RESUMO
A new type of medical information system named Problem Mapping System (P-Map) has been developed, which aids physicians with solving patients' problems. With this system, physicians can define the problems of in-patients, monitor their progress clearly, and share information efficiently. In P-map, a list of problems, such as disease names, can be set for each inpatient easily. The progress of each problem is clearly shown using progress lines on a time axis. Physicians can save the Subjective Objective Assessment Plan (SOAP) notes which are linked to each problem. At the final stage of patient care, a discharge summary can be made easily. With the aid of this system, the quality of patient care is improved due to the following: (1) physicians can make the best decision; (2) medical staff in the same team can provide the best medical treatment; (3) evaluation of each medical treatment is easy; (4) saved data can be used effectively for education and research; (5) the system can improve cooperation with other medical institutes by providing discharge summary information which can be distributed using e-mail; and (6) the system can improve patients' understanding for the purpose of informed consent by providing clear and well organized information to patients.
Assuntos
Sistemas Computacionais , Sistemas de Informação Hospitalar/organização & administração , Qualidade da Assistência à Saúde/organização & administração , Humanos , Japão , Sistemas Computadorizados de Registros Médicos/organização & administração , Registros Médicos Orientados a ProblemasRESUMO
Fyn-deficient mice produced by inserting the beta-galactosidase gene (lacZ) into the fyn gene locus were tested in a radial maze, an open field and an elevated plus-maze. In the radial maze, the homozygous Fyn-deficient (fynz/fynz) mice showed no impairment in spatial learning, although they showed a stronger avoidance tendency for those arms located closer to the experimenter during pretraining (adaptation). In the open-field test, the fynz/fynz mice defecated more frequently in the bright condition than did the +/fynz mice, and they were less active during the first 10-min test period than the +/fynz mice. In addition, the temporal pattern of locomotor activity for fynz/fynz mice was altered by changing the illumination while the pattern for +/fynz mice remained relatively unchanged. Scores reflecting the fear-response in the elevated plus-maze were higher in the fynz/fynz mice. These results indicate that Fyn deficiency increased fear-response, but did not impair spatial learning in the radial maze. It is suggested that we should take account of effects of emotional factors in the learning experiment using mutant mice.
Assuntos
Comportamento Animal/fisiologia , Medo , Aprendizagem em Labirinto/fisiologia , Atividade Motora/fisiologia , Animais , Camundongos , Camundongos Endogâmicos C57BL , Camundongos Mutantes , Fosfotransferases/metabolismo , Fatores SexuaisRESUMO
An electron spin resonance (ESR) spin trapping technique was applied to determine the generation of superoxide anions in submitochondrial particles prepared from the ischemic heart. Ischemia was produced in the dog heart by occlusion of the circumflex coronary artery for 60 min. Mitochondria were prepared from ischemic and non-ischemic regions of myocardial tissue. To avoid the influence of superoxide dismutase located in the mitochondrial matrix, submitochondrial particles were utilized instead of whole mitochondria. Using the spin trap 5,5'-dimethyl-1-pyrroline-N-oxide (DMPO), the kind of active oxygen species generated from the mitochondrial electron transport system was determined from ESR spectrum. The relative signal intensity of the DMPO-superoxide anion adduct was found to be high in submitochondrial particles prepared from subsarcolemmal mitochondria obtained from the ischemic region, as compared with those from the non-ischemic region.
Assuntos
Doença das Coronárias/metabolismo , Espectroscopia de Ressonância de Spin Eletrônica , Mitocôndrias Cardíacas/química , Superóxidos/análise , Animais , Bovinos , Doença das Coronárias/patologia , Óxidos N-Cíclicos , Radicais Livres , Mitocôndrias Cardíacas/ultraestrutura , Frações Subcelulares/química , Succinatos/metabolismo , Ácido Succínico , Superóxido Dismutase/análiseRESUMO
The ultrastructure and membrane fluidity were examined in two fractions of myocardial mitochondria isolated from the ischemic region following occlusion of the circumflex coronary artery of the dog. Transmission electron microscopy revealed that 60 min of ischemia produced more structural change in the subsarcolemmal mitochondria than in the intermyofibrillar mitochondria. Changes in the dynamic properties of the mitochondrial membranes were examined using the spin labeling technique with electron spin resonance (ESR). From the ESR spectra, the membrane fluidity of the subsarcolemmal mitochondria was found to decrease significantly after ischemic injury, whereas no difference was observed in intermyofibrillar mitochondria. In addition, a negative correlation between the increase of order parameter S and dysfunction of respiratory responses of subsarcolemmal mitochondria was found. These results suggest that the two fractions of mitochondria in the myocardium showed different responses to acute ischemic injury. The damage to mitochondrial membranes occurred during the period of ischemia.
