TRPC6 and c-MET were expressed in DU145 and PC3 cells In additio

TRPC6 and c-MET were expressed in DU145 and PC3 cells. In addition, functional TRPC6

channels were present in DU145 and PC3 cells, and TRPC6 knockdown suppressed TRPC-like currents evoked by oleoyl-2-acetyl-sn-glycerol (OAG). Inhibition of TRPC6 channels in DU145 and PC3 cells abolished OAG- and HGF-induced Ca2+ entry. Furthermore, inhibition of TRPC6 channels arrested DU145 and PC3 cells at the G2/M phase and suppressed HGF-induced cell proliferation. Collectively, our results indicate that TRPC6 has an important role in HGF-induced DU145 and PC3 cell proliferation.”
“Some genes affect meat quality in chickens. We looked for polymorphisms in the Gallus gallus alpha-RyR gene (homologous to RyR 1) that could be associated with PSE (pale, soft and exudative) meat. Because RyR genes are over 100,000 bp long Geneticin in vivo and code for proteins with about 5000 amino acids, primers were designed to amplify a fragment of hotspot region 2, a region with a high

density of mutations in other species. Total blood DNA was extracted from 50 birds, 25 that had PSE meat and 25 normal chickens. The DNA samples were amplified by PCR, cloned, sequenced, and used to identify single nucleotide polymorphisms (SNPs). The amplified fragment WZB117 of alpha-RyR was 604 nucleotides in length; 181 nucleotides were similar to two exons from a hypothetical turkey cDNA sequence for alpha-RyR. A non-synonymous nucleotide substitution (G/A) was identified in at least one of the three sequenced clones obtained from nine animals, six PSE (HAL+) birds and three normal (HAL-) birds; they were heterozygous for this mutation. This SNP causes a change from Val to Met in the alpha-RYR protein. Since the frequencies of this SNP were not significantly different in the PSE versus normal chickens, it appears that this mutation (in heterozygosity) does not alter the structure or function of the muscle protein, making it an inappropriate candidate as a genetic marker for PSE meat.”
“The microstructure of chocolate model systems was investigated at the meso (similar to 10 mu 3 MA m), micro (similar to 50 mu m), and macro (0.1-1 mm) scales simultaneously, to examine effect

of pre-crystallization process and/or solid particle addition on the formation of a dense structure. The structure density was quantified by measuring the diffusion rate of small molecules at different length scales. At the meso scale, fluorescence recovery after photobleaching (FRAP) was utilized to quantify local diffusion rate solely in the fat phase, whereas high-performance liquid chromatography (HPLC) measurements were made to assess the global diffusion of the same molecules at the macro scale. Both techniques were used in combination with microstructure characterization using confocal laser scanning microscopy (micro scale) and supported by differential scanning calorimeter melting curves for estimating cocoa butter polymorphism.

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