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1.
Int Angiol ; 29(2 Suppl): 61-8, 2010 Apr.
Article in English | MEDLINE | ID: mdl-20357751

ABSTRACT

AIM: We aimed to determine the current status of the medical expenses for the treatment of arteriosclerosis obliterans (ASO) and evaluate the cost effectiveness of the medical practices employed in ASO treatment in Japan. METHODS: We performed a prospective observational study using 140 ASO patients. The cost of the medical practices comprised the costs of outpatient treatment, pharmacological agents, and hospitalization. To compare the average monthly costs, the patients were divided into preintervention, postintervention, or conservative-therapy groups. To compare the total costs and effectiveness of each treatment, the patients who had first visited our division during the study period were classified into surgery, endovascular-revascularization (EVR), or conservative-therapy groups. The adverse reactions of the 4 most popular agents for ASO were investigated, and bleeding events were assessed specifically. RESULTS: The average monthly costs for outpatient treatment and pharmacological agents were yen 168,002 in conservative cases, yen 149,871 in preoperation cases, and yen 128,527 in postoperation cases. The mean total costs were yen 5,407,950 in conservative cases, yen 7,375,290 in surgical cases, and yen 2,631,650 in EVR cases. The average change of the gauge in clinical status was 0.57 in conservative cases, 2.13 in surgical cases, and 2.25 in EVR cases. Warfarin induced more bleeding complications than the other agents. CONCLUSION: The costs of pharmacological agents represented much of the medical costs in any treatment groups.


Subject(s)
Arteriosclerosis Obliterans/economics , Arteriosclerosis Obliterans/therapy , Cardiovascular Agents/economics , Cardiovascular Agents/therapeutic use , Health Care Costs , Outcome and Process Assessment, Health Care/economics , Vascular Surgical Procedures/economics , Aged , Aged, 80 and over , Ambulatory Care/economics , Amputation, Surgical/economics , Angioplasty, Balloon/economics , Angioplasty, Balloon/instrumentation , Cardiovascular Agents/adverse effects , Combined Modality Therapy , Cost-Benefit Analysis , Drug Costs , Female , Hospital Costs , Hospitalization/economics , Humans , Japan , Male , Middle Aged , Models, Economic , Prospective Studies , Stents/economics , Treatment Outcome
2.
Diabetes Care ; 24(7): 1248-52, 2001 Jul.
Article in English | MEDLINE | ID: mdl-11423510

ABSTRACT

OBJECTIVE: To test the hypothesis that intra-abdominal fat plays a primary role over general adiposity for metabolic abnormalities and atherosclerosis. RESEARCH DESIGN AND METHODS: We cross-sectionally studied 849 Japanese men aged 50.3 +/- 8.5 years (range 20-78) with BMI 23.5 +/- 2.9 kg/m(2). Intimal-medial thickness (IMT) of the carotid artery was measured by ultrasound. General adiposity was assessed by BMI. Waist circumference and waist-to-hip ratio (WHR) were used as a surrogate measure for abdominal fat. Abdominal subcutaneous fat area (ASF) and intra-abdominal fat area (IAF) were measured by computed tomography. Correlations between these measures and carotid IMT were analyzed. The interaction of generalized adiposity (BMI) and IAF in relation to metabolic variables, such as glucose tolerance, insulin resistance, and serum lipids, was also evaluated. RESULTS: BMI, waist circumference, WHR, ASF, and IAF were all correlated with carotid IMT. Adjustment for BMI eliminated the associations between IMT and waist circumference, ASF, and IAF. In contrast, WHR retained a significant correlation with IMT. BMI and IAF were associated with insulin resistance, glucose tolerance, HDL cholesterol, and blood pressure independently of each other. IAF was an independent correlate for serum triglyceride, but BMI was not. CONCLUSIONS: The primary importance of IAF over general adiposity for carotid atherosclerosis was not confirmed. Caution is recommended when using WHR as a measure of abdominal fat. The roles of IAF for metabolic abnormalities may be more limited than conventionally thought. BMI and WHR are simple and better clinical predictors for carotid atherosclerosis versus IAF.


