8,737 research outputs found
TACC3-ch-TOG track the growing tips of microtubules independently of clathrin and Aurora-A phosphorylation
Full text linkThe interaction between TACC3 (transforming acidic coiled coil protein 3) and the microtubule polymerase ch-TOG (colonic, hepatic tumor overexpressed gene) is evolutionarily conserved. Loading of TACC3–ch-TOG onto spindle microtubules requires the phosphorylation of TACC3 by Aurora-A kinase and the subsequent interaction of TACC3 with clathrin to form a microtubule binding surface. Whether there is a pool of TACC3–ch-TOG that is independent of clathrin in human cells, and what is the function of this pool, are open questions. Here, we report that TACC3 is recruited to the plus-ends of microtubules by its association with ch-TOG and that this pool is independent of phosphorylation and binding to clathrin. The plus-end binding of TACC3–ch-TOG persists in interphase and we propose that one cellular function of TACC3–ch-TOG is to modulate cell migration. We also describe the distinct subcellular pools of TACC3, ch-TOG and clathrin. TACC3 is often described as a centrosomal protein, but we show that there is no significant population of TACC3 at centrosomes. The delineation of distinct protein pools reveals a simplified view of how these proteins are organized and controlled by post-translational modification
Differences in the effect on neural stem cells of fetal bovine serum in substrate-coated and soluble form 5901-5908
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Change in electrophoretic mobility of PC12 cells after cultured on PVA membranes modified with different diamines
No full textThe cell-biomaterial interaction is of extreme importance in regulating the numerous functions necessary for cell adhesion, growth, and differentiation. In the current study, electrophoresis was used to investigate the interactions between cells and biomaterials by measuring the change in electrophoretic mobility of pheochromocytoma (PC12) cells after they were cultured on the poly (vinyl alcohol) membranes modified with different diamines. Variations in cellular activity and electrophoretic mobility of cultured cells were compared. It was found that the intracellular metabolism and the cell surface charge properties were altered after cells contacting biomaterials and the variation of the latter occurred earlier than that of the former. Although the precise mechanism by which the variation of electrophoretic mobility of cultured PC12 cells was unknown, the biomaterials could influence the cell mobility within a short incubation time. It was hypothesized that changes in extracellular matrix components of cell surface may be in part responsible
The effect of chitosan and PVDF substrates on the behavior of embryonic rat cerebral cortical stem cells 4461-4469.
No full textOpioid receptor independent effects of morphine on membrane currents in single cardiac myocytes.
No full textSimultaneous determination of adenosine and its metabolites by capillary electrophoresis as a rapid monitoring tool for 5 '-nucleotidase activity
No full text[[abstract]]A simple and rapid capillary electrophoretic method was developed for the simultaneous determination of micro-molar adenosine, hypoxanthine and inosine in enzyme assays without using radioactive labeled substrates. Prior to electrophoretic separation, addition of acetonitrile and sodium chloride to the assay solution and brief centrifugation are recommended for the purpose of sample cleanup and sample stacking. Under the optimal condition, the good separation with high efficiency was achieved in 6 min. Using deoxyadenylate as an internal standard, the linear range of the method was 5-200 mu M, and the concentration limits of detection of adenosine, hypoxanthine and inosine were 2.2, 3.6 and 1.4 mu M, respectively. Application of the proposed method was demonstrated by the activity assay of 5'-nucleotidase from Hep G2 cells. (c) 2006 Elsevier B.V. All fights reserved.[[note]]SC
Medical utilization and cost of women with stress urinary incontinence in outpatient clinics
No full textSynthesis and characterization of five-coordinate gallium and indium complexes stabilized by tridentate, substituted pyrrole ligands
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