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The thienopyridine A-769662 and benzimidazole 991 inhibit human TASK-3 potassium channels in an AMPK-independent manner.
Biochem Pharmacol
December 2024
Centre for Discovery Brain Sciences, Hugh Robson Building, University of Edinburgh, Edinburgh EH8 9XD, UK. Electronic address:
Article Synopsis
- TASK-1/3 channels in carotid body type 1 cells are key for sensing low oxygen levels, affecting potassium currents and ultimately influencing breathing patterns.
- Recent studies questioned whether AMP-activated protein kinase (AMPK) directly inhibits TASK-3 channels in response to hypoxia, although a recognizable phosphorylation motif was found in human TASK-3.
- Experiments with various AMPK activators indicated that two compounds, A-769662 and 991, inhibit hTASK-3 currents, while establishing that AMPK does not regulate TASK-3 currents as initially proposed.
Investigation of the specificity and mechanism of action of the ULK1/AMPK inhibitor SBI-0206965.
Biochem J
August 2021
Novo Nordisk Foundation Center for Basic Metabolic Research, University of Copenhagen, Copenhagen, Denmark.
SBI-0206965, originally identified as an inhibitor of the autophagy initiator kinase ULK1, has recently been reported as a more potent and selective AMP-activated protein kinase (AMPK) inhibitor relative to the widely used, but promiscuous inhibitor Compound C/Dorsomorphin. Here, we studied the effects of SBI-0206965 on AMPK signalling and metabolic readouts in multiple cell types, including hepatocytes, skeletal muscle cells and adipocytes. We observed SBI-0206965 dose dependently attenuated AMPK activator (991)-stimulated ACC phosphorylation and inhibition of lipogenesis in hepatocytes.
View Article and Find Full Text PDFCell-specific regulation of iNOS by AMP-activated protein kinase in primary rat hepatocytes.
J Surg Res
January 2018
Department of Surgery and Price Institute of Surgical Research, University of Louisville, Louisville, Kentucky.
Article Synopsis
- AMP-activated protein kinase (AMPK) plays a key role in regulating metabolic pathways in liver cells (hepatocytes), particularly during sepsis and shock, by influencing nitric oxide (NO) production and inducible nitric oxide synthase (iNOS) expression.
- Experiments using rat hepatocytes showed that proinflammatory cytokines IL-1β and IFNγ increased iNOS expression and AMPK activity, with AMPK inhibition leading to reduced NO production, whereas AMPK activation had the opposite effect.
- The findings suggest that AMPK enhances NO production and iNOS expression in hepatocytes through specific signaling pathways, indicating that medications that alter AMPK activity could impact inflammatory responses in liver cells.
AMP-activated protein kinase activates neuropeptide Y neurons in the hypothalamic arcuate nucleus to increase food intake in rats.
Neurosci Lett
July 2011
Division of Integrative Physiology, Department of Physiology, Jichi Medical University School of Medicine, Shimotsuke, Tochigi 329-0498, Japan.
AMP-activated protein kinase (AMPK) is an energy sensor that is activated by the increase of intracellular AMP:ATP ratio. AMPK in the hypothalamic arcuate nucleus (ARC) is activated during fasting and the activation of AMPK stimulates food intake. To clarify the pathway underlying AMPK-induced feeding, we monitored the activity of single ARC neurons by measuring cytosolic Ca(2+) concentration ([Ca(2+)](i)) with fura-2 fluorescence imaging.
View Article and Find Full Text PDFElucidation of the substrate specificity, kinetic and catalytic mechanism of adenylosuccinate lyase from Plasmodium falciparum.
Biochim Biophys Acta
April 2009
Molecular Biology and Genetics Unit, Jawaharlal Nehru Centre for Advanced Scientific Research, Jakkur, Bangalore 560 064, India.
Adenylosuccinate lyase (ASL) catalyzes two distinct but chemically similar reactions in purine biosynthesis. The first, exclusive to the de novo pathway involves the cleavage of 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR) to 5-aminoimidazole-4-carboxamide ribonucleotide (AICAR) and fumarate and the second common to both de novo and the salvage pathways involves the cleavage of succinyl-adenosine monophosphate (SAMP) to AMP and fumarate. A detailed kinetic and catalytic mechanism of the recombinant His-tagged ASL from Plasmodium falciparum (PfASL) is presented here.
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