ArticleJournal of molecular neuroscience : MN2012
PYK-2 is tyrosine phosphorylated after activation of pituitary adenylate cyclase activating polypeptide receptors in lung cancer cells.
Article in Journal of molecular neuroscience : MN, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
5 citing papers in PubMed, 39 citations in OpenAlex.
- Integrin αVβ1-activated PYK2 promotes the progression of non-small-cell lung cancer via the STAT3-VGF axis.Cell communication and signaling : CCS · 2024Article
- Automated assembly of molecular mechanisms at scale from text mining and curated databases.Molecular systems biology · 2023Article
- Activated PyK2 and Its Associated Molecules Transduce Cellular Signaling from the Cancerous Milieu for Cancer Metastasis.International journal of molecular sciences · 2022Review
- Gene Expression Data Mining Reveals the Involvement of GPR55 and Its Endogenous Ligands in Immune Response, Cancer, and Differentiation.International journal of molecular sciences · 2021Article
- Molecular mechanisms underlying the Nephroprotective effects of PACAP in diabetes.Journal of molecular neuroscience : MN · 2014Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.