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Biomedical subjects

Y Kawade

Publications and source records attributed to Y Kawade.

At least 55 records · Page 3Linked to original sources
PubMed1983

Structure and expression of a cloned cDNA for mouse interferon-beta.

A unique sequence in the mouse genome which cross-hybridized to a cloned human interferon-beta 1 gene was detected by DNA blot analysis. Taking advantage of this, a cDNA library prepared from partially purified mRNA for mouse interferon-beta was screened using human interferon-beta 1 DNA as a probe. One of the positive clones, pM beta-3, contained a 680-base pair cDNA insert, whose base sequence contained a single large open reading frame for 182 amino acids. The coding sequences of the cDNA showed homologies of 63% at the nucleotide and 48% at the amino acid level with respect to human interferon-beta 1 cDNA (Taniguchi, T., Ohno, S., Fujii-Kuriyama, Y., and Muramatsu, M. (1980) Gene 10, 11-15). The first 21 amino acids, considered to be the signal peptide, were followed by 24 amino acids, whose sequence was identical with the NH2-terminal sequence that had been reported for mouse interferon-beta from Ehrlich ascites tumor cells (Taira, H., Broeze, R. J., Jayaram, B. M., Lengyel, P., Hunkapiller, M. W., and Hood, L. E. (1980) Science (Wash. D.C.) 207, 528-530). The complete primary sequence of mature interferon-beta polypeptide consisting of 161 amino acids (Mr = 19,700) was deduced. There are three N-glycosylation sites, and this offers an explanation for the larger molecular size (Mr = 26,000-40,000) of natural mouse interferon-beta in comparison to the deduced interferon polypeptide. The cDNA, when fused to a SV40 promoter sequence and then introduced into COS-7 cells, directed the synthesis and secretion of a protein product indistinguishable from the authentic mouse interferon-beta.

Amino Acid Sequence↗
PubMed1983

Properties of non-glycosylated human interferon-beta from MG63 cells.

MG63 cells induced by Sendai virus produce human interferon (IFN)-beta with a molecular weight of 22000. In the presence of tunicamycin, they produced non-glycosylated, biologically active, IFN-beta with a molecular weight of 17000. It had slightly lower heat stability (at 56 degrees C) than normal glycosylated IFN, but the sensitivity to neutralization by antisera and the cross-species activities on murine, bovine and hamster cells were unaltered, indicating dispensability of the carbohydrate moiety for these parameters. However, the IFN yields were markedly reduced by the glycosylation inhibitor, suggesting an important role of glycosylation in production by cells of IFN-beta.

Cell Line↗
PubMed1982

Antigenic correlations between components of C243 and L cell interferons.

The three components of virus-induced interferon (IFN) from C243 cells, with molecular weights of 19,000, 24,000 and 30,000, were examined for neutralization by antisera against the alpha (24,000) and beta (36,000) types of virus-induced L cell IFN. The results indicated that the C243 19,000 component belongs to the alpha type, and the 24,000 and 30,000 components to the beta type. The 19,000 component was also indistinguishable from L cell IFN-alpha in the reaction with antisera against human IFN-alpha.

Animals↗
PubMed1982

Interferon production in mixed cultures of mouse spleen cells and tumor cells: IFN-gamma as the main component.

Interferon (IFN) production in mixed cultures of mouse spleen cells and tumor cells was investigated, mainly using mouse myeloid leukemic cells, M1, and spleen cells from syngeneic SL mice. Spleen cells from other mouse strains (C57BL/6, BALB/c nude and C57BL/6 beige) and other tumor cells (L929 and YAC-1) were similarly effective for IFN production, but mouse mammary carcinoma FM3A cells were not. As the IFN-inducing stimulus, mycoplasma contaminating the tumor cells, or endogenous retrovirus in them, may possibly be involved. The type of IFN produced was identified as IFN-gamma as a major component and IFN-alpha and -beta as minor ones, by acid stability tests and neutralization by antisera with defined specificities against alpha, beta, and gamma. Depletion of natural killer cells from spleen cells did not appreciably affect IFN production, but depletion of Thy 1.2 antigen-bearing cells greatly reduced IFN-gamma production, indicating that T cells were the main IFN producers.

Animals↗
PubMed1982

Production of interferon-beta by human lymphoblastoid cells of T and non-T--non-B lineages.

