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Biomedical subjects

Y Higa

Publications and source records attributed to Y Higa.

28 records · Page 2Linked to original sources
PubMed1990

[Cerebrospinal fluid transfer of cefbuperazone in the blood-brain barrier lesions of neurosurgical patients].

Cefbuperazone (CBPZ) was given in 15 patients after surgery. There was no infections except for 1 case in which signs of infections were suspected. As side effects, slight elevations in hepatic transaminase levels were observed in 3 patients during the CBPZ chemotherapy. CBPZ concentrations in 7 patients were studied. The subjects were divided into 3 groups according to CT finding during the chemotherapy to correlate CBPZ concentrations to degrees of blood-brain barrier lesions; Group I: no enhancement, Group II: mild or focal enhancement, Group III: diffuse and marked enhancement. It was interesting to note that the more marked enhancement were obtained, the higher levels of CSF concentration of CBPZ.

Adolescent↗
PubMed1983

In vitro studies on some parameters of the binding of the rat hemopexin--heme complex with the hepatic membrane receptor.

The binding of [125I]Hpx--heme with the rat hepatic plasma membrane receptor was studied at 37 degrees C as well as different parameters such as plasma membrane concentration, calcium dependence, optimal pH and specific binding. A Scatchard plot revealed the existence of one binding for [125I]Hpx--heme on the isolated liver plasma membrane with a Kd = 3.2 X 10(-8) M.

Animals↗
PubMed1982

Kinetic aspects of hemoglobin.haptoglobin-receptor interaction in rat liver plasma membranes, isolated liver cells, and liver cells in primary culture.

125I-Hemoglobin.haptoglobin injected intravenously into rats was incorporated into liver parenchymal cells as evidenced by a cell separation technique. A mixture of freshly isolated liver parenchymal and nonparenchymal cells failed to internalize and degrade the 125I-hemoglobin.haptoglobin added, although it retained the ability to bind the molecule. The liver parenchymal cells in primary culture also lacked the ability to degrade 125I-hemoglobin.haptoglobin, although they bound the molecule more extensively as compared with the freshly isolated liver cells. It was confirmed that the 125I-hemoglobin.haptoglobin which was bound to the freshly isolated liver parenchymal cells localized on the outer surface of liver plasma membranes. Scatchard plots revealed the existence of two binding sites for 125I-hemoglobin-haptoglobin on the isolated liver plasma membrane: an apparent high affinity binding site (Kd = 1.3 X 10(-7) M) and an apparent low affinity binding site (Kd = 4.0 X 10(-6) M) at 37 degrees C. In contrast, freshly isolated liver parenchymal cells had only an apparent low affinity binding site (Kd = 1.4 X 10(-6) M) at 37 degrees C. Impairment of the apparent high affinity binding site during the isolation procedure with collagenase seemed to be related to loss of the ability to internalize and degrade the 125I-hemoglobin.haptoglobin molecules into the freshly isolated liver parenchymal cells or liver parenchymal cells in primary culture.

Animals↗
PubMed1981

Catabolism of globin-haptoglobin in liver cells after intravenous administration of hemoglobin-haptoglobin to rats.

The intracellular site of uptake and degradation of globin-haptoglobin, the protein moiety of hemoglobin-haptoglobin, in rat liver cells was investigated in vivo. Hemoglobin-haptoglobin, administered intravenously to rats, is cleared from circulation and incorporated exclusively into liver parenchymal cells through the receptor specific for the molecule (Kino, K., Tsunoo, H., Higa, Y., Takami, M., Hamaguchi, H., and Nakajima, H. (1980) J. Biol. Chem. 255, 9616-9620). Intrahepatocellular distribution of radioactivity was determined after intravenous administration of (125I-hemoglobin)-haptoglobin or hemoglobin-(125I-haptoglobin) to rats. The 125I-labeled hemoglobin-haptoglobin was incorporated first in organelles of low density (density range, 1.05-1.07 g/ml) recovered in Golgi subfractions of the liver cells in a substantially intact form. The organelles progressively acquired a higher density, presumably through fusion with primary lysosomes. In the resulting organelles of high density (density range, 1.07-1.15 g/ml), which are probably secondary lysosomes, hemoglobin-haptoglobin first dissociated symmetrically to yield two 82,000-dalton subunits by a limited proteolysis, and further digestion of the constituent polypeptide chains seemed to proceed thereafter in the organelles during the transport process across the cells.

Animals↗
PubMed1980

Hemoglobin-haptoglobin receptor in rat liver plasma membrane.

The presence of a receptor specific for the hemoglobin . haptoglobin complex is demonstrated in rat liver plasma membranes. Hemoglobin . haptoglobin complex, administered intravenously to rats, was cleared from the circulation at a constant rate with exclusive incorporation of the molecule into hepatocytes. This incorporation was unaffected by the simultaneous injection of asialoglycoprotein or heme . hemopexin complex. In vitro experiments with isolated liver plasma membranes indicated the absence of competitive binding of these molecules to the membrane and suggested that this receptor might recognize an altered conformation of the haptoglobin moiety of the complex resulting from the binding with hemoglobin. These observations suggest that the mechanism of recognition and binding of hemoglobin . haptoglobin complex by the receptor is different from that of the asialoglycoprotein receptor or heme . hemopexin receptor.

Animals↗