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http://purl.uniprot.org/citations/22581436http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22581436http://www.w3.org/2000/01/rdf-schema#comment"The signal transduction mechanisms of pituitary adenylate cyclase activating polypeptide (PACAP) were investigated in lung cancer cells. Previously, PACAP-27 addition to NCI-H838 cells increased phosphatidylinositol turnover and intracellular cAMP leading to proliferation of lung cancer cells. Also, PACAP receptors (PAC1) regulated the tyrosine phosphorylation of ERK, focal adhesion kinase, and paxillin. In this communication, the effects of PACAP on cytosolic Ca(2+) and PYK-2 tyrosine phosphorylation were investigated. PACAP-27 increased cytosolic Ca(2+) within seconds after addition to FURA-2 AM loaded NCI-H838 cells. The increase in cytosolic Ca(2+) caused by PACAP was inhibited by PACAP(6-38) (PAC1 antagonist), U73122 (phospholipase C inhibitor), or BAPTA (calcium chelator), but not H89 (PKA inhibitor). PACAP-38, but not vasoactive intestinal peptide (VIP), addition to NCI-H838 or H1299 cells significantly increased the tyrosine phosphorylation of PYK-2 after 2 min. The increase in PYK-2 tyrosine phosphorylation caused by PACAP was inhibited by PACAP(6-38), U73122, or BAPTA, but not H89. The results suggest that PAC1 regulates PYK-2 tyrosine phosphorylation in a calcium-dependent manner."xsd:string
http://purl.uniprot.org/citations/22581436http://purl.org/dc/terms/identifier"doi:10.1007/s12031-012-9785-6"xsd:string
http://purl.uniprot.org/citations/22581436http://purl.uniprot.org/core/author"Jensen R.T."xsd:string
http://purl.uniprot.org/citations/22581436http://purl.uniprot.org/core/author"Moody T.W."xsd:string
http://purl.uniprot.org/citations/22581436http://purl.uniprot.org/core/author"Di Florio A."xsd:string
http://purl.uniprot.org/citations/22581436http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22581436http://purl.uniprot.org/core/name"J Mol Neurosci"xsd:string
http://purl.uniprot.org/citations/22581436http://purl.uniprot.org/core/pages"660-666"xsd:string
http://purl.uniprot.org/citations/22581436http://purl.uniprot.org/core/title"PYK-2 is tyrosine phosphorylated after activation of pituitary adenylate cyclase activating polypeptide receptors in lung cancer cells."xsd:string
http://purl.uniprot.org/citations/22581436http://purl.uniprot.org/core/volume"48"xsd:string
http://purl.uniprot.org/citations/22581436http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/22581436
http://purl.uniprot.org/citations/22581436http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/22581436
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http://purl.uniprot.org/uniprot/#_P41586-mappedCitation-22581436http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22581436
http://purl.uniprot.org/uniprot/#_P18509-mappedCitation-22581436http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22581436
http://purl.uniprot.org/uniprot/#_Q53BH1-mappedCitation-22581436http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22581436
http://purl.uniprot.org/uniprot/#_Q53BH6-mappedCitation-22581436http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22581436
http://purl.uniprot.org/uniprot/#_Q14289-mappedCitation-22581436http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22581436
http://purl.uniprot.org/uniprot/#_Q6ZRA8-mappedCitation-22581436http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22581436
http://purl.uniprot.org/uniprot/#_Q59GM4-mappedCitation-22581436http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22581436
http://purl.uniprot.org/uniprot/#_Q6RKA2-mappedCitation-22581436http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22581436