PMID: 11334629May 4, 2001Paper

Molecular cloning and functional expression of Xenopus laevis oocyte ATP-activated P2X4 channels

Biochimica Et Biophysica Acta
P F JurankaC E Morris

Abstract

All cells contain mechanosensitive ion channels, yet the molecular identities of most are unknown. The purpose of our study was to determine what encodes the Xenopus oocyte's mechanosensitive cation channel. Based on the idea that homologues to known channels might contribute to the stretch channels, we screened a Xenopus oocyte cDNA library with cation channel probes. Whereas other screens were negative, P2X probes identified six isoforms of the P2X4 subtype of ATP-gated channels. From RNase protection assays and RT-PCR, we demonstrated that Xenopus oocytes express P2X4 mRNA. In expression studies, four isoforms produced functional ATP-gated ion channels; however, one, xP2X4c, had a conserved cysteine replaced by a tyrosine and failed to give rise to functional channels. By changing the tyrosine to a cysteine, we showed that this cysteine was crucial for function. We raised antibodies against a Xenopus P2X4 C-terminal peptide to investigate xP2X4 protein expression. This affinity purified anti-xP2X4 antibody recognized a 56 kDa glycosylated Xenopus P2X4 protein expressed in stably transfected HEK-293 cells and in P2X4 cDNA injected oocytes overexpressing the cloned P2X4 channels; however, it failed to recognize proteins in con...Continue Reading

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Citations

May 2, 2012·Purinergic Signalling·Karina Kaczmarek-HájekAnnette Nicke
Jul 22, 2015·The Biochemical Journal·Andrew K J BoyceLeigh Anne Swayne
Sep 25, 2002·Physiological Reviews·R Alan North
Aug 14, 2019·Frontiers in Cellular Neuroscience·Camille BlanchardKarine Massé
Feb 3, 2007·American Journal of Physiology. Regulatory, Integrative and Comparative Physiology·Monika Sundqvist

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