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Biomedical subjects

T Kokubu

Publications and source records attributed to T Kokubu.

At least 145 records · Page 8Linked to original sources
PubMed1983

Characterization and immunohistologic demonstration of angiotensin-converting enzyme in human renal cell carcinoma.

Angiotensin-converting enzyme (ACE, EC 3.4.15.1) was demonstrated in the tissue of human renal cell carcinoma and its cultured cells by immunofluorescence and immunohistochemistry using a specific rabbit antibody to human kidney ACE. The biochemical properties of the partially purified enzyme from the tumor tissue were identical with the pure enzyme from normal kidney with respect to Km, optimal pH, chloride ion activation and heat sensitivity. Catalytic activities of tumor and normal kidney enzymes were similarly inhibited by an ACE inhibitor, captopril, and by the antibody to human kidney ACE. However, double immunodiffusion analysis showed spur-forming immunoprecipitin bands between the tumor and normal kidney enzyme. These data suggest that human renal cell carcinomas have a new isozyme of ACE differing in part immunologically from the enzyme of normal kidney.

Adenocarcinoma↗
PubMed1982

Plasma lipids and lipoproteins in Japanese male patients with coronary artery disease and in their relatives.

Plasma cholesterol (CH), triglyceride (TG) and high density lipoprotein cholesterol (HDL-C) were measured in 92 consecutive Japanese male subjects undergoing diagnostic coronary cineangiography. Sixty-nine of them were classified as having coronary artery disease (CAD), the remaining 23 subjects were classified as having normal coronary arteries (NCA). The CAD group had significantly lower HDL-C and higher TG levels than the NCA group. However, there was no significant difference in plasma CH between the two groups. First-degree relatives of the CAD patients were also investigated. The male blood relatives of the CAD patients also had significantly lower HDL-C and higher TG levels than the non-blood male relatives and healthy control males. The female blood relatives, however, showed no significant differences from the non-blood female relatives and the healthy control females in plasma CH, TG and HDL-C levels. These results suggest that low HDL-C and hypertriglyceridemia are the prevalent coronary risk factors, rather than hypercholesterolemia, in a population with a low fat intake such as the Japanese, and that these lipid abnormalities are related to sex and genetic factors.

Adult↗
PubMed1982

Biochemical and immunological studies of angiotensin converting enzymes from human, bovine, dog, hog, rabbit, rat and sheep kidneys.

1. Molecular and kinetic properties of angiotensin converting enzymes from seven different species' kidneys were similar concerning apparent molecular weight, heat sensitivity, Km value, optimum pH, activation by chloride ion, and inhibition by specific converting enzyme inhibitors (captopril and SA 446). 2. Rabbit antibody against pure human kidney enzyme cross-reacted partially with each animal kidney enzyme except for the rabbit enzyme. Antigenic determinants of animal enzymes were variable from species to species and differed from those of the human enzyme in extent and specificity.

Angiotensin-Converting Enzyme Inhibitors↗
PubMed1982

Effect of prazosin on serum lipids.

On the premise that serum lipids may be correlated with the increased mortality from coronary heart disease seen in Japan despite successful antihypertensive therapy, we undertook an open, noncomparative study to determine the effect of prazosin on serum lipid. All patients were adults (mean age of 59, with a range of 45 to 72), and all had a sitting blood pressure greater than 160 mm Hg systolic or 90 mm Hg diastolic. After a stabilization period of 2 to 4 weeks, prazosin was started at 0.5 mg t.i.d. This dose was maintained for 1 week and was then titrated upwards to achieve optimal antihypertensive effect. Maximum dose permitted was 12 mg/day. All patients were treated for at least 12 weeks. Concomitant therapy was allowed in patients who had been stabilized on other drugs prior to entry into the study. At the end of 12 weeks of therapy, prazosin (at an average dose of 4.5 mg) had lowered blood pressure by an average of 10/9 mm Hg in the sitting position, 11/7 mm Hg in the supine position, and 19/13 mm Hg in the standing position. Pulse rate did not change. Total cholesterol and triglycerides were essentially unchanged, and LDL and VLDL decreased by 4.5%. However, high density lipoprotein (HDL) cholesterol increased by 12.5%. These changes were statistically significant and yielded an increase of 20.3% in the cholesterol ratio. No side effects were noted in any patient, and none of the patients discontinued therapy during the study. This is an ongoing study, in which 14 patients have so far completed the 12 weeks of therapy. On the basis of these preliminary results, prazosin would seem to be an effective and safe antihypertensive agent with considerable favorable effects on serum lipids.