Subject(s)
Adipose Tissue/anatomy & histology , Body Constitution , Body Mass Index , Carotid Arteries/anatomy & histology , Carotid Artery Diseases/epidemiology , Glucose Intolerance/epidemiology , Abdomen , Adult , Aged , Area Under Curve , Asian People , Blood Glucose/metabolism , Blood Pressure , Carotid Arteries/diagnostic imaging , Cholesterol/blood , Cross-Sectional Studies , Electrocardiography , Glucose Tolerance Test , Humans , Insulin/blood , Insulin Resistance , Japan , Male , Middle Aged , Predictive Value of Tests , Risk Factors , Tomography, X-Ray Computed , Triglycerides/blood , Tunica Intima/diagnostic imaging , Tunica Media/diagnostic imaging , Ultrasonography
3.
Clin Endocrinol (Oxf) ; 55(6): 797-803, 2001 Dec.
Article in English | MEDLINE | ID: mdl-11895222

ABSTRACT

OBJECTIVE: Dehydroepiandrosterone (DHEA) and DHEA-sulphate (S) have been suggested to play protective roles in many pathological states, some of which are observed in hyperthyroidism. If DHEA and DHEA-S levels change in hyperthyroidism, they might participate as a possible causative link with such pathophysiological changes in hyperthyroidism. However, the CRH-ACTH-DHEA system in hyperthyroidism has not been clearly defined. We examined plasma levels of DHEA and DHEA-S together with ACTH and cortisol in both hyperthyroid (Hyper) and euthyroid states (Eu). METHODS: Eighteen patients (5 men and 13 women, aged 46.9 +/- 2.8 years) with Graves' disease were studied before treatment and again in the euthyroid state following treatment with methimazole. A 100 microg hCRH stimulation test and a low-dose (0.5 microg) 1-24 ACTH stimulation test were performed on separate days. Basal levels and A area under the response curve (AUC) were compared between Hyper and Eu. RESULTS: DHEA-S was higher in Hyper than in Eu. However, basal DHEA did not differ between Hyper and Eu. The ratio of DHEA to DHEA-S was lower in Hyper than in Eu. AAUC of DHEA during a CRH test was lower in Hyper than in Eu. However, AAUC of DHEA during an ACTH test was similar in both Hyper and Eu. Basal ACTH was higher in Hyper than in Eu. In both CRH and ACTH tests, AAUC of cortisol response was lower in Hyper than in Eu, although the basal cortisol level was not different. CONCLUSION: The balance of the conversion between DHEA-S and DHEA in the hyperthyroid state favoured DHEA-S. Similar to cortisol, the DHEA response in the CRH test in hyperthyroidism seemed to be insufficiently compensated for by increased ACTH, although the DHEA response to low-dose ACTH was similar in the hyperthyroid and euthyroid states. Increased DHEA-S might play some role in the pathological states in many organs in hyperthyroidism.


Subject(s)
Corticotropin-Releasing Hormone , Dehydroepiandrosterone Sulfate/blood , Dehydroepiandrosterone/blood , Hyperthyroidism/blood , Adrenocorticotropic Hormone/blood , Adult , Antithyroid Agents/therapeutic use , Area Under Curve , Female , Humans , Hydrocortisone/blood , Male , Methimazole/therapeutic use , Middle Aged , Thyrotropin/blood , Thyroxine/blood , Triiodothyronine/blood
4.
J Hepatol ; 31(2): 215-20, 1999 Aug.
Article in English | MEDLINE | ID: mdl-10453932

