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Differential Functions of Ras for Malignant Phenotypic Conversion
Aree Moon 대한약학회 2006 Archives of Pharmacal Research Vol.29 No.2
Among the effector molecules connected with the group of cell surface receptors, Ras proteins have essential roles in transducing extracellular signals to diverse intracellular events, by controlling the activities of multiple signaling pathways. For over 20 years since the discovery of Ras proteins, an enormous amount of knowledge has been accumulated as to how the proteins function in overlapping or distinct fashions. The signaling networks they regulate are very complex due to their multiple functions and cross-talks. Much attention has been paid to the pathological role of Ras in tumorigenesis. In particular, human tumors very frequently express Ras proteins constitutively activated by point mutations. Up to date, three members of the Ras family have been identified, namely H-Ras, K-Ras (A and B), and N-Ras. Although these Ras isoforms function in similar ways, many evidences also support the distinct molecular function of each Ras protein. This review summarizes differential functions of Ras and highlights the current view of the distinct signaling network regulated by each Ras for its contribution to the malignant phenotypic conversion of breast epithelial cells. Four issues are addressed in this review: (1) Ras proteins, (2) membrane localization of Ras, (3) effector molecules downstream of Ras, (4) Ras signaling in invasion. In spite of the accumulation of information on the differential functions of Ras, much more remains to be elucidated to understand the Ras-mediated molecular events of malignant phenotypic conversion of cells in a greater detail.
Effect of Glycyrrhizae Radix on the Glucuronidation in Rat Liver
Moon, Aree,Lee, Mi-Kyung,Kim, Seung-Hee,Kim, Young-Choong,Lee, Song-Deuk The Pharmaceutical Society of Korea 1995 Archives of Pharmacal Research Vol.18 No.5
Pretreatment of Glycyrrhizae Radix(GR) to male Sprague-Dawley rats was demonstrated to increase excretion of acetaminophen-glucuronide ocnjugate when bile nad urine were assayed after administration of acetaminophen. In order to study the effect of GR on the glucuronidation in rats, we examined enzymatic activities of hepatic UDP-glucuronosyl-transferases (UDP-GT1 and UDP-GT2) and intracellular concentrations of hepatic UDP-glucuronic acid (UDP-GA), upon the administration of GR (1 g/kg body weight, p.o.) or glycyrrhizin (23 mg/kg body weight, p.o.) a major component of GR, for 6 days. GR and glycyrrhizin caused increases in specific activities of UDP-GT2 111% and 96% respectively. Specific activity of UDP-GT1 was increased 25% by GR treatment whereas it was not significantly increased by glycyrrhizin. Concentrations of UDP-GA were increased 257% by GR and 484% by glycyrrhizin. These data indicate that GR activated glucuronidation and thus suggest the possibility that GR may influence detoxification of xenobiotics in rat liver.