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Biomedical subjects

H Kido

Publications and source records attributed to H Kido.

At least 235 records · Page 13Linked to original sources
PubMed1981

Purification of thymus mRNA coding for a 16,000-dalton polypeptide containing the thymosin alpha 1 sequence.

A mRNA fraction purified by preparative polyacrylamide disc gel electrophoresis from calf thymus polysomes codes for a polypeptide(s) having a mass of 16,000-17,000 daltons. This polypeptide contains amino acid sequences corresponding to residues 11-18 and 19-25 of thymosin alpha 1. The yield of the octapeptide indicates that the 16,000-dalton peptide is the major product formed in the cell-free synthesis system containing the purified mRNA.

Animals↗
PubMed1979

Amplification of growth inhibition by glucocorticoid on L5178Y and L1210 lymphoblasts in vivo.

One component of a factor in Proteus mirabilis (Factor 1) which specifically amplifies the induction of several liver enzymes by glucocorticoid in target cells also increases the growth inhibition of glucocorticoid on the ascitic form of L1210 cells and solid tumors of L5178Y lymphoblasts in vivo. The growth of L5U78Y and L1210 lymphoblasts was inhibited by a triamcinolone acetonide dose of over 0.5 to 1.0 mg/kg body weight. Factor 1 increased the inhibitory effect of a triamcinolone acetonide dose of less than 4.0 mg/kg bodyweight but had little effect on the effects of doses of over 4.0 mg. Factor 1 (10 biological units/kg body weight) itself also caused marked inhibition of the growth of these lymphoblasts without affecting the body weight or adrenal gland weight, its effect being equivalent to that of 3- to 4-mg/kg body weight doses of triamcinolone acetonide alone. There was no significant difference in the level of plasma total corticoids or that of plasma adrenocorticotropic hormone between rats treated with 0.9% NaCl solution or those treated with Factor 1, and Factor 1 had no cytotoxic effec on cultured L5178Y lymphoblasts. Thus, Factor 1 may amplify the effect of physiological level of glucocorticoid in mice sufficiently to inhibit the growth of these lymphoblasts without causing any significant side effects to the host animal.

Adrenal Cortex Hormones↗
PubMed1977

A new factor from enteric bacteria of rats amplifying induction of liver enzyme by glucocorticoid. 1. Purification, properties and biological action.

1. A factor, which amplifies the inductions of several liver enzymes by glucocorticoid, was partially purified from Proteus mirabilis from rat intestine. The factor (amplifier) was completely inactivated by alpha-glucosidase, but not by other glycoside hydrolases, proteases, nucleases or phosphatases tested; it was also hydrolysed by HCl with liberation of reducing sugars. Thus the oligosaccharide in this factor seems to be essential for the amplification. 2. In adrenalectomized rats the amplifier increased the inductions of several liver enzymes, such as tyrosine aminotransferase and leucine aminotransferase, by glucocorticoid. But it did not amplify the induction of tyrosine aminotransferase by glucagon or insulin or the activities of enzymes that are not induced by glucocorticoid. The amplifier by itself did not have any glucocorticoid-like action in adrenalectomized rat. These results show that the amplifier specifically increases the inductions of liver enzymes by glucocorticoid. 3. Since similar amplification was also observed in isolated perfused liver and cultured hepatoma cells in vitro, the amplifier seems to act directly on the target organ or cells.

Animals↗
PubMed1977

A new factor from enteric bacteria of rats amplifying induction of liver enzyme by glucocorticoid. 2. Mechanism of action.

1. An amplifier of the action of glucocorticoid was purified from Proteus mirabilis as described previously. It was found that it amplified the induction of liver tyrosine aminotransferase by dexamethasone markedly with doses of dexamethasone that caused minimal enzyme induction, but had little effect with doses that caused maximal induction. Thus the amplification may represent a saving of glucocorticoid. The amplification of enzyme activity was brought about by increase in amount of enzyme. 2. The amplification was observed when the amplifier was administered before or with dexamethasone, but not when it was given 2 h after dexamethasone. These results and the finding that actinomycin D inhibited the amplification indicate that the amplifier does not act on the translational level of enzyme induction. 3. It was found that the amplifier increased both incorporation of [3H]dexamethasone into the cytosol and binding of [3H]dexamethasone of cytosol protein and that it decreased decay of the [3H]dexamethasone-protein complex.

Animals↗
PubMed1977

Establishment of a clonal strain of hepatoma cells derived from Morris hepatoma 8999.

A new line of tissue culture cells derived from a slow-growing hepatoma 8999 was established and named 8999C. The isolation method, growth pattern, and morphology of the 8999C cells are described. Several hepatic enzyme activities in 8999C cells were compared to those in the original hepatoma 8999. The ornithine aminotransferase (EC 2.6.1.13), tyrosine aminotransferase (EC 2.6.1.5), and arginase (EC 3.5.3.1) activities in the 8999C cells were one-third, one-tenth, and one-hundredth of those of the respective activities in the original hepatoma 8999, and mitochondrial serine protease, which has much higher activity in hepatoma 8999 than in normal liver cells, was not detected in 8999C cells. Tyrosine aminotransferase in 8999C cells was induced by dexamethasone but not by N6,O2'-dibutyryladenosine 3',5'-cyclic monophosphate or insulin. Unlike in hepatoma 8999, glucocorticoid did not induce arginase in 8999C cells.

Arginase↗