Picture of virus under microscope

Research under the microscope...

The Strathprints institutional repository is a digital archive of University of Strathclyde research outputs.

Strathprints serves world leading Open Access research by the University of Strathclyde, including research by the Strathclyde Institute of Pharmacy and Biomedical Sciences (SIPBS), where research centres such as the Industrial Biotechnology Innovation Centre (IBioIC), the Cancer Research UK Formulation Unit, SeaBioTech and the Centre for Biophotonics are based.

Explore SIPBS research

Coupling of a P2Z-like purinoceptor to a fatty acid-activated K+ channel in toad gastric smooth muscle cells

Zou, H. and Ugur, M. and Drummond, R.M. and Singer, J.J. (2001) Coupling of a P2Z-like purinoceptor to a fatty acid-activated K+ channel in toad gastric smooth muscle cells. Journal of Physiology, 534 (1). pp. 59-70. ISSN 0022-3751

Full text not available in this repository. (Request a copy from the Strathclyde author)

Abstract

1. Extracellular application of ATP generates two whole-cell currents in toad gastric smooth muscle cells: an immediate inward non-selective cation current (due to the activation of a P2X or P2Z-like receptor) and a slowly developing outward K+ current. The inward non-selective cation current depends on the continuous presence of ATP while the outward K+ current can last for minutes after ATP application ceases. 2. In cell-attached patches, application of ATP to the extra-patch membrane can activate K+ channels in the patch indicating that a diffusible cellular messenger may be involved. The characteristics of these K+ channels are similar to those of a previously described fatty acid-activated K+ channel that is also a stretch-activated channel. 3. This whole-cell K+ current can be induced by ATP in the absence of extracellular Ca2+ (with EGTA present to chelate trace amounts). However, the current generated in the presence of extracellular Ca2+ is considerably larger. 4. The pharmacological profiles for the activation of the non-selective cation current and the K+ current are similar, suggesting that the same P2Z-like receptor could be mediating both responses. This type of plasma membrane receptor/channel-channel coupling by a process that does not appear to involve Ca2+ flow through the receptor/channel or a subsequent membrane potential change may be representative of a new class of signalling mechanisms.