ABSTRACT

BACKGROUND/AIMS: Interferon-a has been reported to acutely induce insulin resistance and glucose intolerance. The effects of long-term treatment with interferon-a on glucose metabolism remain unclear. METHODS: Thirty-two Japanese patients with chronic hepatitis C were given interferon-a (6x10(6)U/day) daily for 2 weeks and thereafter 3 times weekly up to 6 months. The patients received a 75-g oral glucose tolerance test before the treatment. Fifteen patients also had an intravenous glucose tolerance test for an assessment of insulin sensitivity with Bergman's minimal model. These tests were repeated 3 months after the treatment. RESULTS: Insulin sensitivity was not affected by the treatment (5.7+/-3.8 vs 5.2+/-3.8 10(-4) x min(-1) x mU(-1) x l , not significant) and a statistically significant but minimum decrease in area under the curve of plasma glucose (1012+/-332 vs 928+/-282 mmol x l(-1) x min, p<0.01) in a 75-g oral glucose tolerance test was noted. Acute insulin response to intravenous glucose tolerance tests (214+/-275 vs 294+/-334 mU x l(-1) x min, p<0.05) increased slightly. CONCLUSION: Contrary to the known acute metabolic effects, interferon-a therapy for 3 months in patients with chronic hepatitis C did not have deleterious effects on insulin sensitivity and glucose tolerance.


Subject(s)
Antiviral Agents/therapeutic use , Blood Glucose/metabolism , Hepatitis C, Chronic/blood , Hepatitis C, Chronic/drug therapy , Insulin Resistance , Interferon-alpha/therapeutic use , Adult , Antiviral Agents/pharmacology , Female , Glucose Tolerance Test/methods , Humans , Interferon-alpha/pharmacology , Male , Middle Aged
5.
FEBS Lett ; 434(3): 335-8, 1998 Sep 04.
Article in English | MEDLINE | ID: mdl-9742950

ABSTRACT

Previous studies using retinal analogs (Wada, A., Sakai, M., Kinumi, T., Tsujimoto, K., Yamauchi, M. and Ito, M. (1994) J. Org. Chem. 59, 6992-6997; Wada, A., Sakai, M., Imamoto, Y., Shichida., Y., Yoshizawa, T. and Ito, M. (1993) Chem. Pharm. Bull. 41, 793-795) revealed that both retinochrome and visual pigments share a common chromophoric conformation in which the ring region of retinal is twisted ca. 50 degrees with respect to the plane of the polyene chain, suggesting a highly conserved 6-s-cis conformation throughout rhodopsin-like pigments in animals. By contrast, 6-s-trans conformation was commonly observed or suggested in archaebacterial rhodopsins examined thus far. Here we have reconstituted in vivo both the photoreceptor for photobehavioral responses of the unicellular alga Chlamydomonas reinhardtii and the second archaeal sensory photoreceptor phoborhodopsin from a series of retinal analogs. Results exclusively point to the conclusion that in both photoreceptors retinal has the coplanar 6-s-trans conformation, though recent molecular cloning studies revealed no homology between Chlamydomonas photoreceptor (chlamyrhodopsin) and archaeal rhodopsins.


Subject(s)
Archaea/chemistry , Chlamydomonas/chemistry , Retinaldehyde/chemistry , Rhodopsin/analogs & derivatives , Animals , Molecular Conformation , Rhodopsin/chemistry
6.
Bioorg Med Chem Lett ; 8(11): 1365-8, 1998 Jun 02.
Article in English | MEDLINE | ID: mdl-9871767

ABSTRACT

8,16-Ethanoretinal 3 was synthesized from 2-methylcyclohexanone. From the binding experiments of 3 and 8,18-ethanoretinal 2 with apoproteins of sensory rhodopsin I and phoborhodopsin, it was found that retinal was incorporated as 6s-trans conformation in the both proteins.


Subject(s)
Archaeal Proteins , Bacteriorhodopsins/chemistry , Carotenoids , Halorhodopsins , Retinaldehyde/chemistry , Sensory Rhodopsins , Bacteriorhodopsins/metabolism , Halobacterium/metabolism , Stereoisomerism
7.
Eur J Biochem ; 179(2): 365-71, 1989 Feb 01.
Article in English | MEDLINE | ID: mdl-2645139

