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Biomedical subjects

K Inagaki

Publications and source records attributed to K Inagaki.

At least 163 records · Page 9Linked to original sources
PubMed1985

[Effects of iontophoretically-applied LHRH, TRH, estrogen and clomiphene on thermo-sensitive neurons in the rat hypothalamus].

Studies were performed on the correlation between the hypothalamic temperature-sensitive neurons and hypothalamic neurons sensitive to LHRH, TRH, conjugated estrogen and clomiphene in 103 castrated matured female rats by the technique of microiontophoresis using a multi-barrel glass microelectrode. Out of 348 neurons in the hypothalamus, 24 neurons were found to be LHRH-sensitive, 20 TRH-sensitive, 41 estrogen-sensitive, and 18 clomiphene-sensitive. There were 19(28.8%) warm-sensitive and 11(16.7%) cold-sensitive neurons located in the preoptic area. From among the 19 warm-sensitive neurons, 14 neurons showed excitation by estrogen and 4 showed suppression by LHRH. Out of the 11 cold-sensitive neurons, estrogen, LHRH, and TRH excited 4, 3, and 3 neurons, respectively. It is suggested from these studies that LHRH mainly exhibits its thermo-regulatory functions by exciting warm-sensitive neurons and it is for this reason that exogenous estrogens are effective in alleviating hot flushes in natural as well as post-operative menopause which are thought to be caused by LHRH.

Action Potentials↗
PubMed1985

Maternal liver impairment associated with prolonged high-dose administration of terbutaline for premature labor.

Widespread use of beta 2-sympathomimetic therapy for premature labor has resulted in a diverse number of serious maternal complications, ie, pulmonary edema, myocardial ischemia, etc. However, to the authors' knowledge, there has been only one previous report of mild maternal liver impairment associated with this therapy. Recently, a patient developed marked elevation of liver enzymes (serum glutamic oxaloacetic transaminase, serum glutamic pyruvic transaminase) during therapy with terbutaline sulfate for premature labor.

Adult↗
PubMed1984

D-glucose anomeric preference of hexokinases from animals and yeast.

The D-glucose anomeric preference of hexokinases partially purified from animals (rat, mouse, and chicken) and baker's yeast (Saccharomyces cerevisiae) were investigated by the assay system with glucose-6-phosphate dehydrogenase as a coupling enzyme. With low Km hexokinases in animal tissues and cells, the ratios of Vmax for the beta-anomer to Vmax for the alpha-anomer (V beta/V alpha) were within a range from 1.3 to 1.5. In yeast, the V beta/V alpha value was 1.1 for hexokinase A, 0.8 for hexokinase B, and 1.4 for glucokinase. The possible explanation for D-glucose anomeric preference of hexokinase is discussed.

Animals↗
PubMed1984

Purification and properties of amino acid racemase from Aeromonas punctata subsp. caviae.

An amino acid racemase, which occurs in the cytoplasmic fraction of Aeromonas punctata subsp. caviae, has been purified to homogeneity by the criteria of electrophoresis and ultracentrifugation. The enzyme has a molecular weight of about 80,000 and consists of two subunits identical in molecular weight (about 40,000). The enzyme contains 2 mol of pyridoxal 5'-phosphate per mol of enzyme, and exhibits absorption maxima at 280 nm and 420 nm. The holoenzyme is resolved by dialysis against hydroxylamine to yield the inactive apoenzyme, which is reconstituted by the addition of pyridoxal 5'-phosphate to recover the full activity. The enzyme catalyzes racemization of a number of amino acids, e.g. lysine, ornithine, ethionine, arginine, glutamine, and methionine. The Michaelis constants were determined: 1 mM for L-lysine; 0.9 mM for D-lysine; 0.9 mM for L-ornithine; 1 mM for L-arginine; and 2.6 microM for pyridoxal 5'-phosphate. This enzyme is similar in enzymological properties to the racemase of Pseudomonas putida, but is distinct from it in immunochemical properties.

Aeromonas↗
PubMed1983

Preference of glucokinase for the alpha anomer of hexose: relation to alpha-anomer preference in hexose-induced insulin release by pancreatic islets.

The alpha anomers of glucose and mannose were more rapidly phosphorylated than the beta anomers by rat liver glucokinase, whose chromatographic and kinetic properties are known to be quite similar to those of pancreatic islet glucokinase. This result may explain our previous findings of the alpha-anomeric preference in glucose- and mannose-stimulated insulin release, and therefore suggests to support the hypothesis that glucokinase in islets functions as a crucial hexose sensing enzyme for insulin release induced by glucose and mannose.

Animals↗
PubMed1982

Inhibition of aldose reductases from rat and bovine lenses by flavonoids.

Thirty flavones, four isoflavones and thirteen coumarins were tested as inhibitors of lens aldose reductase, which is believed to participate in the initiation of cataract formation in diabetes. Many were found to be potent inhibitors, and the two most potent ones were axillarin (5,7,3',4'-tetrahydroxy-3,6-dimethoxyflavone) and 6,3',4'-trihydroxy-5,7,8-trimethoxyflavone (LARI 1). These two flavones inhibited aldose reductase purified from rat lens with IC50 values of 2.6 X 10(8) and 3.6 X 10(8) M respectively. They also inhibited aldose reductase purified from bovine lens with IC50 values of 1.8 X 10(7) M. The potencies of the two compounds were superior to those of all the previously reported inhibitors of aldose reductase. Inhibition of rat and bovine lens aldose reductases by the two compounds was of a non-competitive type with DL-glyceraldehyde as the variable substrate. Some flavones including axillarin and LARI 1 were found to be poorly or scarcely inhibitory against several adeninenucleotide-requiring enzymes, which are involved in glycolysis and other metabolic reactions. These results obtained show that the two flavones have some features which may be required in clinically useful drugs for diabetic patients. All the potent inhibitors of the compounds tested had a flavone skeleton, one (or two free) hydroxyl(s) in ring C, and more than three hydroxyls (free or methylated) in ring A. The possible relationships of structures to inhibitory potencies of the compounds tested are discussed.

Aldehyde Reductase↗