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Y Bando

Publications and source records attributed to Y Bando.

102 records · Page 6Linked to original sources
PubMed1985

Distribution of cathepsins B and H in rat tissues and peripheral blood cells.

The concentrations of cathepsins B and H in various tissues and peripheral blood cells of rats were determined by means of sensitive immunoassays. The minimum detectable amounts of cathepsins B and H were 30 pg and 20 pg/assay, respectively, and the presence of endogenous thiol proteinase inhibitors did not interfere with the immunoassays. Cathepsin B was found at high levels in the kidney, vagina, spleen, and adrenal gland, and cathepsin H at high levels in the kidney, vagina, liver, lung, and spleen. Low levels of cathepsins B and H were present in the heart, skeletal muscle, and testis. The ratios of cathepsins B and H in various organs were different: the brain and adrenal gland contained much higher levels of cathepsin B than of cathepsin H, whereas the lung and liver contained higher levels of cathepsin H than of cathepsin B. In several organs such as the kidney, spleen, liver, and lungs, the level of cathepsins B plus H was much higher than that of thiol proteinase inhibitors (TPI-alpha + TPI-beta), whereas in tissues containing large amounts of TPI-alpha, such as the skin, esophagus and stomach, the level of inhibitors was higher than that of cathepsins B plus H. Of the peripheral blood cells tested, macrophages had the highest contents of cathepsins B and H, and so their level of cathepsins B plus H was much higher than that of TPI-alpha plus TPI-beta, whereas lymphocytes and neutrophils contained comparable amounts of proteinases and inhibitors.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1985

Different immunolocalizations of cathepsins B, H, and L in the liver.

Different localizations of cathepsin B, H, and L in normal rat liver were revealed immunohistochemically with anticathepsin Fab'-horseradish peroxidase conjugates. Staining of cathepsin B was strong in the periportal sinusoids, possibly in Kupffer cells; and weaker in panlobular hepatocytes. Staining of cathepsin H was strong in panlobular hepatocytes, especially in the periphery of the cytoplasm, possibly representing the peribiliary dense bodies; and weaker in periportal sinusoidal cells, possibly Kupffer cells. Staining of cathepsin L was strongest in centrilobular hepatocytes and weaker in periportal sinusoidal cells, possibly Kupffer cells. These findings, revealed for the first time in the present study, show that the histologic and intracellular localizations of the three cathepsins are different, suggesting that they have different roles in degradation of exogenous and endogenous proteins.

Animals↗
PubMed1984

Amino acid sequence of rat epidermal thiol proteinase inhibitor.

The complete amino acid sequence of rat epidermal thiol proteinase inhibitor was determined. The unique 103-residue sequence was derived by analysis of two peptides generated by limited proteolysis of the native inhibitor with Staphylococcus aureus V8 protease and of three cyanogen bromide fragments. The protein has a high degree of sequence homology to either rat liver or human leucocyte inhibitor but is not identical and may represent a new type of low molecular weight thiol proteinase inhibitors.

Amino Acid Sequence↗
PubMed1984

Mechanism of postmortem autolysis of skeletal muscle.

Male Wistar rats were treated with the carboxyl, thiol, and serine protease inhibitors, pepstatin, Ep-475[L-trans-epoxysuccinyl-leucylamide(3-methyl) butane; E-64-c], and chymostatin. Then the femoral muscles of these rats and control animals were used for preparation of myofibril proteins. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis was used to analyze the degradation of these myofibril proteins with time (day) after death. The protease activities of the muscle were also measured. Tropomyosin was degraded most rapidly, followed by the heavy chain of myosin, alpha-actinin, and light chains of myosin (L1 and L2). Actin and troponin-T were degraded slowly, still remaining unchanged 2 weeks after death. The degradation of protein was not inhibited by pepstatin but was inhibited strongly by Ep-475 and very strongly by chymostatin. Chymostatin inhibited degradation of all components except alpha-actinin more strongly than Ep-475. Data on enzyme activities were consistent with these findings. These results suggest that after death the components of myofibrils are degraded with various proteases at various rates depending on their properties or their structure and that the proteases involved in the degradation show some specificity.

Animals↗
PubMed1984

Different tissue distributions of two types of thiol proteinase inhibitors from rat liver and epidermis.

The concentrations of two types of endogenous inhibitors of thiol proteinases were determined in soluble extracts of various rat tissues by means of a sensitive enzyme immunoassay method, which consisted of solid-phase immobilized anti-rat liver inhibitor or anti-rat epidermal inhibitor and antibodies labeled with horseradish peroxidase. The minimum detectable amounts of inhibitors from liver and epidermis were 30 pg and 3 pg/assay, respectively. The tissue distributions of the epidermal and liver-type inhibitors were found to differ. The liver-type inhibitor was found to be widely distributed in various tissues at levels of 76-420 ng/mg protein, whereas the epidermal-type inhibitor was found at high levels in the skin, tongue, esophagus, stomach, intestine, and vagina, but at quite low levels in other tissues tested.

