http://purl.uniprot.org/citations/15004180 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/15004180 | http://www.w3.org/2000/01/rdf-schema#comment | "LL-37 is a cationic peptide that is found in the granules of neutrophils and is secreted by epithelial cells from a variety of tissues. Levels of LL-37 in vivo increase upon infection, and its production and secretion are increased upon stimulation with proinflammatory mediators. It has been postulated that LL-37 modulates the immune response by interacting with the effector cells of innate immunity; however, the mechanism of this interaction is unknown. LL-37 induced phosphorylation and activation of the mitogen-activated protein kinases, extracellular signal-regulated kinase 1/2 (ERK1/2) and p38, in human peripheral blood-derived monocytes and a human bronchial epithelial cell line, but not in B or T lymphocytes. Phosphorylation was not dependent on the G protein-coupled formyl peptide-like receptor 1, which was previously proposed to be the receptor for LL-37-induced chemotaxis on human monocytes and T cells. Activation of ERK1/2 and p38 was markedly increased by the presence of GM-CSF, but not M-CSF. Exposure to LL-37 also led to the activation of Elk-1, a transcription factor that is downstream of and activated by phosphorylated ERK1/2, the up-regulation of various Elk-1-controlled genes, and the transcription and secretion of IL-8. Inhibition of either p38 or ERK1/2 kinases led to a reduction in LL-37-induced IL-8 secretion and inhibition of the transcription of various chemokine genes. The ability of LL-37 to signal through these pathways has broad implications in immunity, monocyte activation, proliferation, and differentiation."xsd:string |
http://purl.uniprot.org/citations/15004180 | http://purl.org/dc/terms/identifier | "doi:10.4049/jimmunol.172.6.3758"xsd:string |
http://purl.uniprot.org/citations/15004180 | http://purl.uniprot.org/core/author | "Hancock R.E."xsd:string |
http://purl.uniprot.org/citations/15004180 | http://purl.uniprot.org/core/author | "Speert D.P."xsd:string |
http://purl.uniprot.org/citations/15004180 | http://purl.uniprot.org/core/author | "Davidson D.J."xsd:string |
http://purl.uniprot.org/citations/15004180 | http://purl.uniprot.org/core/author | "Bowdish D.M."xsd:string |
http://purl.uniprot.org/citations/15004180 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
http://purl.uniprot.org/citations/15004180 | http://purl.uniprot.org/core/name | "J Immunol"xsd:string |
http://purl.uniprot.org/citations/15004180 | http://purl.uniprot.org/core/pages | "3758-3765"xsd:string |
http://purl.uniprot.org/citations/15004180 | http://purl.uniprot.org/core/title | "The human cationic peptide LL-37 induces activation of the extracellular signal-regulated kinase and p38 kinase pathways in primary human monocytes."xsd:string |
http://purl.uniprot.org/citations/15004180 | http://purl.uniprot.org/core/volume | "172"xsd:string |
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