ABSTRACT

Respiratory-deficient mutants of Saccharomyces cerevisiae assigned to pet complementation group G72 are impaired in mitochondrial protein synthesis. The loss of this activity has been correlated with the inability of the mutants to acylate the two methionyl-tRNAs of yeast mitochondria. A nuclear gene (MSM1) capable of complementing the respiratory deficiency has been cloned by transformation of the G72 mutant C122/U3 with a yeast genomic library. In situ disruption of the MSM1 gene in a wild-type haploid strain of yeast induces a respiratory-deficient phenotype but does not affect the ability of the mutant to grow on fermentable substrates indicating that the product of MSM1 functions only in mitochondrial protein synthesis. Mitochondrial extracts prepared from the mutant with the disrupted copy of MSM1 were found to be defective in acylation of the two mitochondrial methionyl-tRNAs thereby confirming the identity of MSM1 as the structural gene for the mitochondrial methionyl-tRNA synthetase. The sequence of the protein encoded by MSM1 is similar to the Escherichia coli and yeast cytoplasmic methionyl-tRNA synthetases. Based on the primary-sequence similarities of the three proteins, the mitochondrial enzyme appears to be more related to the bacterial than to the yeast cytoplasmic methionyl-tRNA synthetase.


Subject(s)
Amino Acyl-tRNA Synthetases/genetics , Genes, Fungal , Genes , Methionine-tRNA Ligase/genetics , Saccharomyces cerevisiae/genetics , Amino Acid Sequence , Base Sequence , Cell Nucleus/enzymology , Cloning, Molecular , Cytoplasm/enzymology , Escherichia coli/enzymology , Mitochondria/enzymology , Molecular Sequence Data , Mutation , Oxygen Consumption , Phenotype , Saccharomyces cerevisiae/enzymology
8.
J Biol Chem ; 263(2): 850-6, 1988 Jan 15.
Article in English | MEDLINE | ID: mdl-2826465

ABSTRACT

Respiratory deficient mutants of Saccharomyces cerevisiae previously assigned to complementation group G59 are pleiotropically deficient in respiratory chain components and in mitochondrial ATPase. This phenotype has been shown to be a consequence of mutations in a nuclear gene coding for mitochondrial leucyl-tRNA synthetase. The structural gene (MSL1) coding for the mitochondrial enzyme has been cloned by transformation of two different G59 mutants with genomic libraries of wild type yeast nuclear DNA. The cloned gene has been sequenced and shown to code for a protein of 894 residues with a molecular weight of 101,936. The amino-terminal sequence (30-40 residues) has a large percentage of basic and hydroxylated residues suggestive of a mitochondrial import signal. The cloned MSL1 gene was used to construct a strain in which 1 kb of the coding sequence was deleted and substituted with the yeast LEU2 gene. Mitochondrial extracts obtained from the mutant carrying the disrupted MSL1::LEU2 allele did not catalyze acylation of mitochondrial leucyl-tRNA even though other tRNAs were normally charged. These results confirmed the correct identification of MSL1 as the structural gene for mitochondrial leucyl-tRNA synthetase. Mutations in MSL1 affect the ability of yeast to grow on nonfermentable substrates but are not lethal indicating that the cytoplasmic leucyl-tRNA synthetase is encoded by a different gene. The primary sequence of yeast mitochondrial leucyl-tRNA synthetase has been compared to other bacterial and eukaryotic synthetases. Significant homology has been found between the yeast enzyme and the methionyl- and isoleucyl-tRNA synthetases of Escherichia coli. The most striking primary sequence homology occurs in the amino-terminal regions of the three proteins encompassing some 150 residues. Several smaller domains in the more internal regions of the polypeptide chains, however, also exhibit homology. These observations have been interpreted to indicate that the three synthetases may represent a related subset of enzymes originating from a common ancestral gene.


