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Biomedical subjects

M Kawase

Publications and source records attributed to M Kawase.

At least 163 records · Page 9Linked to original sources
PubMed1988

Study of the effect of an anti-androgen (oxendolone) on experimentally induced canine prostatic hyperplasia. II. Endocrinological analysis.

The results of hormonal investigation of effects of an antiandrogen, Oxendolone (OXD), alone or in combination with medroxyprogesterone acetate (MPA), on experimentally induced canine BPH are reported. Seventeen beagle dogs were divided into 5 groups: 2 castrate controls for Group 0, 3 BPH controls for Group 1 which received 3 alpha-androstanediol (3 alpha-A) and estradiol (E2) for one year, and 12 dogs consisting of 3 groups which received 3 alpha-A and E2 for 6 months followed by testosterone propionate (TP) and E2 for another 6 months. The last 3 groups were treated with either 200 mg/week of OXD (Group 3) or OXD + 30 mg/week of MPA (Group 4), and otherwise untreated with these hormones (Group 2, T-E controls). On the blood hormone analysis, both T and 5 alpha-dihydrotestosterone (DHT) were generally lowered in the T-E administered groups (Group 2, 3 and 4) compared to those in Group 1. While MPA significantly decreased these androgen levels, OXD did not influence at all. The concentrations of E2 were similar. Although T content in the prostate did not differ significantly within the experimental groups, DHT was the highest in Group 1 and the lowest in Group 4 and was nearly the same level to Group 0. MPA reduced tissue DHT content but OXD did not. In the receptor assay study, nuclear androgen receptor (AR) content in Group 3 and 4 was significantly lower than that in Group 1. No obvious decrease in nuclear AR content could be seen among the other groups.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1987

Determination of covalently bound myo-inositol in bovine erythrocyte acetylcholinesterase and porcine kidney alkaline phosphatase.

Bovine erythrocyte acetylcholinesterase and porcine kidney alkaline phosphatase were purified to a homogeneous state. By using gas chromatography-mass spectrometry, we demonstrated the presence of covalently bound myo-inositol in these purified enzymes. The quantitative data suggest that one molecule of myo-inositol is bound to each subunit of these enzyme proteins. The covalently bound inositol was removed from these enzyme molecules by deamination with nitrous acid, suggesting the possibility that myo-inositol is directly bound to amino sugar.

Acetylcholinesterase↗
PubMed1987

Simple and sensitive determination of methylglyoxal in biological samples by gas chromatography with electron-capture detection.

Methylglyoxal was allowed to react with 4,5-dichloro-1,2-phenylenediamine, and the 6,7-dichloro-2-methylquinoxaline formed was determined by gas chromatography with electron-capture detection. The standard curve of the quinoxaline was linear up to 160 pmol/ml. The recoveries of methylglyoxal from coffee and rat liver homogenate were 84.1 and 77.6%, respectively. This procedure was very selective and so sensitive that as little as 9 fmol of the quinoxaline could be measured in biological and food samples.

Aldehydes↗
PubMed1986

Detection of metastatic medullary thyroid cancer with 131I-MIBG scans in Sipple's syndrome.

While 131I-meta-iodobenzyl guanidine (131I-MIBG) scanning has made possible the scintigraphic visualization of pheochromocytoma and neuroblastoma, an accumulation of this agent has recently been reported in medullary thyroid cancer. We present the case of a patient with Sipple's syndrome (multiple endocrine neoplasia type IIa), in whom we were able to identify distant metastases and local invasion of medullary thyroid cancer as well as primary thyroid tumour and right adrenal pheochromocytoma, using 131I-MIBG scans. This case highlights the usefulness of 131I-MIBG in the detection of metastatic medullary thyroid cancer and suggests that this agent may also be of therapeutic use in the treatment of tumours.

3-Iodobenzylguanidine↗
PubMed1985

Acute effect of triiodothyronine on the dynamics of thyrotropin release from superfused anterior pituitary cells.

The effects of triiodothyronine (T3) on the dynamics of thyrotropin (TSH) release induced by TSH-releasing hormone (TRH) were examined in the presence or absence of a protein synthesis inhibitor, cycloheximide (CX), in a superfusion system using primarily cultured cells of the rat anterior pituitary gland on microcarrier beads. When the cells were continuously stimulated with TRH (10 nM, 180 min), TSH release occurred in a biphasic manner and the profile of TSH release was characterized by an initial sharp peak (phase I), followed by a lower plateau form phase (phase II). Both phase-I and phase-II releases were significantly suppressed in the presence of T3 (1 ng/ml), which was added to the superfusion medium 1 h before initiation of TRH stimulation. The biphasic nature of the release profile was maintained in the presence of T3, suggesting that the site of the T3 action may be common between phase-I and phase-II release. We have already suggested that phase-I release is protein synthesis-independent and phase-II release protein synthesis-dependent using CX in TRH-stimulated cells. In the presence of CX, phase-I release was not suppressed by T3, while phase-II release was still suppressed by T3. The inability of CX to reverse the T3-induced suppression of phase-II release may be masked by the direct CX effect on phase-II release of TSH. The present study indicates that each component (phase I and phase II) of the biphasic release of TSH induced by TRH stimulation was acutely suppressed by T3 and suggests that the T3 action is mediated through protein synthesis.

Animals↗
PubMed1984

Identical myoglobin is present in both skeletal and smooth muscles of chicken.

Chicken gizzard has been considered to be an exceptional organ of smooth musculature in which a myoglobin is present. Since the characterization of the gizzard myoglobin has to date, been very incomplete, we studied the structures and functions in detail. The main component, which constituted roughly 90% of the protein, isolated by chromatofocusing, was homogeneous by electrophoretic and ultracentrifugal analyses. The molecular weight was consistently 1.8 X 10(4) by equilibrium sedimentation and iron analysis, and the isoelectric point was 7.8. Spectroscopic properties of the oxy-, carboxy- and deoxy-derivatives were typical of myoglobin. The oxygenation equilibria were also typical of myoglobin, showing neither homotropic nor heterotropic allosteric interactions, and the temperature-dependence (delta H0) was estimated as -16.6 kcal/mol. All these characteristics of the gizzard myoglobin were identical with those of the protein from the skeletal muscles. The amino acid composition and peptide mapping results also concluded that identical myoglobin was present in the gizzard, skeletal and probably cardiac muscles.

Amino Acids↗