induction of matrix metalloproteinase-1 production induced by keratinocyte-conditioned medium (as well as by epidermal growth factor or interleukin-1beta), and also inhibited proliferation. A p38 signalling inhibitor (SB203580) blocked matrix metalloproteinase-1 elaboration induced by keratinocyte-conditioned medium or interleukin-1beta, but did not inhibit matrix metalloproteinase-1 elaboration or cell growth induced by epidermal growth factor. These data indicate that keratinocyte-fibroblast interactions are mediated by multiple stimulating agents acting on specific receptors to induce signalling through different mitogen-activated protein kinase pathways leading to altered expression of key biological functions."xsd:string
http://purl.uniprot.org/citations/12177784http://purl.org/dc/terms/identifier"doi:10.1038/sj.bjc.6600478"xsd:string
http://purl.uniprot.org/citations/12177784http://purl.uniprot.org/core/author"Varani J."xsd:string
http://purl.uniprot.org/citations/12177784http://purl.uniprot.org/core/author"Bhagavathula N."xsd:string
http://purl.uniprot.org/citations/12177784http://purl.uniprot.org/core/author"Moon S.E."xsd:string
http://purl.uniprot.org/citations/12177784http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12177784http://purl.uniprot.org/core/name"Br J Cancer"xsd:string
http://purl.uniprot.org/citations/12177784http://purl.uniprot.org/core/pages"457-464"xsd:string
http://purl.uniprot.org/citations/12177784http://purl.uniprot.org/core/title"Keratinocyte stimulation of matrix metalloproteinase-1 production and proliferation in fibroblasts: regulation through mitogen-activated protein kinase signalling events."xsd:string
http://purl.uniprot.org/citations/12177784http://purl.uniprot.org/core/volume"87"xsd:string
http://purl.uniprot.org/citations/12177784http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12177784
http://purl.uniprot.org/citations/12177784http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12177784
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http://purl.uniprot.org/uniprot/#_P03956-mappedCitation-12177784http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12177784
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