RESUMO
SNP genotyping device is an essential tool in the upcoming era ofpersonal genome and personalised medicine. Human genome has more than 10 million SNPs whereas conventional SNP genotyping device can only hold 1 million SNPs. Thus, intelligent SNP contents selection is required to maximise the value of SNP genotyping device. Here, we developed a new selection algorithm and applied this method to design genotyping contents for cancerand pharmacogenomic association study. This approach significantly increased the product value when compared with contents of competitive SNP genotyping product.
Assuntos
Algoritmos , Genoma Humano , Farmacogenética/métodos , Polimorfismo de Nucleotídeo Único , Genótipo , Humanos , Desequilíbrio de LigaçãoRESUMO
Since detergent-resistant lipid rafts are involved in pathogen invasion, cholesterol homeostasis, angiogenesis, neurodegenerative diseases and signal transduction, protein identification in the rafts could provide important information to study their function. Here, we analyzed detergent-resistant raft proteins isolated from rat liver by capillary liquid chromatography-tandem mass spectrometry. Out of 196 proteins identified, 32% belonged to the raft or plasma membrane, 24% to mitochondrial, 20% to microsomal, 7% to miscellaneous, and 17% are unknown proteins. For example, membrane-bound receptors, trimeric GTP-binding proteins, ATP-binding cassette transporters, and glycosylphosphatidylinositol-anchored proteins were identified in this analysis. Unexpectedly, there were many mitochondrial proteins, raising a new issue for the presence of mitochondrial rafts or the localization of mitochondrial proteins into plasma membrane rafts. We confirmed that ATP synthase alpha and beta were expressed on the surface of the plasma membrane in HepG2 hepatocytes by immunofluorescence, cell surface biotinylation, and cellular fractionation. They had two distinct biochemical properties, detergent insolubility and low density, suggesting that the ATP synthase complex might be located in plasma membrane rafts as well as in the mitochondria.