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Biomedical subjects

M Gotoh

Publications and source records attributed to M Gotoh.

At least 505 records · Page 28Linked to original sources
PubMed1983

Giant scrotal hemangioma with azoospermia.

We report a case of giant scrotal hemangioma with azoospermia, which was 37 cm in maximum circumference and 20 cm in length along the raphe. The biopsy specimens of the testes were examined histologically and cytologically. The testicular damage was believed to be due to the heat generated by hemangioma.

Adolescent↗
PubMed1983

Cytoplasmic inclusion bodies in Leydig cells from the testes of postpubertal cryptorchid patients.

During the course of electron microscopic studies on testes from cryptorchid patients, we have observed an inclusion body in the cytoplasm of Leydig cells. Such inclusion bodies were detected in Leydig cells of post-pubertal patients (16 to 30 years), but were not evident in the cells of pubertal and pre-pubertal patients (3 to 12 years), or in cells from the contralateral descended scrotal testes of cryptorchid patients or in cells from normal controls. These inclusion bodies are therefore believed to result from specific cytological changes which occur in cryptorchid testes during puberty.

Adolescent↗
PubMed1983

Arterial renin--partial characterization and its possible role in the pathogenesis of hypertension.

1) Renin-like enzyme of rat aorta was purified by chromatography with DEAE-cellulose and Sephadex G-200. 2) The molecular weight of renin-like enzyme was 124,000 and 72,000 on Sephadex G-200 gel filtration. The isozymes, however, migrated as a single band with molecular weight of 71,000 on SDS/polyacrylamide gel electrophoresis. These isozymes showed the same optimal pH (6.5) and temperature (37 degrees C). 3) Renin-like enzyme showed high activity in the microsomal fraction of the aorta. 4) In one-clip, two-kidney Goldblatt hypertensive rats, the aortic renin concentration increased significantly, but not parallel with the activity in plasma. 5) Renin, widely distributed in subcellular fractions of the aorta, may play a possible role in the local control of vascular tone. It is likely that renin in vascular wall is of local origin.

Animals↗
PubMed1983

Glucagon secretory responses to insulin-induced hypoglycemia and arginine in streptozotocin-induced diabetic dogs.

To clarify whether the reactivity of A cells is regulated by B cell function in the pancreas, plasma glucagon (IRG) responses to insulin-induced hypoglycemia and to arginine infusion were evaluated in streptozotocin (STZ; total 40 mg/kg) treated and control dogs. There was no significant rise in plasma IRG levels during the insulin-induced hypoglycemia in the STZ-treated dogs. In contrast, arginine enhanced the IRG secretion from the pancreas to a similar extent in the two groups. This was deduced from the difference between IRG levels in the pancreaticoduodenal and peripheral veins. Neither intravenous glucose nor arginine infusion resulted in a significant rise in plasma insulin (IRI) levels in the STZ-treated dogs. IRI content in the pancreas of STZ-treated dogs was significantly reduced to 5 percent below the levels in the control dogs. The IRG content for control and STZ-treated dogs did not differ. These results indicate that while the responsiveness of A cells to hypoglycemia may depend on the secretory capacity of B cells, such is not the case with arginine.

Animals↗
PubMed1983

Angiotensin-converting enzyme activity of the brain and the aorta in experimental hypertensive rats.

Angiotensin-converting enzyme activity in six areas of the brain (cerebral cortex, midbrain, thalamus, hypothalamus, striatum, and cerebellum) and subcellular fractions of the aorta (homogenate, mitochondria, microsomes, and supernatant) was determined in both normotensive and renal hypertensive rats [Goldblatt one-clip, one-kidney (1-c, 1-k) and one-clip, two-kidney (1-c, 2-k) hypertensive, and two-clip, two-kidney (2-c, 2-k) hypertensive rats]. Converting-enzyme activity was relatively high in the thalamus and relatively low in the cerebellum in normotensive and renal hypertensive rats. The enzyme activity in the hypothalamus of Goldblatt 1-c, 2-k rats was significantly higher than that of normotensive and other renal hypertensive rats. However, there was no significant difference in the enzyme activity in each brain area among normotensive, Goldblatt 1-c, 1-k hypertensive and 2-c, 2-k hypertensive rats. The enzyme activity of the supernatant from aortic subcellular fractions was extremely high in normotensive and renal hypertensive rats. However, the enzyme activity in all aortic fractions from Goldblatt 1-c, 2-k rats was significantly higher than that of normotensive and other renal hypertensive rats. There was no significant difference in the enzyme activity among normotensive, Goldblatt 1-c, 1-k hypertensive and 2-c, 2-k hypertensive rats. Therefore, it is likely that increased angiotensin-converting enzyme activity in the brain and the aorta may play a role in the initiation or the maintenance of hypertension in Goldblatt 1-c, 2-k hypertensive rats.

Animals↗
PubMed1983

Acute effects of captopril on serum angiotensin-converting enzyme activity, the renin-aldosterone system and blood pressure in patients with sarcoidosis.

Captopril, an orally active angiotensin-converting enzyme (ACE) inhibitor, was administered to three patients in an active stage of sarcoidosis. The serum ACE level, aldosterone concentration in plasma and blood pressure decreased rapidly after administration, while plasma renin activity was not significantly changed. It is suggested that inhibition of ACE by captopril offers a possible therapeutic approach to the treatment of sarcoidosis.

Adult↗
PubMed1983

[Clinical study on preoperative chemotherapy of primary breast cancer. 2--A comparative study of CPA + FT-207 (5-FUDS) and CPA + FT-207 (5-FUDS) + MMC].

