Results 31 to 40 of about 14,110 (214)

Glibenclamide reverses cardiovascular abnormalities of Cantu syndrome driven by KATP channel overactivity. [PDF]

open access: yesJ Clin Invest, 2020
Cantu syndrome (CS) is a complex disorder caused by gain-of-function (GoF) mutations in ABCC9 and KCNJ8, which encode the SUR2 and Kir6.1 subunits, respectively, of vascular smooth muscle (VSM) KATP channels.
McClenaghan C   +9 more
europepmc   +3 more sources

Upregulation of cardioprotective SUR2A by sub-hypoxic drop in oxygen [PDF]

open access: yes, 2014
The effects of hypoxia on gene expression have been vigorously studied, but possible effects of small changes in oxygen tension have never been addressed.
Sukhodub, Andriy   +9 more
core   +1 more source

KATP channel opening accelerates and stabilizes rotors in a swine heart model of ventricular fibrillation

open access: yes, 2023
El artículo habla del estudio realizado que investiga los mecanismos que causan la fibrilación ventricular (FV), un ritmo cardíaco peligroso. Se centra en el papel de los canales KATP y su relación con la formación de rotores estables durante la FV.
García Torrent, María Jesús   +10 more
core   +1 more source

Morphine Efficacy, Tolerance, and Hypersensitivity Are Altered After Modulation of SUR1 Subtype KATP Channel Activity in Mice

open access: yesFrontiers in Neuroscience, 2019
ATP-sensitive potassium (KATP) channels are found in the nervous system and are downstream targets of opioid receptors. KATP channel activity can effect morphine efficacy and may beneficial for relieving chronic pain in the peripheral and central nervous
Cole Fisher   +9 more
doaj   +1 more source

The Selective Rat Toxicant Norbormide Blocks KATP Channels in Smooth Muscle Cells But Not in Insulin-Secreting Cells

open access: yesFrontiers in Pharmacology, 2019
Norbormide is a toxicant selective for rats to which it induces a widespread vasoconstriction. In a recent paper, we hypothesized a role of ATP-sensitive potassium (KATP) channels in norbormide-induced vasoconstriction.
Simona Saponara   +8 more
doaj   +1 more source

Nucleotide inhibition of the pancreatic ATP-sensitive K+ channel explored with patch-clamp fluorometry

open access: yeseLife, 2020
Pancreatic ATP-sensitive K+ channels (KATP) comprise four inward rectifier subunits (Kir6.2), each associated with a sulphonylurea receptor (SUR1). ATP/ADP binding to Kir6.2 shuts KATP. Mg-nucleotide binding to SUR1 stimulates KATP. In the absence of Mg2+
Samuel G Usher   +2 more
doaj   +1 more source

Pharmacological rescue of trafficking-impaired ATP-sensitive potassium channels

open access: yesFrontiers in Physiology, 2013
ATP-sensitive potassium (KATP) channels link cell metabolism to membrane excitability and are involved in a wide range of physiological processes including hormone secretion, control of vascular tone, and protection of cardiac and neuronal cells against ...
Gregory M. Martin   +3 more
doaj   +1 more source

KATP channels are necessary for glucose-dependent increases in amyloid-β and Alzheimer’s disease–related pathology

open access: yesJCI Insight, 2023
Elevated blood glucose levels, or hyperglycemia, can increase brain excitability and amyloid-β (Aβ) release, offering a mechanistic link between type 2 diabetes and Alzheimer’s disease (AD).
John Grizzanti   +21 more
doaj   +1 more source

Immunolocalization of KATP channel subunits in mouse and rat cardiac myocytes and the coronary vasculature.

open access: yes, 2005
BACKGROUND: Electrophysiological data suggest that cardiac KATP channels consist of Kir6.2 and SUR2A subunits, but the distribution of these (and other KATP channel subunits) is poorly defined.
Artman, M   +27 more
core   +1 more source

Identification of putative potassium channel homologues in pathogenic protozoa [PDF]

open access: yes, 2012
K(+) channels play a vital homeostatic role in cells and abnormal activity of these channels can dramatically alter cell function and survival, suggesting that they might be attractive drug targets in pathogenic organisms.
Prole, D L   +3 more
core   +1 more source

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