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we simulated the dynamic rearrangement of actomyosi

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we simulated the dynamic rearrangement of actomyosin networks. Our simulation results indicate that an increase in the density fraction of myosin induces a higher-order structural transition of actomyosin filaments from networks to bundles, in addition to increasing the force generated by actomyosin filaments in the network. We compare our simulation results with experimental results and confirm that actomyosin bundles bridging focal ICG-001 adhesions and the characteristics of myosin-dependent rearrangement of actomyosin networks agree qualitatively with those observed experimentally. (C) 2011 Elsevier Ltd. All rights reserved.”
“The contribution of aberrant production of bioactive lipids to pathophysiological changes associated with obesity has risen to the forefront of lipid research. Increased diacylglycerol has been appreciated as a cause of insulin resistance, but emerging data support a role for sphingolipids in other metabolic diseases including obesity, diabetes, atherosclerosis and metabolic syndrome. Recent data demonstrate that elevation of plasma free fatty acids promotes aberrant sphingolipid production and composition in various tissues including skeletal muscle, pancreas and adipocytes. Moreover, rectifying these

aberrant sphingolipid profiles often attenuates pathologies associated with selleck chemicals llc their production. Although data thus far generate more questions than they answer, they indicate a major contribution of sphingolipids to pathologies associated with obesity. This review summarizes recent work in these areas.”
“The renin-angiotensin (RA) system is important for the regulation of blood pressure and electrolyte balance, and renin is the rate-limiting enzyme in this system. The recent discovery of (pro)renin receptor (PRR) has reinforced the functional role of the RA system. PRR non-proteolytically activates prorenin and its role has attracted the attention of researchers towards the RA system. However, there is insufficient information

on the biochemical structure and biological functioning of PRR due to the difficulty of measuring Farnesyltransferase PRR expression. In this work, human PRR (hPRR) with intact transmembrane and C-terminal domain (hPRR-wTM) and PRR without this domain (hPRR-w/oTM) were expressed in insect cells using baculovirus expression system (BES). Both hPRR-wTM and hPRR-w/ oTM were fused with FLAG peptide by its N-terminus. Most of the hPRR-wTM was expressed in cell fraction and hPRR-w/oTM was secreted into the culture medium. hPRR-wTM was solubilized from the membrane fraction of recombinant baculovirus-infected cells by various detergents, suggesting that hPRR-wTM might be a transmembrane protein. hPRR-wTM was purified from the solubilized fraction using anti-FLAG M2 antibody agarose.

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