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Biomedical subjects

T Noda

Publications and source records attributed to T Noda.

At least 469 records · Page 26Linked to original sources
PubMed1983

[Anticancer effects of OK-432 (2). Anticancer actions of M phi activated by OK-432].

Mouse spleen cells (DDI, BALB/c, 10 weeks old), either pretreated in vitro with 100 u/ml of OK-432-induced IFN gamma for 18 hr or obtained from mice 24 or 48 hr after iv injection of OK-432 (100 micrograms/mouse), were examined for their antitumor effect by Winn assay against Meth-A tumor cells in BALB/c mice. Both of these spleen cells preparations clearly inhibited the growth of admixed Meth-A cells. In order to determine the effector subpopulation, these spleen cells were treated with either anti-Thy-1 monoclonal antibody plus complement, anti-asialo GM1 serum plus complement or in combination of adherence on plastic plates followed by Sephadex G-10 column treatment. As a result, the effector activity in Winn assay was lost only after the removal of macrophages through plastic plate adherence and Sephadex G-10 column treatment, but not after anti-Thy-1 or anti-asialo GM1 treatment, with either spleen cell populations. Moreover, after anti-Thy-1 treatment, the effector activity of spleen cells increased, suggesting the presence of suppressor T cells in these spleen cell populations. The growth of Meth-A cells was not only inhibited by these activated macrophages in Winn assay but also by adoptive transfer of OK-432-induced cytotoxic spleen macrophages, intralegionally 4 days after the implantation of 1 X 10(6) Meth-A cells. In conclusion, the effector cells which appeared in mouse spleens after iv injection of OK-432 were found to be cytotoxic macrophages, which inhibited the growth of Meth-A cells, both in vitro and in vivo. IFN gamma induced by OK-432 in mouse spleen cell cultures produced the same cytotoxic macrophages when added to the spleen cell cultures, at a dose as low as 100 u/ml. All of our evidence suggests that the systemic action of OK-432 can be explained by the effect of IFN gamma induction.

Animals↗
PubMed1982

Reoperative surgery in cholelithiasis.

From 1965 to 1980, reoperations for residual or recurrent stones were performed on 78 out of 962 Japanese patients with cholelithiasis. The majority of patients who required reoperation had intrahepatic stones. Most of the causes of reoperation were residual stones due to incomplete removal or the non-detection of intrahepatic stones at the previous surgery. Very careful examination of the intrahepatic biliary trees should be done in patients with biliary tract diseases, because in many, the first operation was done during their youth. To remove the intrahepatic calculi completely, hepatic lobectomy should be considered as a final procedure. The causes of reoperation of common duct stones were residual in 60 per cent and recurrent in 40 per cent. Definitive surgery should be done at the first or at least the second operation to avoid irreversible hepatic disorders which have untoward effects on the prognosis. It is important not only to remove the stones but also to relieve the bile stasis in the biliary tract.

Aged↗
PubMed1982

[Antitumor effect of OK-432 (1)--antitumor effect of OK-432 induced interferon-gamma (IFN gamma)].

Recent findings that OK-432 induces IFN gamma both in vivo and in vitro prompted us to examine the host-mediated antitumor effects of OK-432 previously observed, such as activation of cytotoxic macrophages and augmentation of NK cell activity, through the action of induced IFN. By using partially purified IFN gamma produced in vitro with mouse spleen cells in the presence of OK-432, antitumor effects were examined against Meth-A cells both in vivo and in vitro. Repeated intratumoral injections of IFN gamma (300 U/mouse) resulted in 75% inhibition of tumor growth. In vitro studies also showed that 50 U/ml was enough to inhibit the growth of Meth-A cells. Augmentation of NK cell activity was found both in vivo by a single i.p. injection of 200 U/mouse, and in vitro, with as low a concentration as 5 U/ml. When macrophages obtained from mice after i.p. injection of thioglycolate medium were treated in vitro with OK-432 induced IFN gamma, 20 U/ml was shown to activate the cytotoxic effect of M phi on Meth-A cells. All of the experiments were conducted with a positive control of purified mouse IFN-alpha/beta. With antitumor and cell activating effects compared in units, OK-432 induced IFN gamma was almost 10 times or more as active as IFN alpha/beta.