Animals↗
PubMed1984

Increases in cathepsins B and L and thiol proteinase inhibitor in muscle of dystrophic hamsters. Their localization in invading phagocytes.

In dystrophic hamsters, increases in the levels of cathepsin B plus L and thiol proteinase inhibitor were marked in skeletal muscle, but only slight in heart muscle. The lysosomal hydrolases did not increase in parallel in dystrophic muscle: cathepsin B plus L and beta-glucuronidase increased, but cathepsin C and acid phosphatase did not. In immunohistochemical studies with antibodies against rat liver cathepsin B and thiol proteinase inhibitor, the proteinase and inhibitor were both stained in phagocytes, chiefly macrophages, but not in muscle cells, indicating that the increases in cathepsin B plus L and thiol proteinase inhibitor in dystrophic muscle are due to their presence in invading phagocytes. The levels of cathepsin B plus L, beta-glucuronidase and thiol proteinase inhibitor in isolated peritoneal macrophages were 50 to 180 times higher than those in skeletal muscle, but the levels of acid phosphatase and cathepsin C were only about 10 to 30 times those in skeletal muscle. Plots of the cathepsin B plus L activities versus the level of thiol proteinase inhibitor in homogenates of tissues of various animals showed an exponential rather than a linear relation between the two activities, suggesting that the syntheses of the proteinases are higher than that of the inhibitor in phagocytes invading dystrophic muscle.

Animals↗
PubMed1983

[Experimental induction of atherosclerosis in guinea pigs fed a cholesterol and vitamin D2-rich diet].

Atherosclerotic lesions of aorta and arteries were induced in guinea pigs fed a diet supplemented with 1% cholesterol and vitamin D2 (0.75 million IU/kg of diet) for 6 weeks. Histopathological observation revealed intimal proliferation and calcification of the intima and media, but no atheroma was present at the sites of arterial injury. However, the biochemical findings revealed accumulation of cholesterol, mainly esterified, and calcium in the aorta. Significant correlation between the calcium and phosphorus contents in the aorta indicates the presence of a probable calcium-phosphate complex. Synergism for the induction of atherosclerotic lesions was shown between high cholesterol and excess vitamin D2. Sodium 4-(hexadecylamino)benzoate (cetaben) (90 mg/kg/day, p.o.) and trisodium ethane-1-hydroxy-1,1-diphosphonate (EHDP) (5 mg/kg/day, s.c.) inhibited the development of atherosclerotic lesions induced in this manner. These effects were associated with a significant reduction of serum and aortic cholesterol levels and a significant elevation of HDL-cholesterol levels caused by cetaben, and a significant reduction in aortic calcium caused by EHDP. These two drugs and clofibrate, however, had no significant effect on the regression of pre-established atherosclerotic lesions.

4-Aminobenzoic Acid↗
PubMed1982

Effects of clonidine and guanfacine on drinking and ambulation in spontaneously hypertensive rats.

Present experiment was undertaken to compare the effects of clonidine and guanfacine on water drinking behavior and ambulatory activity in spontaneously hypertensive rats (SHR). Equipotent hypotensive doses of clonidine and guanfacine, 150 micrograms/kg and 1500 micrograms/kg, respectively, given twice a day at 8:00 and 20:00, produced a triphasic pattern of behavioral changes; initial increase in water drinking and ambulation during the light period, decrease in water intake and ambulation at the beginning of the dark period, and a second increase in water drinking and ambulation at the end of the dark period. Guanfacine treated SHR showed less change in water drinking behavior and ambulation than the clonidine treated SHR.

Animals↗
PubMedDate not supplied

Troglitazone combination therapy in obese type 2 diabetic patients poorly controlled with alpha-glucosidase inhibitors.

The efficacy and safety of treatment with troglitazone combined with an alpha-glucosidase inhibitor, in obese type 2 diabetic patients who were previously administered alpha-glucosidase inhibitors alone, in improving glycaemic control and reducing insulin resistance were studied. Obese type 2 diabetic patients, poorly controlled with alpha-glucosidase inhibitors, were randomized to receive either oral troglitazone 200 mg twice daily (22 patients: group A) or a placebo (20 patients: group B) in addition to their usual alpha-glucosidase inhibitor. In group A, significant decreases in the mean levels of haemoglobin A1c and basal plasma insulin levels were observed 6 months after the start of combined therapy. Serum triglyceride levels significantly decreased but serum lactic acid dehydrogenase and body weight significantly increased. New systemic oedema was observed in six patients. Combined therapy with troglitazone and alpha-glucosidase inhibitors may be effective for diabetic metabolic abnormalities, although the potential development of adverse effects such as body-weight gain and systemic oedema demands vigilance.

Acarbose↗