Expression of ATP-Sensitive Potassium (KATP) Channel Subunits in Mammalian Liver

ATP-sensitive potassium channel (KATP channel) expression in the normal canine pancreas and in canine insulinomas

BACKGROUND Pancreatic beta cells express ATP-sensitive potassium (KATP) channels that are needed for normal insulin secretion and are targets for drugs that modulate insulin secretion. The KATP channel is composed of two subunits: a sulfonylurea receptor (SUR 1) and an inward rectifying potassium channel (Kir6.2). KATP channel activity is influenced by the metabolic state of the cell and initia...

ATP-sensitive potassium (KATP) channel activation decreases intraocular pressure in the anterior chamber of the eye.

PURPOSE. ATP-sensitive potassium channel (K(ATP)) openers target key cellular events, many of which have been implicated in glaucoma. The authors sought to determine whether K(ATP) channel openers influence outflow facility in human anterior segment culture and intraocular pressure (IOP) in vivo. METHODS. Anterior segments from human eyes were placed in perfusion organ culture and treated with ...

Potassium accumulation in the globally ischemic mammalian heart. A role for the ATP-sensitive potassium channel.

We investigated the contribution of opening of the ATP-sensitive K+ channel to extracellular accumulation of K+ during ischemia with the use of glibenclamide, a specific blocker of this K+ channel. To characterize the electrophysiological effects of glibenclamide during metabolic inhibition (by either application of dinitrophenol or hypoxia) we performed patch-clamp studies in isolated membrane...

Distribution of Kir 6 . 0 and SUR 2 ATP - sensitive potassium channel subunits in isolated ventricular

A mechanism for ATP-sensitive potassium channel diversity: Functional coassembly of two pore-forming subunits.

ATP-sensitive potassium channels are an octomeric complex of four pore-forming subunits of the Kir 6.0 family and four sulfonylurea receptors. The Kir 6.0 family consists of two known members, Kir 6.1 and Kir 6.2, with distinct functional properties. The tetrameric structure of the pore-forming domain leads to the possibility that mixed heteromultimers may form. In this study, we examine this b...