Subject(s)
Amino Acyl-tRNA Synthetases/analysis , Escherichia coli/enzymology , Isoleucine-tRNA Ligase/analysis , Leucine-tRNA Ligase/analysis , Methionine-tRNA Ligase/analysis , Saccharomyces cerevisiae/enzymology , Acylation , Amino Acid Sequence , Base Sequence , DNA Restriction Enzymes/metabolism , Genotype , Isoleucine-tRNA Ligase/genetics , Leucine-tRNA Ligase/genetics , Methionine-tRNA Ligase/genetics , Molecular Sequence Data , Mutation
9.
Mol Gen Genet ; 149(1): 33-42, 1976 Nov 24.
Article in English | MEDLINE | ID: mdl-796670

ABSTRACT

1. Fourteen cytoplasmic mutants of Saccharomyces cerevisiae with a specific deficiency of cytochrome b have been studied. The mutations have been shown to occur in two separate genetic loci, COB 1 and COB 2. These loci can be distinguished by mit- X mit- crosses. Pairwise crosses of cytochrome b mutants belonging to different loci yield 4-6% wild type recombinants corresponding to recombinational frequencies of 8-12%. In intra-locus crosses, the recombinational frequencies range from 1% to less than 0.01%. The two loci can also be distinguished by mit- X rho- crosses. Twenty rho- testers have been isolated of which ten preferentially restore mutations in COB 1 and ten others in COB 2. 2. The COB 1 and COB 2 loci have been localized on mitochondrial DNA between the two antibiotic resistance loci OLI 1 and OLI 2 in the order OLI 2-COB 2-COB 1-OLI 1. The results of mit- X mit- and mit- X rho- crosses have also been used to map the cytochrome b mutations relative to each other. The maps obtained by the two independent methods are in good agreement. 3. Mutations in COB 1 have been found to be linked to the OLI1 locus in some but not in other strains of S. cervisiae. This evidence suggests that there may be a spacer region between the two loci whose length varies from strain to strain. 4. Two mutations in COB 2 have been found to cause a loss of a mitochondrial translation product corresponding to the cytochrome b apoprotein. Instead of the wild type protein the mutants have a new low-molecular weight product which is probably a fragment of cytochrome b. The fact that the mutations revert suggests that they are nonsense mutations in the structural gene of cytochrome b.


Subject(s)
Cytochromes/biosynthesis , DNA, Mitochondrial , Genes , Saccharomyces cerevisiae/metabolism , Anti-Bacterial Agents , Drug Resistance , Genetic Complementation Test , Genetic Linkage , Mutation , Protein Biosynthesis , Recombination, Genetic
11.
J Biol Chem ; 250(20): 8228-35, 1975 Oct 25.
Article in English | MEDLINE | ID: mdl-170284

ABSTRACT

Mutants of Saccharomyces cereviaiae showing defects in cytochrome oxidase, coenzyme QH2-cytochrome c reductase, and rutamycin-sensitive ATPase are described. The mutations have been established to be nuclear, based on complementation with a cytoplasmic petite tester strain and 2:2 segregation of tetrads. Genetic analysis indicate the coenzyme QH2-cytochrome c reductase and cytochrome oxidase mutants fall into 9 and 10 different complementation groups, respectively. The mutants also form distinct classes based on absorption spectra of the mitochondrial cytochromes. Two of the ATPase mutants lack detectable F1 ATPase, while the third synthesizes F1 but does not integrate it into a membrane complex. The latter mutant is missing one of the mitochondrially synthesized subunits of the rutamycin-sensitive ATPase complex.


Subject(s)
Adenosine Triphosphatases/metabolism , Cytochrome Reductases/metabolism , Electron Transport Complex IV/metabolism , Mitochondria/enzymology , Saccharomyces cerevisiae/enzymology , Cell Nucleus/metabolism , Genetic Complementation Test , Membranes/drug effects , Membranes/enzymology , Mutation , NADPH-Ferrihemoprotein Reductase/metabolism , Rutamycin/pharmacology , Species Specificity , Ubiquinone
12.
J Biol Chem ; 250(20): 8236-42, 1975 Oct 25.
Article in English | MEDLINE | ID: mdl-171256

ABSTRACT

Mutants of Saccharomyces cervisiae with defects in enzymes of the electron transfer chain and in the rutamycin-sensitive ATPase have been isolated. Some of the mutants are specifically affected in either cytochrome oxidase, coenzyme QH2-cytochrome c reductase or ATPase. Other strains are deficient in both cytochrome oxidase and coenzyme QH2-cytochrome c reductase but still have rutamycin-sensitive ATPase. All the mutants reported in this study fail to be complemented by a rho0 tester derived from a respiratory competent strain. The meiotic spore progeny obtained by mating the mutants to a respiratory competent haploid yeast, when scored for growth on glycerol, show a non-Mendelian segregation of the phenotype. These two genetic tests indicate the mutations to be cytoplasmically inherited.


