Extracellular ATP activates ERK1/ERK2 via a metabotropic P2Y1 receptor in a Ca2+ independent manner in differentiated human skeletal muscle cells

Biochemical Pharmacology
Christopher MayMartin Hohenegger

Abstract

ATP is released at the neuromuscular junction to regulate development and proliferation. The sequential expression of P2X and P2Y receptors has been correlated to these effects in many species and cell lines. We have therefore investigated ATP mediated signalling in differentiated primary human skeletal muscle cells. ATP was capable to trigger Ca2+ transients in these cells via P2Y receptors which were not attributable to Ca2+ influx via P2X receptors. Instead, ATP propagated the formation of inositol phosphate (IP) with an EC50 of 21.3 microM. The Ca2+ transient provoked by ATP was abrogated roughly 75% by the phospholipase C (PLC) inhibitor, U73122. Interestingly, the ryanodine sensitive Ca2+ pool was not involved in ATP triggered Ca2+ release. On mRNA level and by a pharmacological approach we confirmed the presence of the P2Y1, P2Y2, P2Y4 and P2Y6 receptors. Substantially, ATP activated IP formation via a P2Y1 receptor. In addition, ATP elicited extracellular signal regulated kinase (ERK)1/2 phosphorylation in a time and concentration dependent manner, again mainly via P2Y1 receptors. The ATP mediated ERK1/2 phosphorylation was strictly dependent on phospholipase C and PI3 kinase activity. Importantly, ATP mediated ERK1/2 p...Continue Reading

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Citations

Jun 10, 2009·Purinergic Signalling·Clare M TurnerFrederick W K Tam
Aug 15, 2013·Purinergic Signalling·Geoffrey BurnstockIsabel R Orriss
Oct 14, 2009·The Journal of Biological Chemistry·Sonja BuvinicEnrique Jaimovich
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Feb 11, 2011·Molecular and Cellular Biochemistry·Tiziana MartinelloRomeo Betto
Jul 10, 2014·Journal of the International Society of Sports Nutrition·Ralf JägerJacob M Wilson

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