Search

For Japan, the ongoing severe fiscal condition requires urgent attention. To redress this situation, certain policy options are available: for instance, tax policy shift, pension system reform, and accelerating the economic growth. In this study, I quantify these policy changes required for achieving fiscal consolidation on the basis of an overlapping generations (OLG) model that considers multiple generations and provide a policy comparison of these options using the utility of each generation as a criterion. The simulation results suggest that a drastic policy change is necessary.If the consolidation were to depend only on the increase in consumption tax, the tax rate should be about 30%. In the case of pension system reform, its replacement rate should be cut to less than half of that in the current system. Among the policy options, pension reform seems to be suitable from the viewpoint of intergenerational equality and long-term economic growth.

The structural requirements of dehydroepiandrosterone (DHEA) for the induction of peroxisomal β-oxidation were studied in cultured rat hepatocytes. The hepatocytes were incubated for 5 days with various steroids, including 3- and 17-substituted analogues and 5-hydrogenated analogues of DHEA, and the activities of peroxisomal β-oxidation and carnitine acetyltransferase were measured. Among the steroids examined, DHEA, DHEA sulfate (DHEAS), dehydroandrosterone sulfate, androstenediol 3-sulfate, epiandrosterone sulfate and androsterone sulfate significantly induced the enzymes; 4.6- to 14.2-fold for β-oxidation and 5.1- to 10.9-fold for carnitine acetyltransferase at 50 μM. All of the sulfated steroids were more effective than the corresponding unsulfated forms. DHEAS was the most potent inducer. The 3-sulfuric group was required for the marked induction of peroxisomal β-oxidation, and the 17-carbonyl group was also important. Furthermore, the relatively planar conformation of the steroidal hydrophobic backbone was crucial for inducing the enzyme. The configuration of the 3-sulfuric group (β-configuration) and the presence of a double bond at position C5 were not primary determinants for the action of DHEAS. On the other hand, the introduction of bulky substituents to position C17 or aromatization of ring A led to a loss of inducing activity. Thus, there are strict structural requirements for the DHEA induction of peroxisomal β-oxidation, suggesting the presence of a certain specific recognition site in the cell for DHEAS, which mediates the peroxisome proliferator action of DHEA.

The in-vivo effect of dehydroepiandrosterone (DHEA) on hepatic enzyme activities of rats, mice, hamsters and guinea pigs was investigated. After DHEA treatment (300 mg/kg body weight, per os, 14 days), the activities of peroxisomal β-oxidation, catalase, carnitine acetyltransferase, carnitine palmitoyltransferase, lauric acid ω-hydroxylation, 1-acylglycerophosphocholine acyltransferase, malic enzyme and cytosolic palmitoyl-CoA hydrolase were increased in rats and in mice although to a smaller extent in the latter. These enzyme activities, however, were unchanged in hamsters with the exception of ω-hydroxylation (2.5-fold increase) and 1-acylglycerophosphocholine acyltransferase (2.0-fold increase). No significant changes were observed in any of these enzyme activities in guinea pigs. Immunoblot analysis confirmed the induction of peroxisomal acyl-CoA oxidase and enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme in rats and mice. These results indicate that there are species differences in the inducing effect of DHEA on hepatic peroxisome proliferation-associated enzymes, which correlates well with the enzyme induction observed with other peroxisome proliferators.

The structures of the insecticidal alkaloids, guinesines (4-hydroxy-3-(I-methyl-2-pyrrolidinyl)-1,2-ditbiolanes), were simplified in several ways while retaining the dithiolane ring. Most of the compounds synthesized showed activity against Chilo suppressalis and Tetranychus urticae. High potency against Chilo suppressalis was displayed by 3-(dimethylaminomethyl)-1,2-dithiolane, and a broad pesticidal spectrum was recognized in the case of 4-(dimethylaminomethyl)-1,2-dithiolane.

A variety of derivatives of 3- and 4-(dimethylaminomethyl)-1,2-dithiolanes were prepared as their biological equivalents in an analogous way to that for the nereistoxin derivatives. Most of them sh...

Acyl-CoA thioesterases, also known as acyl-CoA hydrolases, are a group of enzymes that hydrolyze CoA esters such as acyl-CoAs (saturated, unsaturated, branched chain), bile acid-CoAs, CoA esters of prostaglandins etc, to the corresponding free acid and coenzyme A. There is however significant confusion regarding the nomenclature of these genes. In agreement with the HUGO Gene Nomenclature Committee (HGNC) and the Mouse Genomic Nomenclature Committee (MGNC), a revised nomenclature for mammalian acyl-CoA thioesterases/hydrolases has been suggested for the 12 member family. The family root symbol is ACOT, with human genes named ACOT1-12, and rat and mouse named Acot1-12. Several of the ACOT genes are the result of splicing events and these splice variants are catalogued.

A long-chain acyl-CoA hydrolase, BACH, is markedly distributed in the brain and localized in neurons. However, the physiological significance of BACH is unclear. To study the gene function, we expressed the mouse BACH gene in C3H 10T1/2 fibroblastic cells using a mifepristone (RU486)-inducible gene expression system. A cell clone, 10T-S6/44, was generated by stable transfection of two plasmids encoding a mifepristone-dependent transactivator and an inducible transgene product, BACH with a C-terminal MYC-tag (BACH-MYC). The transgene expression in the 10T-S6/44 cells was tightly regulated by mifepristone. Induction of BACH-MYC and an increase in palmitoyl-CoA hydrolase activity were observed in the cells treated with 3 x 10(-11) M mifepristone and reached maximal levels at a concentration of 1 x 10(-9) M for 48 h. The growth rate of cells showing the maximal induction of BACH-MYC was reduced, whereas phospholipid synthesis was unchanged. These results suggested that BACH affects specific cellular systems and functions, but not all acyl-CoA-utilizing processes.