Possible involvement of superoxide dismutase in the mutagenicity of quercetin in Salmonella typhimurium strain TA98.
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Biomedical subjects
Publications and source records attributed to M Kohno.
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The relationship between the renal pathologic activity of systemic lupus erythematosus (SLE) and serum lactate dehydrogenase (LDH) was examined in 28 patients with active SLE involving only the kidney. Serum levels of total LDH, LDH1, and LDH2 were significantly higher in the patients with diffuse proliferative lupus nephritis (World Health Organization class IV) than in those with milder renal disease (classes I through III and V). Total LDH levels showed good correlations with the activity index and the total pathologic score of the renal pathologic scoring system, and with the glomerular hypercellularity and overall deposits. The elevated level of LDH was mainly due to elevated levels of its isozymes LDH1 and LDH2. These results suggest that the elevation of serum LDH levels in patients with SLE reflects the renal pathologic changes due to lupus nephritis.
Whether peripheral beta-endorphin contributes to the antihypertensive action of clonidine was examined by measuring plasma levels of beta-endorphin-like immunoreactivity (beta EpLI) after acute administration of clonidine in patients with essential hypertension. Administration of clonidine (0.225 mg) in one dose significantly lowered blood pressure, decreased heart rate and reduced the plasma level of beta EpLI and ACTH, while the placebo had no effect on blood pressure, heart rate or plasma level of beta EpLI suggesting that peripheral beta-endorphin does not play a major role in the antihypertensive action of acute clonidine administration.
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Protein phosphorylation of quiescent human skin fibroblasts was analyzed following stimulation by epidermal growth factor, fibroblast growth factor, platelet-derived growth factor, serum, or 12-O-tetradecanoyl-phorbol-13-acetate. In mitogen-treated cells, a markedly increased phosphorylation of two Mr = 43,000 proteins and two Mr = 41,000 proteins was always detected by two-dimensional gel electrophoresis. More acidic forms were the dominant species and contained phosphotyrosine, phosphoserine, and phosphothreonine, while the basic forms contained phosphotyrosine and phosphoserine. The two Mr = 41,000 proteins were structurally related to each other. All mitogens seemed to stimulate the phosphorylation of each protein with the same site specificity. Induction of the same set of phosphoproteins was observed in mitogen-stimulated rat and mouse fibroblasts as well. These stimulated phosphorylations occurred rapidly, were maximal 5 min after exposure of cells to mitogens, and diminished gradually after 30 min. Mitogen-induced phosphorylation of these proteins was correlated to the extent of mitogen-stimulated DNA synthesis. In addition, such increased protein phosphorylation was not observed in exponentially growing cells, nor in Rous sarcoma virus-transformed rat cells. Thus, phosphorylation of the Mr = 43,000 and 41,000 proteins, which represents a common and specific response of cells to mitogens, could constitute an early event involved in the control of cellular G0----G1 transition.
After horseradish peroxidase (HRP) injections into various parts of the ventral thalamic nuclear group and its adjacent areas, the distribution of labeled neurons was compared in the cerebral cortex, basal ganglia, and the brain stem. The major differences in distribution patterns were as follows: Injections of HRP into the lateral or ventrolateral portions of the ventroanterior and ventrolateral nuclear complex of the thalamus (VA-VL) produced retrogradely labeled neurons consistently in area 4 gamma (lateral part of the anterior and posterior sigmoid gyri, lateral sigmoid gyrus and the lateral fundus of the cruciate sulcus), the medial division of posterior thalamic group (POm), suprageniculate nucleus (SG) and anterior pretectal nucleus ipsilaterally, and in the nucleus Z of the vestibular nuclear complex bilaterally. Injections into the medial or dorsomedial portion of the VA-VL resulted in labeled neurons within the areas 6a beta (medial part of the anterior sigmoid gyrus), 6a delta (anterior part of ventral bank of buried cruciate sulcus), 6 if. fu (posterior part of the bank), fundus of the presylvian sulcus (area 6a beta), medial part of the nucleus lateralis posterior of thalamus and nucleus centralis dorsalis ipsilaterally, and in the entopeduncular nucleus (EPN) and medial pretectal nucleus bilaterally. Only a few neurons were present in the contralateral area 6a delta. After HRP injections into the ventral medial nucleus (VM), major labeled neurons were observed in the gyrus proreus, area 6a beta (mainly in the medial bank of the presylvian sulcus), and EPN ipsilaterally, and in the medial pretectal nucleus and substantia nigra bilaterally. Following HRP injections into the centre médian nucleus (CM), major labeled neurons were found in the areas 4 gamma, 6a beta, and the orbital gyrus ipsilaterally, and in the EPN, rostral and rostrolateral parts of the thalamic reticular nucleus, locus ceruleus, nucleus reticularis pontis oralis et caudalis and nucleus prepositus hypoglossi bilaterally. The contralateral intercalatus nucleus also possessed labeled neurons. With HRP injections into the paracentral and centrolateral nuclei, labeled neurons were observed in the gyrus proreus and the cortical areas between the caudal presylvian sulcus and anterior rhinal sulcus ipsilaterally, and in the nuclei interstitialis and Darkschewitsch bilaterally. Minor differences in the distribution pattern were observed in the superior colliculus, periaqueductal gray, mesencephalic and medullary reticular formations, and vestibular nuclei in all cases of injections.
