Linked Life Data

16493055

Source:http://linkedlifedata.com/resource/pubmed/id/16493055

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2006-2-22
pubmed:abstractText
Although the neuropeptide pituitary adenylate cyclase-activating polypeptide (PACAP) has been implicated in the regulation of several immune responses, its target receptors and signaling mechanisms have yet to be fully elucidated in immune cells. In this study, we found that PACAP27, but not PACAP38, specifically stimulated intracellular calcium mobilization and ERK phosphorylation in human neutrophils. Moreover, formyl peptide receptor-like 1 (FPRL1) was identified as a PACAP27 receptor, and PACAP27 was found to selectively stimulate intracellular calcium increase in FPRL1-transfected rat basophil leukocytes-2H3 cell lines. In addition, PACAP27-induced calcium increase and ERK phosphorylation were specifically inhibited by an FPRL1 antagonist, Trp-Arg-Trp-Trp-Trp-Trp (WRW4), thus supporting the notion that PACAP27 acts on FPRL1. In terms of the functional role of PACAP27, we found that the peptide stimulated CD11b surface up-regulation and neutrophil chemotactic migration, and that these responses were completely inhibited by WRW4. The interaction between PACAP27 and FPRL1 was analyzed further using truncated PACAPs and chimeric PACAPs using vasoactive intestinal peptide, and the C-terminal region of PACAP27 was found to perform a vital function in the activation of FPRL1. Taken together, our study suggests that PACAP27 activates phagocytes via FPRL1 activation, and that this results in proinflammatory behavior, involving chemotaxis and the up-regulation of CD11b.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0022-1767
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
176
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2969-75
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:16493055-Amino Acid Sequence, pubmed-meshheading:16493055-Animals, pubmed-meshheading:16493055-Antigens, CD11b, pubmed-meshheading:16493055-Cell Line, Tumor, pubmed-meshheading:16493055-Extracellular Signal-Regulated MAP Kinases, pubmed-meshheading:16493055-Humans, pubmed-meshheading:16493055-Ligands, pubmed-meshheading:16493055-Molecular Sequence Data, pubmed-meshheading:16493055-Neutrophil Activation, pubmed-meshheading:16493055-Neutrophils, pubmed-meshheading:16493055-Pituitary Adenylate Cyclase-Activating Polypeptide, pubmed-meshheading:16493055-Protein Isoforms, pubmed-meshheading:16493055-Rats, pubmed-meshheading:16493055-Receptors, Formyl Peptide, pubmed-meshheading:16493055-Receptors, Lipoxin, pubmed-meshheading:16493055-Signal Transduction, pubmed-meshheading:16493055-Up-Regulation
pubmed:year
2006
pubmed:articleTitle
Pituitary adenylate cyclase-activating polypeptide 27 is a functional ligand for formyl peptide receptor-like 1.
pubmed:affiliation
Division of Molecular and Life Sciences, Pohang University of Science and Technology, Pohang, Korea.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't