Human lymphoblastoid cells of T and non-T--non-B lineages were examined for interferon (IFN) production induced by Sendai virus. All of the four T cell lines examined and two of the three non-T--non-B cell lines produced IFN-beta, and the third non-T--non-B cell line, HL-60, a mixture of IFN-alpha and -beta, in contrast to two B cell lines, which produced IFN-alpha

Cell Line↗
PubMed1982

High-level induction of gamma interferon with various mitogens in mice pretreated with Propionibacterium acnes.

Various T-cell mitogens induced high levels of circulating gamma interferon (IFN-gamma) in mice that had been pretreated with Propionibacterium acnes. Administration of lipopolysaccharide, a B-cell mitogen, to these mice also caused pronounced production of IFN-gamma in addition to IFN-alpha and IFN-beta. The enhanced induction was most marked at about 1 week after the pretreatment.

Animals↗
PubMed1982

[Characterization and bioactivity of interferon induced by Streptococcus faecalis preparation, TH69].

It was demonstrated that TH69, an lyophylized preparation of streptococcus faecalis TH001 (ATCC No. 31663) induced interferon gamma (IFN gamma) in spleen cell cultures. The IFN activity was found in 8 hrs and reached to the peak of 120-240 U/ml 24-48 hrs after incubation in every concentration of 4, 20, and 100 micrograms/ml of TH69. TH69-induced IFN (TH69-IFN) was produced by T cells assisted by macrophages which were stimulated with TH69, and the activity was neutralized by 80-90% with anti-IFN gamma serum but hardly neutralized with anti-IFN alpha, beta serum. Therefore, TH69-IFN was found to be mostly gamma type. The elution profile of TH69-IFN activity on a column with Toyopearl HW-55S showed that molecular weight of IFN was estimated at 18,000-28,000. Sequential purification on this column of TH69-IFN increased the specific activity to approximately 2.5 X 10(4) U/mg protein (partially purified TH69-IFN: TH69-IFNp). A small amount of TH69-IFNp (5-50 U/ml) augmented NK activity and induced cytotoxic macrophages in vitro. Growth of Meth-A tumor cells exposed to TH69-IFNp of 100 U/ml in vitro declined to 50% and three times injection of TH69-IFN (200 U/50 microliters) into the tumor sites of mice given implants of Meth-A suppressed the tumor growth.

Animals↗
PubMed1981

Augmented utilization of branched-chain amino acids by skeletal muscle in decompensated liver cirrhosis in special relation to ammonia detoxication.

Femoral arterio-venous (A-V) differences of blood free amino acids and plasma ammonia (NH3) were simultaneously determined after an overnight fast in 16 patients with decompensated liver cirrhosis in the absence and presence of encephalopathy, as compared with those in 8 control subjects. In spite of increased releases of phenylalanine (Phe) and tyrosine (Tyr) from the peripheral tissue, releases of isoleucine (Ile) and leucine (Leu) as well as alanine (Ala) were found to be significantly reduced in decompensated liver cirrhosis, particularly in the presence of hepatic encephalopathy. Furthermore, NH3 was found to be significantly taken up by the skeletal muscle of these patients, and a positive correlation was observed between arterial NH3 level and the A-V differences of Leu, of Ile and of Ala. These findings strongly suggest that net degradation (or utilization) of branched-chain amino acids (in particular, Leu and Ile) is enhanced in the muscle for detoxication of ammonia (i.e., glutamine synthesis) by supplying the carbon skeleton and energy in cirrhosis of the liver.

Adult↗
PubMed1981

Antigenic cross-reaction between the alpha types of human and mouse interferon.

Cross-neutralization of the alpha and beta types of human and mouse interferons was tested using antibodies directed against the heterologous types of interferons. The alpha type of mouse interferon (MuIFN-alpha) prepared from L cells was found to be completely neutralizable by high-titered antibody against human alpha-type interferon (HuIFN-alpha), although the titers were much lower than those obtained in neutralization reactions with the homologous interferon. MuIFN-alpha from virus-induced lymphocytes, as well as non-glycosylated MuIFN-alpha from L cells, reacted similarly. The cross-reaction was also observed by the binding of anti-HuIFN-alpha antibody to a column of immobilized MuIFN-alpha. The binding experiment indicated that only a small fraction of the anti-HuIFN-alpha antibody population is heterologous reactive. Reciprocally, HuIFN-alpha from L cells, again with relatively low antibody titers, and the antibody responsible for the heterologous reaction was shown to be the anti-MuIFN-alpha and not anti-MuIFN-beta type. It is concluded that the alpha types of human and mouse interferon bear an antigenic homology. On the other hand, no significant antigenic cross-reactivity has been detected between the beta types of human and mouse interferons.

Animals↗