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1.
FEBS Lett ; 364(3): 293-7, 1995 May 15.
Artigo em Inglês | MEDLINE | ID: mdl-7538936

RESUMO

BDV naturally infects horses and sheep, and causes sporadic neurological disease. Serological evidence suggests an association of BDV, or a related virus, with specific psychiatric diseases in humans. Here, by using a nested RT-PCR technique, we demonstrate that human BDV RNA is present in the PBMC of psychiatric patients. In an examination of a total of 60 patients from 5 wards of a hospital in Japan, the detection rate differed within each ward, ranging from 8% to > 50% (37% on the average). Of particular note was the finding that the human derived BDV sequences, which included deleted forms in about 23% of the positive samples, were slightly different from those derived from horse BDV. These results suggest urgent consideration of the measures to be taken to cope with the effects of blood transfusion. In addition, the detection of a high level of BDV in the PBMC of patients will help our understanding of the pathogenesis in the disease.


Assuntos
Vírus da Doença de Borna/genética , Leucócitos Mononucleares/virologia , Transtornos Mentais/virologia , RNA Viral/sangue , Anticorpos Antivirais/sangue , Sequência de Bases , Southern Blotting , Vírus da Doença de Borna/imunologia , Etídio , Humanos , Japão , Dados de Sequência Molecular , Reação em Cadeia da Polimerase , RNA Viral/química , DNA Polimerase Dirigida por RNA , Sequências Repetitivas de Ácido Nucleico , Coloração e Rotulagem
2.
Neurosci Lett ; 66(1): 39-42, 1986 May 06.
Artigo em Inglês | MEDLINE | ID: mdl-3714113

RESUMO

The formation of the capillary-glial complex of developing rat brain ranging in age from embryonic day 16 (E16) rats to birth, which occurs at E20, and in the postnatal rats to day 56 (P56) was determined by measuring the horseradish peroxidase (HRP) activity, which was exogenously injected and penetrated within the brain. The activity of glutathione S-transferases (GSTs) which are located exclusively in astroglial cells was also determined. HRP penetrated into and resided within the central nervous system until birth, although after this age the tracers were rarely observed to be included. On the other hand, GST activity was first detected at E18, and after P5 it increased remarkably. The functional significance of astroglial cells located at the blood-brain or blood-ventricle interface is considered, and we suggest that the ontogenetic development of a blood-brain barrier is compatible with the corresponding appearance of GST.


Assuntos
Astrócitos/fisiologia , Barreira Hematoencefálica , Glutationa Transferase/metabolismo , Animais , Astrócitos/enzimologia , Histocitoquímica , Peroxidase do Rábano Silvestre , Imunoquímica , Ratos/embriologia , Ratos/crescimento & desenvolvimento
3.
Neurosci Lett ; 66(2): 131-4, 1986 May 15.
Artigo em Inglês | MEDLINE | ID: mdl-3725177

RESUMO

Indirect immunocytochemical staining with antisera raised against purified glutathione S-transferase (GST) was employed to analyse astrogliogenesis in rat brain from embryonic day-16 (E16) rats to birth (which occurs at E20) and in postnatal rats to day 56 (P56). Some GST-positive cells are already recognized at E16 in the choroid plexus and pial surface. At a slightly older age--between E18 and birth--GST-positive cells are located in the ventricular zone. After this age, GST-positive cells are easily recognized in the subventricular zone and in astroglial cells of white and gray matter. On the other hand, neurons and oligodendroglial cells have never been stained all through the ages examined.


Assuntos
Animais Recém-Nascidos/metabolismo , Encéfalo/enzimologia , Feto/metabolismo , Glutationa Transferase/metabolismo , Animais , Astrócitos/enzimologia , Encéfalo/embriologia , Encéfalo/crescimento & desenvolvimento , Ventrículos Cerebrais/enzimologia , Plexo Corióideo/enzimologia , Histocitoquímica , Imunoquímica , Pia-Máter/enzimologia , Ratos , Ratos Endogâmicos , Distribuição Tecidual
4.
J Nutr Sci Vitaminol (Tokyo) ; 31(5): 481-90, 1985 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-3935762

RESUMO

The erythrocytes from the vitamin E-deficient rats showed no changes in comparison with the erythrocytes from the vitamin E-supplemented rats in lipid peroxides, membrane fluidity, lipid composition, and activities of defensive enzymes against the lipid peroxide formation. Once erythrocytes from vitamin E-deficient rats were exposed to H2O2, the erythrocyte membrane fluidity was significantly reduced, which was presumed to be accompanied by an increase in the hemolysis and lipid peroxide formation. Large decreases in arachidonic acid and phospholipid were also observed. These findings suggest that the reduced membrane fluidity is due to the loss of phospholipid from the erythrocytes, and raises the possibility that the reduced fluidity might contribute to the peroxidative hemolysis of the vitamin E-deficient rat erythrocytes.


