Vascular endothelial growth factor-A (VEGF-A

Plasma polymerization and deposition of linear, cyclic and aromatic fluorocarbons on (100)-oriented single crystal silicon substrates J. Vac. Sci. Technol. A 20, 1955 (2002; 10.1116/1.1513640 X-ray photoelectron spectroscopy and scanning electron microscopy characterization of novel poly(monosubstituted) acetylenes containing doping species Plasma polymerization of pyrrole was carried out in the presence and absence of iodine, and the resulting films were characterized by optical and electrical means. Their infrared spectra were very similar to each other, suggesting that iodine was neither bonded in any manner to, nor strongly interacting with, the pyrrole polymer chains. Based on their infrared spectra, a chemical structure was proposed for the plasma-polymerized pyrrole ͑PPPy͒ film. An analysis of the electronic spectra gave band gap energies of 1.3 and 0.8 eV for the undoped and doped PPPy films, respectively. In line with this result, the current-voltage characteristics of the two types of polymer films revealed that the conductivity of the doped PPPy film was approximately two times greater than that of the undoped one. An investigation of the scanning electron micrographs led us to conclude that iodine had changed the surface morphology of the PPPy film, resulting in the small increase in conductivity. A detailed analysis of the conduction mechanism disclosed that the conduction mechanism in the undoped PPPy film is a Schottky-type mechanism.

Cell adhesion is essential for proper tissue architecture and function in multicellular organisms. Cell adhesion molecules not only maintain tissue integrity but also possess signaling properties that contribute to diverse cellular events such as cell growth, survival, differentiation, polarity, and migration; however, the underlying molecular basis remains poorly defined. Here we identify that the cell adhesion signal initiated by the tight-junction protein claudin-6 (CLDN6) regulates nuclear receptor activity. We show that CLDN6 recruits and activates Src-family kinases (SFKs) in second extracellular domain-dependent and Y196/200-dependent manners, and SFKs in turn phosphorylate CLDN6 at Y196/200. We demonstrate that the CLDN6/SFK/PI3K/AKT axis targets the AKT phosphorylation sites in the retinoic acid receptor γ (RARγ) and the estrogen receptor α (ERα) and stimulates their activities. Interestingly, these phosphorylation motifs are conserved in 14 of 48 members of human nuclear receptors. We propose that a similar link between diverse cell adhesion and nuclear receptor signalings coordinates a wide variety of physiological and pathological processes.

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