Adjuvants, Immunologic↗
PubMed1981

Susceptibilities of various myofibrillar proteins to cathepsin B and morphological alteration of isolated myofibrils by this enzyme.

The abilities of cathepsin B purified from liver to degrade purified myofibrillar proteins, myosin, actin, troponin, tropomyosin, and alpha-actinin from rabbit skeletal muscle were studied. The amino acids or peptides liberated from these proteins by cathepsin B were determined quantitatively by fluorometry with o-phthalaldehyde, and qualitatively by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. At a molar ratio of cathepsin B to substrate of 1 : 100, the order of susceptibilities was myosin much greater than troponin greater than tropomyosin much greater than actin. alpha-Actinin was not degraded. Myosin heavy chain was degraded to several fragments with molecular weights of 175,000, 170,000, 160,000, and 145,000, whereas the light chains were scarcely degraded. Cathepsin B degraded troponin-T rapidly, and troponin-I more slowly, but did not degrade troponin-C. Troponin-T and troponin-I were degraded to three fragments with molecular weights of 30,000, 18,000, and 12,800. Tropomyosin was degraded slightly and its product had a molecular weight of 32,000. Actin was also degraded only slowly, and no liberated product could be detected. Morphological changes in myofibrils prepared from glycerinated psoas muscle of rabbit during incubation with cathepsin B were observed. Three notable phenomena were observed: 1) disappearance of the Z-band in the early stage of incubation, 2) disappearance of the M-line following loss of the Z-band, and 3) decrease in the density of the A-band after swelling of the myofibrils.

Actins↗
PubMed1981

Effects of cathepsin B, H, and D in pectoral muscle of dystrophic chickens (line 413) of in vivo administration of E-64-c (N-[N-(L-3-transcarboxyoxirane-2-carbonyl)-L-leucyl]-3-methyl-butylamine).

The total activities of cathepsin B and cathepsin H in pectoral muscle of dystrophic chickens (Line 413) were about two times higher than in control chickens (Line 412), and cathepsin D activity was about 3 times higher in this muscle in the dystrophic chickens. When E-64-c, a synthesized potent thiol inhibitor was injected subcutaneously, in various doses, daily for 80 days into dystrophic chickens (L 413), the activities of cathepsin B and cathepsin H were reduced to the levels in control chickens (Line 412), but cathepsin D activity, which is insensitive to E-64-c in vitro, was not changed.

Animals↗
PubMed1981

Adenylate cyclase activation and competitive binding with renal tissue using synthetic eel calcitonin analog and its fragments.

The structure-function relationship of calcitonin (CT) was investigated using a synthetic eel CT (E-CT) analog and its fragments. Adenylate cyclase activation and competitive binding to rat renal receptors were used as parameters of function. [Asu1,7]E-CT analog, synthesized by replacing the S-S bond of Cys1-Cys7 in the natural hormone with ethylene linkage of 1-amino suberic acid (Asu), and E-CT fragment 11-32 had about 1/5th and 1/50th the potencies of synthetic E-CT, respectively, in both adenylate cyclase activation and competitive inhibition of 125I-labeled [Asu1,7]iodo-E-CT binding on rat renal plasma membranes. The minimal chain length required to activate adenylate cyclase in rat renal plasma membranes was between 12-18 amino acids, and the minimal chain length required to affect the CT receptor binding was between 6-12 amino acids, near the C-terminus. Fragments, including the C-terminus, show a disproportionate and potent inhibition of the binding compared with the potency required for adenylate cyclase activation. Thus, the amino acid sequence near the C-terminus probably plays an important role in the binding of CT to the receptor. (Endocrinology 108: 698, 1981.)

Adenylyl Cyclases↗