Anti-CDH3 monoclonal antibody, clone DI-20

Reaction mechanisms in the Al(CH3)(3)-D2O-Si-2(NHEt)(6)-D2O ALD process for AlxSiyOz, were studied in situ with a quartz crystal microbalance (QCM) and a quadrupole mass spectrometer (QMS) at 200 degrees C. Two other pulsing sequences were investigated too to assess the surface reactivity of Si-2(NHEt)(6) and Al(CH3)(3). The resulting films were extensively analyzed with X-ray reflectivity (XRR), X-ray photoelectron spectroscopy (XPS), energy dispersive X-ray (EDX) spectroscopy, and Fourier transform infrared (FT-IR) spectroscopy. The main byproducts observed with QMS were CDH3 and NDHC2H5. The incorporation of methyl groups from TMA into the film through the formation of Si-CH3 bonds was deduced from the results. Several pathways were considered for the adsorption of Si-2(NHEt)(6) on a hydroxylated surface. According to the results, the pathway where both Si atoms in the dimeric Si-2(NHEt)(6) precursor molecule bond to the surface with a cleavage of their Si Si bond is preferred. A model based on the QCM and XPS data was build to better characterize the mechanism. The calculations indicated that 1.3 methyl ligands of Al(CH3)(3) and 3.8 NHEt ligands of Si-2(NHEt)(6) are released in average during their respective metal precursor pulses in reactions with surface hydroxyl groups, the rest being eliminated during the following D2O pulses.

P-Cadherin/CDH3 belongs to the family of classic cadherins that are engaged in various cellular activities including motility, invasion, and signaling of tumor cells, in addition to cell adhesion. However, the biological roles of P-cadherin itself are not fully characterized. Based on information derived from a previous genome-wide cDNA microarray analysis of microdissected pancreatic ductal adenocarcinoma (PDAC), we focused on P-cadherin as one of the genes most strongly overexpressed in the great majority of PDACs. To investigate the consequences of overexpression of P-cadherin in terms of pancreatic carcinogenesis and tumor progression, we used a P-cadherin-deficient PDAC cell line, Panc-1, to construct a cell line (Panc1-CDH3) that stably overexpressed P-cadherin. Induction of P-cadherin in Panc1-CDH3 increased the motility of the cancer cells, but a blocking antibody against P-cadherin suppressed the motility in vitro. Overexpression of P-cadherin was strongly associated with cytoplasmic accumulation of one of the catenins, p120ctn, and cadherin switching in PDAC cells. Moreover, P-cadherin-dependent activation of cell motility was associated with activation of Rho GTPases, Rac1 and Cdc42, through accumulation of p120ctn in cytoplasm and cadherin switching. These findings suggest that overexpression of P-cadherin is likely to be related to the biological aggressiveness of PDACs; blocking of P-cadherin activity or its associated signaling could be a novel therapeutic approach for treatment of aggressive pancreatic cancers.