1,920 research outputs found
Do anionic phospholipids serve as cofactors or second messengers for the regulation of activity of cloned ATP-sensitive K+ channels?
The regulation of ion channels by anionic phospholipids is currently very topical. An outstanding issue is whether phosphatidylinositol 4,5-diphosphate and related species act as true second messengers in signaling or behave in a manner analogous to an enzymatic cofactor. This question is especially pertinent regarding ATP-sensitive K+ channels in smooth muscle, for which there is substantial literature supporting inhibitory regulation by hormones. In this study, we have examined regulation of the potential cloned equivalents of the smooth muscle ATP-sensitive K+ channel (SUR2B/Kir6.1 and SUR2B/Kir6.2). We find that both can be inhibited via the G(q/11)-coupled muscarinic M3 receptor but that the pathways by which this occurs are different. Our data show that SUR2B/Kir6.1 is inhibited by protein kinase C and binds anionic phospholipids with high affinity, such that potential physiological fluctuations in their levels do not influence channel activity. In contrast, Kir6.2 is not regulated by protein kinase C but binds anionic phospholipids with low affinity. In this case, phosphatidylinositol 4,5-diphosphate and related species have the potential to act as second messengers in signaling. Thus, Kir6.1 and Kir6.2 are regulated by distinct inhibitory mechanisms
Mechanical testing of Additive Manufactured polymer components using Materials Extrusion Technology
A REVIEW OF THERMAL MODELLING FOR METAL ADDITIVE MANUFACTURING PROCESSES: BASIC ANALYTICAL MODELS TO STATE-OF-THE-ART SOFTWARE PACKAGES.
A Simplified Thermal Approximation Method to include the effects of Marangoni Convection in the melt pools of processes that involve moving point heat sources
Phosphoenolpyruvate phosphomutase activity in an L-phosphonoalanine-mineralizing strain of Burkholderia cepacia
A strain of Burkholderia cepacia isolated by enrichment culture utilized l-2-amino-3-phosphonopropionic acid (phosphonoalanine) at concentrations up to 20 mM as a carbon, nitrogen, and phosphorus source in a phosphate-insensitive manner. Cells contained phosphoenolpyruvate phosphomutase activity, presumed to be responsible for cleavage of the CβP bond of phosphonopyruvate, the transamination product of l-phosphonoalanine; this was inducible in the presence of phosphonoalanine
DEVELOPMENTS IN LARGE SCALE ADDITIVE MANUFACTURE β THE POTENTIAL AND LIMITATIONS OF WIRE ARC ADDITIVE MANUFACTURE AND ASSOCIATED TECHNOLOGIES
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