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Biomedical subjects

Y Aoki

Publications and source records attributed to Y Aoki.

At least 649 records · Page 36Linked to original sources
PubMed1987

Accumulation of newly synthesized serum proteins by cadmium in cultured rat liver parenchymal cells.

Effects of cadmium on secretion of the two major serum proteins, albumin and transferrin were studied in primary cultured rat liver parenchymal cells. Exposure to 7 microM cadmium for 8 hr did not inhibit synthesis of both albumin and transferrin whereas secretions of the two proteins were effectively depressed. In the cells exposed to cadmium serum type albumin and proalbumin were accumulated. Cadmium may affect intracellular processing of secretory proteins and also retard the discharge of these proteins resulting in inhibition of protein secretion from the liver parenchymal cells.

Animals↗
PubMed1987

Cadmium inhibits protein secretion from cultured rat liver parenchymal cells.

Depressive action of cadmium (Cd) to the protein secretion from liver was studied in vitro using primary cultures of rat liver parenchymal cells. The cells were cultured in the presence of 0.1-5 microM cadmium chloride. Over this concentration range Cd had no effect on protein synthesis, but caused a dose-dependent inhibition of protein secretion. Although the metallothionein level was increased more than 4-fold by incubation with 10(-6) M dexamethasone, the depressive action of Cd was not prevented by the induction of metallothionein.

Animals↗
PubMed1987

Characterization of cadmium-binding proteins detected in rat liver by the western blotting technique.

Out of the three cadmium-binding proteins (CD-BPs) in rat liver parenchyma (40K, 29K, and 24K CdBPs), the 40K Cd-BP showed the highest affinity for cadmium (Cd), with a dissociation constant (KD) of 1.2 x 10(-8) M. This is in between the affinity of human serum albumin KD = 3.8 x 10(-5) M) and metallothionein (KD = less than 10(-11)). These Cd-BPs may be responsible for hepatic sequestration of cadmium.

Animals↗
PubMed1987

Detection of diatoms in blood by a combination of membrane filtering and chemical digestion.

An improved method for detecting diatom in blood is reported. Blood of cadavers was obtained by cardiac puncture at inquest or from the left atrium directly at autopsy. The blood was hemolyzed by sodium dodecyl sulfate (SDS) and filtered through membrane filter (47 mm in diameter and 5 microns in pore size). When the blood was putrefied, two or three pieces of membranes filters were needed because of choking membrane pore. The membrane filters were digested with fuming nitric acid and diluted with distilled water. The diluted solution was filtered through membrane filter (25 mm in diameter) again. After drying the membrane filter was immersed in oil. Diatoms on the membrane filter were clearly observed microscopically.

Adolescent↗
PubMed1987

Molecular cloning of complementary DNA for human medullasin: an inflammatory serine protease in bone marrow cells.

Medullasin, an inflammatory serine protease in bone marrow cells, modifies the functions of natural killer cells, monocytes, and granulocytes. We have cloned a medullasin cDNA from a human acute promyelocytic cell (ML3) cDNA library using oligonucleotide probes synthesized from the information of N-terminal amino acid sequence of natural medullasin. The cDNA contained a long open reading frame encoding 237 amino acid residues beginning from the second amino acid of natural meduallasin. The deduced amino acid sequence of medullasin shows a typical serine protease structure, with 41% homology with pig elastase 1.

Amino Acid Sequence↗
PubMed1987

Detection of AB antigen in blood stain using enzyme-linked immunosorbent assay.

A new method for detection of AB antigen from blood stain using enzyme-linked immunosorbent assay (ELISA) is described. Flat-bottomed-wells of polystylen plate coated with human anti-B or rabbit anti-A were sensitized with AB antigen which was extracted from blood stain with 1% octyl-glucopyranoside in 0.1 M phosphate buffer pH 8.0. Mouse monoclonal anti-A or anti-B, and peroxidase conjugated anti-mouse immunoglobulin were added to the wells, respectively. Subsequently, the substrate was dropped into the wells, and the absorbance of the solution was measured. By this method, we could distinguish AB group blood stain from the mixed stain of A and B group bloods. When rabbit antiserum was used as the first antibody, differentiation between these antigens was unsuccessful presumably because of non-specific adsorption.

ABO Blood-Group System↗
PubMed1987

[A study of hepato-biliary and alimentary scintigrams using a triple tracer method].

In order to evaluate the gastric emptying and postprandial mixing of bile with food, the scintigraphies of hepatobiliary and gastrointestinal tracts by using three different kinds of radioisotopes were performed simultaneously (99mTc-E.HIDA for hepatobiliary scintigraphy, 111In-DTPA containing orange juice and 131I-albumin containing scrambled egg for gastrointestinal scintigraphy). This method was available for observation of gastric emptying of liquid and solid foods and also examination of the mixing effect of bile and food quantitatively.

Bile↗
PubMed1987

Medullasin enhances human natural killer cell activity by a mechanism other than the induction of interferons or interleukin-2.

The mechanism of activation of human natural killer cell activity by medullasin was studied with special reference to interferons and interleukin-2. Supernatant of lymphocytes treated with medullasin failed to stimulate natural killer cell activity when added to the lymphocyte suspension. Medullasin has been shown to enhance the natural cytotoxicity of lymphocytes stimulated with interferon-alpha or -beta. In the present study, medullasin increased the natural killer cell activity of lymphocytes stimulated with interferon-gamma. Treatment of lymphocytes with medullasin in the presence of antibodies to interferons (alpha, beta and gamma) did not alter the effect of medullasin. Medullasin also increased the natural cytotoxicity of lymphocytes stimulated with interleukin-2. The antibody to interleukin-2 failed to affect the increase of natural killer cell activity by medullasin. These results indicate that the mechanism of activation of human natural killer cell activity by medullasin is not mediated by the induction of interferons or interleukin-2.

Cells, Cultured↗
PubMed1987

Medullasin stimulates the maturation of natural killer cells from human large granular lymphocytes.

Medullasin, a serine protease in bone marrow cells, has been shown to enhance human natural killer cell activity by acting directly on large granular lymphocytes. In the present report the mechanism of activation of natural killer cells by medullasin was studied by employing a single cell assay method in agar. Medullasin enhanced the target-binding capacity of lymphocytes, but the percentage of target-binding cells with dead target remained essentially unchanged. The maximum recycling capacity of natural killer cells was also increased by the treatment with medullasin. These results indicate that medullasin in granulocytes stimulates the maturation of natural killer cells with elevated recycling capacity from human large granular lymphocytes.

Cell Differentiation↗