Aged↗
PubMed1982

Is captopril effective in primary pulmonary hypertension?

Several vasodilating agents have been used for the treatment of primary pulmonary hypertension (PPH). However, no effective therapy is currently available for this distressful disease. We tried to use an angiotensin-I converting enzyme inhibitor, captopril, for one woman suffering from PPH. Her initial treatment with furosemide, digoxin and spironolactone had shown little effect. Further administration of captopril improved her clinical condition from NYHA IV to II and made it possible to treat her at our out-clinic. No adverse effect has been found. We would like to appreciate captopril as one of the effective drugs in the treatment of PPH.

Captopril↗
PubMed1982

Increased urinary excretion of angiotensin converting enzyme in patients with renal diseases.

We measured the activity of angiotensin converting enzyme (ED 3.4.15.1) in urine samples from normal subjects and patients with nephrotic syndrome and chronic glomerulonephritis. Urinary excretion of angiotensin converting enzyme in patients with nephrotic syndrome (1.58 +/- 0.50 (SD) units/day; n = 15) and chronic glomerulonephritis (1.01 +/- 0.45 units/day; n = 12) was significantly increased compared with normal subjects (0.38 +/- 0.10 units/day; n = 18). It was demonstrated that a high molecular weight form of the enzyme (more than 400000) was mainly excreted in urines from patients with nephrotic syndrome. After trypsin treatment, this form was altered to a low molecular weight form (290000). These two different forms of urinary angiotensin converting enzyme were compared with the enzyme purified from human kidney, and found to be identical with respect to Km values (2 mmol/l), pH optimum (pH 8.3), chloride ion dependency (0.8 mol/l), inhibitory effect of captopril (I50, 21 nmol/l), and behavior towards antiserum to human kidney angiotensin converting enzyme.

Adolescent↗
PubMed1982

Isolation of inactive renin from human plasma and its activation by proteolytic enzymes.

A completely inactive renin was isolated from normal human plasma by DEAE-Sepharose column chromatography, 70% ammonium sulfate precipitation and Blue-Sepharose column chromatography. This preparation had a specific activity of 122 ng ANG I/mg protein/h, when activated by trypsin. The inactive renin had an apparent molecular weight of 54,000 daltons as determined by gel filtration on Ultrogel AcA 44. Homogeneous human kidney renin (2.4 ng/100 micrograms of the inactive renin) activated the inactive renin. Trypsin (2 micrograms), highly purified human plasmin (70 micrograms) and homogeneous human plasma kallikrein (130 micrograms) activated the inactive renin by 100%, by 75% and by 17%, respectively. But highly purified human urinary kallikrein (up to 150 micrograms) did not activate the inactive renin at all. Trypsin-activated renin was a little different from natural plasma active renin with respect to molecular and kinetic properties. When the trypsin-activated renin was treated with human urinary kallikrein, its activity was unchanged, but its molecular weight, Km value, Ki value of pepstatin A and pH profile became identical with those of plasma active renin. On the other hand, renin-activated renin had the same kinetic properties of plasma active renin and human kidney renin, but had the same molecular weight (38,000) as human kidney renin that was smaller than natural plasma active renin (43,000).

Cold Temperature↗