Subject(s)
Adenosine Triphosphatases/metabolism , Cytochrome Reductases/metabolism , Electron Transport Complex IV/metabolism , Mitochondria/enzymology , Cytoplasm/metabolism , Genetic Complementation Test , Membranes/drug effects , Membranes/enzymology , Mutation , NADPH-Ferrihemoprotein Reductase/metabolism , Phenotype , Rutamycin/pharmacology , Saccharomyces cerevisiae/enzymology , Spores, Fungal/metabolism , Ubiquinone
13.
Proc Natl Acad Sci U S A ; 72(6): 2054-7, 1975 Jun.
Article in English | MEDLINE | ID: mdl-166377

ABSTRACT

Two mutants with specific defects in cytochrome c oxidase (ferrocytochrome c:oxygen oxidoreductase; EC 1.9.3.1) have been isolated from cultures of Saccharomyces cerevisiae exposed to the mutagens ethyl-methane sulfonate and Mn++. The mutations have been shown to be extranuclear by two criteria. The phenotype persists in diploids formed by a cross with a p-o strain of yeast of the opposite mating type. Tetrad analysis indicates a non-Mendelian segregation (4:0 and 0:4) of the mutations. Both mutants show a total absence of cytochrome oxidase activity and of spectral cytochromes a and as. One of the mutants has been shown to be missing a polypeptide synthesized by mitochondria. The migration of this protein on polyacrylamide gels corresponds to the highest-molecular-weight subunit of cytochrome oxidase.


Subject(s)
Extrachromosomal Inheritance , Mitochondria/enzymology , Saccharomyces cerevisiae/enzymology , Diploidy , Electron Transport Complex IV/biosynthesis , Electrophoresis, Polyacrylamide Gel , Ethyl Methanesulfonate/pharmacology , Genetic Complementation Test , Genetics, Microbial , Macromolecular Substances , Manganese/pharmacology , Mitochondria/analysis , Mutation , Peptides/analysis , Saccharomyces cerevisiae/analysis , Saccharomyces cerevisiae/drug effects , Saccharomyces cerevisiae/ultrastructure
14.
J Bacteriol ; 122(3): 826-31, 1975 Jun.
Article in English | MEDLINE | ID: mdl-168180

ABSTRACT

A selection procedure is described which permits a large number of Saccharomyces cerevisiae mutants to be screened for specific lesions in mitochondrial respiratory enzymes and the adenosine triphosphatase. The method has been used to isolate nuclear mutant strains with specific lesions in coenzyme QH2-cytochrome c reductase, cytochrome oxidase, and adenosine triphosphatase. In addition, two cytoplasmic mutants have been found whose primary defect is in cytochrome oxidase, and others have been found that show variable degrees of abnormalities in their mitochondrial translation products.


Subject(s)
Fungal Proteins/biosynthesis , Mitochondria/metabolism , Mutation , Saccharomyces cerevisiae/metabolism , Adenosine Triphosphatases/biosynthesis , Cell Nucleus/metabolism , Cytoplasm/metabolism , Electron Transport Complex IV/biosynthesis , Ethyl Methanesulfonate , Glycerol/metabolism , Manganese , Mitochondria/enzymology , Mutagens , NADPH-Ferrihemoprotein Reductase/biosynthesis , Nitrosoguanidines , Protein Biosynthesis , Saccharomyces cerevisiae/enzymology , Saccharomyces cerevisiae/isolation & purification
17.
Josanpu Zasshi ; 23(6): 97-102, 1969 Jun.
Article in Japanese | MEDLINE | ID: mdl-5194064

Subject(s)
Prenatal Care
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