Search PubMed⌕ Search

Biomedical subjects

H Katayama

Publications and source records attributed to H Katayama.

At least 361 records · Page 20Linked to original sources
PubMed1979

Identity of mitochondrial and cytosolic glycerate kinases in rat liver and regulation of their intracellular localization by dietary protein.

Glycerate kinase (ATP: D-glycerate 2-phosphotransferase EC 2.7.1.31) is a key enzyme of glyconeogenesis from serine via hydroxypyruvate. A differential centrifugation of rat liver homogenate and an analysis of the particle fraction by sucrose density gradient centrifugation indicated that 72% and 26% of glycerate kinase are present in mitochondria and cytosol, respectively. A study on the intramitochondrial localization of the enzyme suggested that the mitochondrial glycerate kinase was present in inner membrane and/or matrix. It was found that dietary protein selectively induced mitochondrial glycerate kinase. This result suggested that mitochondrial glycerate kinase had a physiological function for gluconeogenesis from serin. However, the metabolic significance of the cytoplasmic enzyme was still unclear. The properties of solubilized-mitochondrial and cytosolic glycerate kinases were compared. However, no difference between the two enzymes could be found in the kinetic properties, thermal stability, molecular size or electrochemical properties. These results suggested that both enzymes originate from common genetic information. In order to elucidate the regulatory mechanism of the intracellular distribution of glycerate kinase in rat liver, the responses of mitochondrial and cytosolic glycerate kinases to an alteration of dietary protein were studied. The result suggested that an alteration of dietary protein content may regulate the distribution and the translocation of glycerate kinase to mitochondria and cytosol as well as the total amount of glycerate kinase.

Animals↗
PubMed1979

Mitochondrial and cytosolic localization of a single glycerate kinase in rat kidney cortex.

The distribution of glycerate kinase [ATP:D-glycerate 2-phosphotransferase, EC 2.7.1.31] in kidney was studied. This enzyme was found to be present in the renal cortex. By differential centrifugation of the homogenate and sucrose density gradient analysis, it was found that 42% and 60% of the renal glycerate kinase were localized in the cytosol and mitochondria, respectively. The mitochondrial enzyme appeared to be present in the inner membrane and/or matrix. No difference was found between the solubilized-mitochondrial and cytosolic glycerate kinase as regards kinetic properties, thermal stability, electrochemical properties, and molecular size. Immunochemical identity of these enzymes was demonstrated using a rabbit antibody against mitochondrial glycerate kinase purified from rat liver. Although the hepatic enzyme was induced by dietary protein (Kitagawa, Y., Katayama, H., & Sugimoto, E. [1979] Biochim. Biophys. Acta 582, 260--275), the renal enzyme in mitochondria and cytosol was not affected by dietary protein. These results on renal glycerate kinase are compared with those for the hepatic enzyme, and the regulatory mechanism for intracellular distribution of the enzymes is discussed.

Animals↗
PubMed1979

Calcification in augmentation mammoplasty.

Twenty-five cases of augmentation mammoplasty from among 1,600 routine mammograms were divided into paraffin and silicon compound groups. Calcification occurred in 11 cases and was seen in 75% of the paraffin group and 29% of the silicone group. The calcifications in the paraffin group were small, annular, and too numerous to be counted. They were diffusely distributed and tended to involve the lymph nodes. The calcifications in the silicone group were large, egg-shaped, localized, and fewer in number. Lymphadenopathy was rare. The two groups also differed in time elapsed between mammoplasty and mammography.

Adult↗
PubMed1976

Comparison of panoramic radiography and Water's projection in the diagnosis of maxillary sinus disease.

Pantomograms and Water's views were independently reviewed by two radiologists with regard to detection of maxillary sinus abnormalities. Panoramic radiography was found to be a better radiologic approach than the Water's projection for the detection of cystlike densities in the maxillary sinus. Cloudiness of the maxillary sinus and sclerotic change of adjacent bony structures were better demonstrated on the Water's view. These two techniques supplement each other and both should be used in order to obtain a more accurate diagnosis of maxillary sinus disease.

Humans↗
PubMed1976

Beneficial effect of methionine and threonine supplements on tyrosine toxicity in rats.

The growth retardation and external pathological lesions that occur in rats fed a 10% casein diet containing 5% tyrosine could be alleviated by the supplementation of extra protein (20% casein) or 0.66% methionine plus 0.90% threonine (equivalent to the contents in a 20% casein, respectively). Liver tyrosine aminotransferase activity is elevated by ingestion of excess tyrosine, but lowered by the supplementation of extra casein of methionine plus threonine. In rats fed a high tyrosine diet supplemented with methionine plus threonine, liver p-hydroxyphenylpyruvate hydroxylase activity was not higher than that of the 10% casein group, but liver homogentisate oxidase activity increased significantly. When excess tyrosine was included in the 10% casein diet, free tyrosine concentrations in plasma, liver, muscle and brain were extremely elevated, but when the high tyrosine diet was supplemented with extra casein or methionine plus threonine, their plasma and tissues tyrosine concentrations lowered significantly. A large increase in total phenols, p-hydroxyphenylpyruvate and free tyrosine excretions in urine was produced in animals fed the high tyrosine-low protein diet, but these were lowered by the supplementation of methionine and threonine to the diet.

4-Hydroxyphenylpyruvate Dioxygenase↗