In 41 cases of primary breast cancer preoperative treatment was performed using 2 methods consisting CPA + FT-207 (5-FUDS) (for Group I) and CPA + FT-207 (5-FUDS) + MMC (for Group II) to determine clinical and histological efficacies. A daily dose of each anticancer drug was: CPA 50-200 mg, FT-207 200-600 mg, and 5-FUDS 200 mg orally, and MMC 4-20 mg intravenously. The mean total doses were 1.8 g, 6.3 g, 3.4 g and 26.3 mg, respectively. Reduction in tumor size was obtained in 11 cases (37.9%) in Group I and 6 cases (50.0%) in Group II. According to Ohboshi's criteria, histological efficacy as defined over Grade II a was seen in 5 cases (17.2%) in Group I and 6 cases (50.0%) in Group II, while the efficacy classified as Grade III was not seen in any of the cases. Although the clinical effect was not always consistent with the histological effect, there was a tendency of agreement between them in Group II. As to the dosages of anticancer drugs, more effective cases were seen when dosages of more than 25 mg/kg of CPA, 80 mg/kg of FT-207 (5-FUDS) or 0.5 mg/kg of MMC were used. Reduction in tumor size began to appear at 2 to 3 weeks after the initiation of treatment.

Adult↗
PubMed1982

[Angiotensin-converting enzyme activity of the aorta in experimental hypertensive rats].

Angiotensin-converting enzyme activity of the aortic subcellular fractions (homogenate, mitochondria, microsomes and supernatant) was determined in normotensive and experimental hypertensive rats (1-clip, 1-kidney Goldblatt hypertensive; 1-clip, 2-kidney Goldblatt hypertensive and 2-clip, 2-kidney hypertensive rats). The systolic blood pressure markedly elevated in each group of experimental hypertensive rats, while it did not in normotensive rats. Angiotensin-converting enzyme activity was consistently high in the microsomal and supernatant fractions of the aorta in experimental hypertensive rats as well as in normotensive rats. However, the enzyme activity from each fraction of the aorta in 1-clip, 2-kidney Goldblatt hypertensive rats was significantly higher than that in normotensive and other experimental hypertensive rats. There was no significant difference in the enzyme activity among normotensive, 1-clip, 1-kidney Goldblatt hypertensive and 2-clip, 2-kidney hypertensive rats. The angiotensin-converting enzyme, widely distributed in subcellular fractions of the aorta, may play a possible role in the local control of vascular tone. It seems likely that increased angiotensin-converting enzyme activity in arterial tissue contributes to the initiation or development of hypertension in 1-clip, 2-kidney Goldblatt hypertension in rats.

Animals↗
PubMed1982

[Clinical study on the angiotensin I-converting enzyme in human urine. (I) Partial purification, enzymic characteristics and excretion in normal subjects].

The angiotensin I-converting enzyme in normal human urine was partially purified with ammonium surfate (3.2M), DEAE-Cellulose ion exchange chromatography (0-0.5M NaCl gradient), and Sephadex G 200 gel filtration. The enzyme was separated into three forms which had different molecular weights of 700000, 290000 and 40000, respectively. The enzymic biochemical characteristics of these three enzymes, however, were identical with regard to their inhibitory effects (bradykinin potentiator c, arg-pro-pro, o-phenanthroline and EDTA), Cl- dependency, optimal pH (8.3) and temperature (37 degrees C), and Km value (2.3mM). The enzymic activity was determined in five normal subjects in three conditions of dietary sodium intake (51, 153 and 340mEq for 5 days, respectively). The enzymic activity correlated well with the concentration of the excreted sodium (r = 0.87, p less than 0.001). There was no significant relation between the enzymic excretion and the concentration of the excreted potassium, nor between the activity and the creatinine excretion. It is suggested that the origin of urinary angiotensin I-converting enzyme is the kidney, and that the enzyme might regulate sodium excretion in cooperation with renal kallikrein-kinin system.

Adult↗
PubMed1982

[Automated microdetermination of lead in capillary blood from earlobes by flameless atomic absorption spectrophotometry].

Recent development of flameless atomic absorption spectrophotometry has made possible more precise and sensitive determinations of metals including lead. This means that a sample size of microliter order of blood has come to give a sufficient analytic signal. Blood lead which has usually been determined using venous blood was determined in the present study using a small amount of capillary blood. The method developed is of lead determination in the capillary blood sample from earlobe by means of flameless atomic absorption spectrophotometry equipped with an automated microsampling system or autosampler. Thus, 70 microliters of heparinized whole blood sample from earlobe gave a satisfactory result in the lead analysis. The procedure is as follows. 1) Blood obtained from the earlobe is collected in a heparinized capillary tube. 2) The blood is diluted in the ratio of 1 : 9 with Triton 5000 X solution for complete hemolysis of erythrocytes, by which the matrix-bound lead is released and a better distribution of samples is made possible in the graphite tube. 3) Finally the sample is analyzed by a flameless atomic absorption spectrophotometer with an autosampler. Making sure the analytical method to be accurate and reliable for blood lead determination, the authors compared capillary blood lead levels (Pb-Bc) with venous ones (Pb-Bv) from the same subjects in the same sampling session. It was found that the correlation between Pb-Bc and Pb-Bv was highly significant (n = 144, r = +0.998, y = 0.97 x+0.32, p less than 0.001) and that they were almost of the same level. It was concluded that the method developed may be recommended for the routine clinical use.

Adult↗