Assuntos
Doença das Coronárias/patologia , Espectroscopia de Ressonância de Spin Eletrônica , Mitocôndrias Cardíacas/patologia , Animais , Cães , Membranas Intracelulares/ultraestrutura , Fluidez de Membrana , Frações SubcelularesRESUMO
Mitochondria may be a source of molecules that activate complement during ischemic injury to myocardium, providing therewith a stimulus for infiltration of polymorphonuclear leukocytes. To identify specific molecules that activate the classical complement pathway, detergent lysates of canine cardiac mitochondria were fractionated by polyacrylamide gel electrophoresis and transferred electrophoretically to nitrocellulose paper (NCP). The NCP replicas of the gels were incubated with isolated C1q and fresh sera as a source of complement, washed briefly, and overlaid with sensitized sheep erythrocytes (RBC) in agarose. A cluster of four to six molecules between 45 and 53 kDa as well as four others, 34, 30, 26, and 23 kDa, consumed complement thereby preventing complement-mediated lysis of sensitized sheep RBC in the agarose overlay. Additional molecules reactive with C1 were identified by their ability to bind isolated human C1q and to serve as assembly sites for later acting complement components. Sites of localization of complement were demonstrated by incubating NCP replicas of fractionated mitochondria with antisera specific for C1q, C3, C5, and C9, followed by peroxidase-conjugated anti-immunoglobulin and substrate. A total of 12 C1q binding molecules ranging in size from 67 kDa to 23 kDa, which can fix later acting complement components, were identified. At least two of these reacted with antisera prepared against canine cardiac lymph collected in the first 3-4 hours after a 45-minute coronary artery occlusion. These studies present direct evidence that specific molecules, released from subcellular fractions of myocardial cells rich in mitochondria, can activate the complement cascade.
Assuntos
Enzimas Ativadoras do Complemento/imunologia , Ativação do Complemento , Complemento C1/imunologia , Via Clássica do Complemento , Doença das Coronárias/imunologia , Mitocôndrias Cardíacas/imunologia , Animais , Sítios de Ligação , Enzimas Ativadoras do Complemento/análise , Complemento C1/análise , Complemento C1q , Testes de Fixação de Complemento/métodos , Cães , Eletroforese em Gel de Poliacrilamida/métodos , Cobaias , Humanos , Linfa/imunologia , Mitocôndrias Cardíacas/análise , Peso Molecular , Proteínas Musculares/análise , Proteínas Musculares/imunologiaRESUMO
To evaluate whether ischemic myocardium releases molecules that react with the first component of complement, we studied cardiac lymph from eight dogs before and at intervals after coronary artery occlusion and reperfusion. Before occlusion, the dogs were injected intravenously with radiolabeled human C1q. Labeled C1q could be detected in the cardiac lymph within minutes following injection. Rabbit antisera, prepared against substances precipitated from postreprefusion cardiac lymph by anti-human C1q, also reacted with specific constituents of isolated cardiac sarcoplasmic reticulum and mitochondria. To evaluate whether mitochondria are the source of these C1q-binding proteins, we isolated intramyofibrillar and subsarcolemmal mitochondria from canine heart and incubated sonicates of these with purified C1q, immobilized on nitrocellulose. Molecules bound to the immobilized C1q were removed with 0.1% sodium dodecyl sulfate, fractionated under reducing conditions by polyacrylamide gel electrophoresis, and transferred electrophoretically to nitrocellulose paper. Antisera prepared against postreperfusion lymph reacted with a 31,000-32,000-dalton protein in these nitrocellulose paper replicas. Since this protein originates from mitochondria, binds to C1q, and is recognized by antibodies made against postreperfusion lymph, this protein is likely to be one of the subcellular constituents that, upon release from ischemic cells, activates the complement cascade. To evaluate the clinical relevance of these observations, we tested sera from 53 patients obtained 48-72 hours after hospitalization for suspected myocardial infarction.(ABSTRACT TRUNCATED AT 250 WORDS)
Assuntos
Enzimas Ativadoras do Complemento/imunologia , Ativação do Complemento , Complemento C1/imunologia , Doença das Coronárias/imunologia , Receptores de Hialuronatos , Linfa/imunologia , Glicoproteínas de Membrana , Miocárdio/metabolismo , Receptores de Complemento/fisiologia , Animais , Proteínas de Transporte/metabolismo , Enzimas Ativadoras do Complemento/metabolismo , Complemento C1/metabolismo , Complemento C1q , Cães , Humanos , Proteínas Mitocondriais , Infarto do Miocárdio/imunologiaRESUMO
Male Wistar rats received intraperitoneal injections of adriamycin (4 mg/kg body weight/day) and/or riboflavin-butyrate (20 mg/kg body weight/day) for 6 consecutive days. Cardiac mitochondria were then prepared for our present experiment. The combined use of riboflavin-butyrate with adriamycin was evaluated for reduction of lipid peroxide formation in rat cardiac mitochondria. In order to find the mechanism of the effect of riboflavin-butyrate, the glutathione peroxidase-glutathione reductase system was examined. Adriamycin reduced the glutathione reductase activity in rat cardiac mitochondria, but did not affect the glutathione peroxidase activity. The mitochondrial content of flavin adenine dinucleotide, a prosthetic group of glutathione reductase, was greatly reduced and apoprotein of glutathione reductase also decreased. The administration of riboflavin-butyrate with adriamycin increased flavin adenine dinucleotide and glutathione reductase activity. These results suggest that exogenous administration of riboflavin-butyrate is capable of reducing lipid peroxide by both enzymatic detoxification through glutathione reductase and non-enzymatic detoxification due to direct reaction with lipid peroxide.