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Glucose must be metabolized by pancreatic β cells to promote glucose-stimulated insulin secretion (GSIS). Zhao et al. found that saturated long-chain monoacylglycerol acts as metabolic coupling factor for GSIS, activating the exocytotic effector Munc13-1, and that the monoacylglycerol signal is controlled by α/β-Hydrolase Domain 6 (ABHD6).
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Here, we report the x-ray structure (2.4 Å) of the IL-6R ectodomains. The N-terminal strand of the Ig-like domain (D 1) is disulfide-bonded to domain D 2, and domains D 2 and D 3, the cytokine-binding domain, are structurally similar to known cytokine-binding domains. The head-to-tail packing of two closely associated IL-6R molecules observed.
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Interleukin-6 (IL-6) is a polyfunctional cytokine that plays a central role in host defense because of its wide range of immune and hemopoietic activities and because of its potent ability to induce the acute-phase responses of the liver ().IL-6 binds first to its cognate α-chain receptor (IL-6R) with low affinity, and then the complex binds to the signal-transducing molecule gp130 to form a.
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The transmembrane and cytoplasmic domains of the IL-6R are not required for IL-6 signal transduction ().Biologically active forms of the extracellular region of the IL-6R or "soluble IL-6R" (sIL-6R; ref. 19) are found naturally in low concentrations in human urine and serum of healthy individuals ().Increased sIL-6R levels have been reported in a number of clinical conditions (e.g., HIV.
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Human alpha/beta hydrolase domain 6 (hABHD6) is an enzyme that hydrolyzes 2-arachidonoylglycerol (2-AG), a potent agonist at both cannabinoid CB1 and CB2 receptors. In vivo modulation of ABHD6.
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Human alpha/beta hydrolase domain 6 (hABHD6) is an enzyme that hydrolyzes 2-arachidonoylglycerol (2-AG), a potent agonist at both cannabinoid CB1 and CB2 receptors.. (5 μL of 550 mM) for 1 hr, respectively. The samples were desalted with a Bio-Spin 6 Column in 50 mM ammonium bicarbonate buffer containing 0.05% w/v octyl-β-glucoside, pH 8.0.
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Organisms can be classified into one of three domains based on differences in the sequences of nucleotides in the cell's ribosomal RNAs (rRNA), the cell's membrane lipid structure, and its sensitivity to antibiotics. The three domains are the Archaea, the Bacteria, and the Eukarya. Prokaryotic organisms belong either to the domain Archaea or.
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This study provides biochemical, pharmacological, cell biology,. Biochemical and pharmacological characterization of human α/β-hydrolase domain containing 6 (ABHD6) and 12 (ABHD12) J. Lipid Res., 53 (2012), pp. 2413-2424. View PDF View article CrossRef View in Scopus Google Scholar.
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α/β-Hydrolase domain 6 (ABHD6) is a monoacylglycerol hydrolase that degrades the endocannabinoid 2-arachidonoylglycerol (2-AG). Although complete or peripheral ABHD6 loss of function is protective against diet-induced obesity and insulin resistance, the role of ABHD6 in the central control of energy balance is unknown.
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α/β-Hydrolase domain 6 (ABHD6) is an enzyme that has been recently reported to regulate 2-arachidonylglycerol (2-AG) hydrolysis [ 6 ]. 2-AG serves as an important lipid precursor for the eicosanoid signalling pathway and also functions as an endogenous signalling lipid for the activation of cannabinoid receptor 1 and 2 (CB1 and CB2.