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Biomedical subjects

E Ueda

Publications and source records attributed to E Ueda.

At least 127 records · Page 7Linked to original sources
PubMed1980

Effects of captopril (SQ 14, 225) on the renin-angiotensin-aldosterone system in normal rats.

High doses of captopril (SQ 14, 225) (120-160 mg/kg/day) were administered orally to normal rats, and the effects on the renin-angiotensin-aldosterone system were observed. Plasma angiotensin converting enzyme (ACE) activity was elevated significantly on the 3rd, 7th and 30th days of captopril administration. ACE activity in the lung and the kidney was significantly decreased on the 1st day then gradually increased, becoming significantly higher than that of controls by the 30th day. Plasma renin activity (PRA) was significantly elevated on the 1st day and remained at a high level until the 30th day. Renal renin content was found to be significantly lower on the 1st and 3rd days. Plasma aldosterone concentration was not affected by captopril treatment, whereas serum potassium concentration was found to be significantly lower on the 1st, 3rd and 30th days. It is suggested that besides its inhibitory action on ACE, captopril has a direct or indirect stimulating action on ACE production as well as on renin release.

Aldosterone↗
PubMed1980

Proteolytic cleavage of an activated subcomponent of the first component of rabbit complement, C1s.

When rabbit C1 purified by affinity chromatography on IgG-Sepharose 6B was chromatographed on DEAE-cellulose in the presence of ethylenediaminetetraacetate, C1s was isolated as two forms, C1s(I) and C1s(II), having different molecular weights. On the other hand, incubation of the C1 with soybean trypsin inhibitor before the chromatography resulted in the isolation of C1s(I) alone, indicating that, during the purification, C1s(II) was derived from C1s(I) by proteolytic cleavage of C1s(I) by a contaminating protease, probably plasmin [EC 3.4.21.7]. In fact, C1s(I) was completely converted to C1s(II) or a C1s(II)-like fragment by highly purified plasmin. Analysis of the polypeptide chain structures revealed that C1s(I), which consisted of H and L chains with molecular weights of 70,000 and 36,000, respectively, was converted to C1s(II) by cleavage of the H chain, since C1s(II) consisted of two chains each with a molecular weight of 37,000. This conversion proceeded without any alteration in C1 esterase activity, but was accompanied by loss of the ability to form C1r-C1s complex.

Animals↗
PubMed1980

Serum angiotensin-converting enzyme activity as an indicator of prognosis in sarcoidosis.

The relationship between the clinical course of sarcoidosis and serum angiotensin-converting enzyme (EC 3.4.15.1) activity was analyzed by observing 51 patients with sarcoidosis during a period of more than 1 yr. The patients were grouped into 3 categories irrespective of treatment: (1) sarcoid lesions in the chest disappeared within 1 yr, (2) sarcoid lesions remained for more than 1 yr with little improvement, (3) sarcoid lesions disappeared within 1 yr, but then relapsed. In group 1 (33 cases), the serum angiotensin-converting enzyme activity decreased from 35.9 +/- 2.0 to 22.0 +/- 1.3 nmol/ml/min after the chest roentgenogram cleared (P less than 0.005). In group 2 (12 cases), the mean serum angiotensin-converting enzyme activity after treatment was not significantly reduced, paralleling the lack of improvement. In group 3 (6 cases), a good correlation was observed between serum enzyme activity and clinical course. These findings indicate that serum angiotensin-converting enzyme activity is an indicator of the clinical course of sarcoidosis.

Adolescent↗
PubMed1979

Response of urinary noradrenaline excretion to reserpine administration in normal and hypertensive subjects.

Reserpine was administered in purpose to determine the "Noradrenaline store" in sympathetic nerve endings. The marked increase of urinary noradrenaline excretion was observed by reserpine 0.4 mg/day administration. Total amount of noradrenaline in urine for first three days of 0.4 mg/day of reserpine administration was considered as a good indicators of "Noradrenaline store". There was no difference of "Noradrenaline store" between normal and hypertensive subjects. The increase % of urinary noradrenaline was higher in labile hypertension than in established hypertension as well as in normal subjects. Though the relationship between "Noradrenaline store" or the increase % of noradrenaline and sympathetic nerve activity was not clear, it is suspected that the releasable noradrenaline in sympathetic nerve granule was higher in labile hypertension than in established hypertension or normal subjects.

Adult↗
PubMed1979

Purification and properties of angiotensin I-converting enzyme in human lung and its role on the metabolism of vasoactive peptides in pulmonary circulation.

Purification of angiotensin I-converting enzyme from human lung and characteristics of the enzyme was studied. Experimental pneumonitis was produced in rabbits and the change of the activity of angiotensin I-converting enzyme was studied in purpose to clarify the role of this enzyme in the metabolism of vasoactive peptides in the lung. Purification was performed using trypsin treatment, acid treatment, DE52-cellulose column chromatography, hydroxyapatite chromatography and Sephadex G-200 gel filtration. The enzyme after final step showed a single band on disc gel electrophoresis. Experimental pneumonitis was produced by injection of Complete Freund's adjuvant (acute pneumonitis) and of N-nitroso-N-methylurethane (chronic pneumonitis). In acute experiment, angiotensin I-converting enzyme activity in pulmonary tissue and in plasma was significantly decreased. In perfusion experiment, conversion of angiotensin I to angiotensin II and inactivation of bradykinin were also significantly decreased. In case of decreased activity of angiotensin I-converting enzyme in the lung, less angiotensin II will be released into systemic circulation and bradykinin will pass through the pulmonary circulation into systemic circulation, thus this may result in the decrease of systemic blood pressure.

Acute Disease↗
PubMed1978

Angiotensin I-converting enzyme in human urine.

It was demonstrated that angiotensin I-converting enzyme was excreted in human urine. The mean activity of the enzyme in normal urine was found to be 0.38 +/- 0.04 (S.E.M.) units/day (n = 18) and the enzymic activity correlated well with the concentration of the excreted sodium (r = 0.76, p less than 0.005). Urinary angiotensin I-converting enzyme was partially purified. Three different molecular weights of enzyme (greater than 400 000, 290 000 and 140 000) were demonstrated by Sephadex G-200 gel filtration. The enzymic properties of these three enzymes were identical with those of angiotensin I-converting enzyme from human lung with regard to inhibitory effects (bradykinin potentiator c and Arg-Pro-Pro), Cl- dependency, pH optimum and KM value.

Angiotensin-Converting Enzyme Inhibitors↗
PubMed1977

A semi-automated measurement of urinary catecholamines using high-speed ion-exchange column chromatography.

Semi-automated measurement of urinary catecholamines, specific for dopa, noradrenaline, adrenaline and dopamine and other metabolites has been developed. Steps included alumina extraction, separation by high-speed ion-exchange column chromatography and fluorescent development by trihydroxyindole (THI) method without interference by other fluorescent substances. Recovery, reproducibility and sensitivity were satisfactory. alpha-Methyldopa, a metabolite of alpha-methyldopa, and isoproterenol were separated completely without interfering with the measurement of noradrenaline, adrenaline and dopamine.

Adult↗