Assuntos
Membrana Eritrocítica/fisiologia , Deficiência de Vitamina E/sangue , Animais , Ácido Araquidônico , Ácidos Araquidônicos/sangue , Polarização de Fluorescência , Peróxido de Hidrogênio/farmacologia , Peróxidos Lipídicos/sangue , Masculino , Fluidez de Membrana , Lipídeos de Membrana/sangue , Fosfolipídeos/sangue , Ratos , Ratos Endogâmicos
5.
Hokkaido Igaku Zasshi ; 60(5): 625-34, 1985 Sep.
Artigo em Japonês | MEDLINE | ID: mdl-4077016

RESUMO

Transfer of mitochondrial protoheme to apocytochrome b5 in vitro was accomplished in a reconstitution system consisting of isolated mitochondria (donor) and apocytochrome b5 (acceptor), which required the existence of cytosol. Properties of formed cytochrome b5 were confirmed by its absorption spectra and the function as NADH-cytochrome c reductase. The content of formed cytochrome b5 was dependent on reaction time and the concentration of mitochondrial protoheme, apocytochrome b5, and cytosolic protein. This heme transfer protein was purified to homogeneity and identified with glutathione S-transferases (GSTs), by their same elution patterns in column chromatographies and the same degree of inhibited activities on the immunotitration study. Double immunodiffusion analysis revealed this protein to be GST-C2 (Yb' Yb'). These observations lead to the conclusion that Yb' subunit of GST located in the cytosol of rat liver stimulates the transfer of mitochondrial protoheme to apocytochrome b5, which indicates that GST has an unrecognized function as yet, involving on the biosynthesis of microsomal cytochrome b5.


Assuntos
Proteínas de Transporte/isolamento & purificação , Grupo dos Citocromos b/biossíntese , Glutationa Transferase/isolamento & purificação , Hemeproteínas/isolamento & purificação , Microssomos Hepáticos/enzimologia , Animais , Citocromos b5 , Heme/metabolismo , Proteínas Ligantes de Grupo Heme , Ratos , Ratos Endogâmicos
6.
Hokkaido Igaku Zasshi ; 60(6): 893-7, 1985 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-4085969

RESUMO

Modulation of acyl-CoA: cholesterol acyltransferase (ACAT; EC 2.3.1.26) activity by different diets or coincubation with serum lipoproteins was studied in rabbit liver and intestinal mucosa microsomal preparations. The total amount of cholesterol in the serum lipoproteins, hepatic cells and small intestine mucosa changes in response to changes in cholesterol dietary period. The concentration of either esterified or unesterified cholesterol present in liver and small intestine microsomes remains within a relatively narrow range, whereas the activity of ACAT increased remarkably. In order to clarify the mechanism by which the activity of ACAT was stimulated, liver microsomes of normal rabbits were preincubated with lipoproteins. All lipoprotein fractions stimulated microsomal ACAT activity, among which the intermediate lipoprotein (IDL) showed most effective. These results suggest that ACAT activity in microsomes was affected not only by the amount of microsomal cholesterol, but also by an extra-microsomal soluble protein such as lipoproteins.


Assuntos
Colesterol na Dieta/administração & dosagem , Intestino Delgado/enzimologia , Microssomos Hepáticos/enzimologia , Esterol O-Aciltransferase/metabolismo , Animais , Mucosa Intestinal/enzimologia , Lipoproteínas/sangue , Coelhos
10.
J Neurochem ; 50(1): 163-6, 1988 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-3335840

RESUMO

The changes of glutathione S-transferase activity were investigated using rat brain astroglioma C6 cells that were synchronized at different phases of the cell cycle. The enzyme showed two significant activity peaks at G2 and G1 phases. Furthermore, when C6 glioma cells were exposed to a culture medium supplemented with specific glutathione S-transferase inhibitors, ethacrynic acid and caffeic acid, cell growth was remarkably suppressed. These results suggest that glutathione S-transferases may be closely related to the mechanism of cell proliferation.


Assuntos
Ciclo Celular , Glioma/enzimologia , Glutationa Transferase/metabolismo , Animais , Ácidos Cafeicos/farmacologia , Divisão Celular/efeitos dos fármacos , Ácido Etacrínico/farmacologia , Glutationa Transferase/antagonistas & inibidores , Interfase , Ratos , Células Tumorais Cultivadas
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