ArticlePflugers Archiv : European journal of physiology2008
Activation of cell migration with fibroblast growth factor-2 requires calcium-sensitive potassium channels.
Article in Pflugers Archiv : European journal of physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 23 citations in OpenAlex.
- Cancer as a Channelopathy-Appreciation of Complimentary Pathways Provides a Different Perspective for Developing Treatments.Cancers · 2022Review
- Ion channels or aquaporins as novel molecular targets in gastric cancer.Molecular cancer · 2017Review
- Physiological impact of abnormal lipoxin A₄ production on cystic fibrosis airway epithelium and therapeutic potential.BioMed research international · 2015Review
- Ion channels and apoptosis in cancer.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2014Review
- Evidence of K+ channel function in epithelial cell migration, proliferation, and repair.American journal of physiology. Cell physiology · 2014Review
- FGF23 promotes renal calcium reabsorption through the TRPV5 channel.The EMBO journal · 2014Article
- The role of Lipoxin A4 in Cystic Fibrosis Lung Disease.Computational and structural biotechnology journal · 2013Review
- Chemotaxis of MDCK-F cells toward fibroblast growth factor-2 depends on transient receptor potential canonical channel 1.Pflugers Archiv : European journal of physiology · 2011Article
- Mechanosensitive Ca(2+) permeant cation channels in human prostate tumor cells.Channels (Austin, Tex.)Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tumor cell migration is crucial for the formation of tumor metastases and the progression of tumor disease. Fibroblast growth factor-2 (FGF-2) is one of the cytokines involved in the autocrine stimulation of tumor development. FGF-2 also stimulates transcription of Ca(2+)-sensitive K(+) channels (IK1 or K(Ca)3.1), which are part of the migration machinery in many cell types. Here, we tested whether FGF-2 acutely stimulates migration of transformed MDCK cells in a K(Ca)3.1 channel-dependent way. FGF-2 accelerates migration dose dependently. The speed of migration increases almost instantaneously. After 2 min, ERK1/2 phosphorylation has almost doubled. FGF-2 does not stimulate migration when ERK1/2 phosphorylation is inhibited. K(Ca)3.1 channel blockade also prevents the stimulatory effect of FGF-2 on cell migration. In addition, FGF-2 treatment leads to an activation of K(Ca)3.1 channels and a rapid rise of the cell area, which is because of an elevated rate of exocytosis. However, the amount of K(Ca)3.1 channels within the plasma membrane does not change. Our results show that there is a reciprocal interrelation between FGF-2 and K(Ca)3.1 channels. K(Ca)3.1 channels that are under the transcriptional control of FGF-2 are part of the FGF-2-mediated signaling cascade leading to an acceleration of migration.
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