Coronary angiography of both right and left coronary arteries, using the Sones technique, was performed during the attack of total spastic obstruction in 11 patients with clinically documented history of variant angina. None of the patients had more than 70% stenosis of organic atherosclerosis in any coronary artery and none had a history of myocardial infarction. Total spastic obstruction occurred spontaneously in 3 of 11 patients, and was provoked by ergonovine maleate in eight patients. Six patients had total spastic obstruction in the left anterior descending coronary artery, four patients had total obstruction in the right coronary artery, and one patient had total obstruction in the left anterior descending and right coronary arteries. In 7 of 11 patients, the coronary artery distal to the total spastic obstruction received collaterals from the nonspastic artery. The collaterals disappeared promptly when the spastic coronary artery was patent. These patients had ST segment elevation in the ECG during the attacks. In the remaining four patients, the spastic artery did not receive any collaterals from the nonspastic artery, associated with ST segment elevation during the attacks. These findings suggest that the brief, repetitive total occlusion of the coronary artery may stimulate the enlargement of collaterals. These collaterals may not always function to prevent the ischemia of the myocardium on the ECG.
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To examine the relationship between the urinary levels of alanine aminopeptidase (AAP) or N-acetyl-beta-D-glucosaminidase (NAG) and the advance of essential hypertension, we measured the urinary levels of these enzymes in 20 normotensive controls, 8 subjects with borderline hypertension and 40 subjects with WHO stage I and stage II essential hypertension. The urinary level of NAG in stage II hypertensives was higher than that in the normotensives, and borderline or stage I hypertensives (p less than 0.01). Systolic blood pressure and the urinary level of NAG was positively correlated in hypertensives (rs = 0.43, p less than 0.01). The urinary level of NAG was correlated inversely with renal blood flow (rs = -0.61, p less than 0.01). The urinary level of AAP in stage II hypertensives was also higher than that in the normotensives (p less than 0.01) or stage I hypertension (p less than 0.01), but the urinary AAP level was not significantly correlated with systolic blood pressure or renal blood flow in hypertension.
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To compare two expressions of the time constant for ventricular relaxation, 39 patients with various heart diseases (six normal, six angina pectoris [AP], 13 myocardial infarction [MI], eight hypertrophic cardiomyopathy [HCM], and six congestive cardiomyopathy [CCM]) were studied. One time constant was obtained by the method of Weiss et al. (T1) and the other was the ratio of left ventricular pressure at peak (-) dP/dt (Pm) to peak (-) dP/dt (T2). The deviation of T2 from T1 was expressed as 100 X (T2 - T1)/T1 (delta %). In normal subjects, T1 was nearly equal to T2 (32 +/- 3 and 32 +/- 6 msec, respectively), resulting in a low value of delta (-1 +/- 9). However, delta values in AP (20 +/- 23, p less than 0.05), MI (24 +/- 26, p less than 0.05), HCM (37 +/- 21, p less than 0.001), and CCM (46 +/- 24, p less than 0.001) were significantly higher than in normal subjects. Thus T1, T2, or delta separated the patient groups from the control subjects, and there were significant differences between T1 and T2 among the types of heart disease.
Adult T-cell leukemia-associated membrane antigen (ATLMA) expressed on the surface of living ATL virus (ATLV)-carrying cells was investigated by an indirect membrane immunofluorescence method using natural antibodies to ATLV in human sera. All the ATLV-positive cell lines tested that had cytoplasmic ATL-associated antigen (ATLA) detectable in acetone-fixed cell smears were also positive for ATLMA, but ATLMA was not detected in any ATLV-negative cell lines. The frequencies of ATLA- and ATLMA-bearing cells in seven cell lines tested were roughly parallel. The frequency of expression of both ATLMA and ATLA in cultures of MT-1 cells increased in the presence of 5-iodo-2'-deoxyuridine. All human sera having ATLA antibody had ATLMA antibody and the titers of the two were similar in most of the sera. The anti-ATLMA titers of human sera determined by using an ATLV-bound non-ATL T-cell line as antigen were also similar to the anti-ATLA titers. Absorption of anti-ATLMA-positive sera with living MT-2 cells, in which almost 100% of the cells express ATLA and ATLMA, caused parallel decreases in the anti-ATLA and anti-ATLMA titers. Analysis of the 125I-labeled surface of MT-2 cells by immunoprecipitation with anti-ATLMA-positive human serum followed by gel electrophoresis revealed that p19, p24, p28, and p46 polypeptides were specifically precipitated. These data suggest that ATLMA on the cell surface is not distinguishable from ATLA in the cytoplasm.