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Biomedical subjects

Y Suhara

Publications and source records attributed to Y Suhara.

53 records · Page 3Linked to original sources

Desferrioxamine B, an inhibitor of Escherichia coli motility, reversing the stimulating effect of cyclic adenosine 3',5'-monophosphate.

A substance inhibiting Escherichia coli motility was isolated by "motilometry" assay from the culture broth of Streptomyces sp. strain NR9GG8 and was found to be identical with desferrioxamine B. Its inhibitory effect was reversed by cyclic adenosine 3',5'-monophosphate (cAMP), while the motility stimulation by cAMP was diminished by this inhibitor. Its effects on various enzymes involved in cAMP metabolism of function of cAMP were examined.

Cyclic AMP↗

A new antibiotic, fumaramidmycin I. Production, biological properties and characterization of producer strain.

A new antibiotic, fumaramidmycin, has been isolated from a streptomycete NR-7GG1 which was characterized and named Streptomyces kurssanovii. The strain produced the antibiotic only when grown on agar plates but not in the submerged culture broth, where the contact with the vegetative mycelia appears to cause the inactivation of the antibiotic. The antibiotic shows an antimicrobial activity against both Gram-positive and Gram-negative bacteria.

Animals↗

A new antibiotic, fumaramidmycin. II. Isolation, structure and syntheses.

A new antibiotic fumaramidmycin produced by Streptomyces kurssanovii NR-7GG1 was isolated as colorless crystals. The structure was shown to be N-(phenylacetyl) fumaramide. Starting from fumaramic acid, fumaramidmycin has been synthesized in good yield, in which the key stage involves N-acylated imino ether formation followed by mild acid hydrolysis. Five analogues of fumaramidmycin have also been prepared.

Anti-Bacterial Agents↗

Restoration by recombinant interferon alpha A/D of host defense systems against tumor in immunosuppressed mice.

Recombinant human interferon alpha A/D (alpha A/D) restored or augmented host defense systems against tumors in immunosuppressed mice. In normal C57BL/6 mice, inoculation of B16 melanoma F1 cells caused few pulmonary metastasis, whereas in mice pretreated with cyclophosphamide (CY) it caused a high incidence of pulmonary metastasis, leading to earlier death than in the normal mice inoculated with the same dose of the tumor. alpha A/D given after the CY treatment counteracted the deleterious effects of the CY treatment. Since such restorative activity was seen even against the subline of B16 F1 which had been made resistant to its direct antiproliferative effect, alpha A/D seems to exert its effect indirectly through host defense systems. However, this activity of alpha A/D in the mice pretreated with CY was abrogated by inoculation of anti-asialo GM1 serum but not by i-carrageenan. The CY treatment reduced NK activity, while alpha A/D given after the CY treatment restored or augmented the NK cell activity in lung cells and peripheral blood mononuclear cells, but not in spleen cells. These findings suggest that the restoration or augmentation of NK activity in the lung and/or peripheral blood might be the major factor leading to the antimetastatic activity of alpha A/D in the mice treated with CY.

Animals↗

Antitumor and antimetastatic activities of human recombinant interferon alpha A/D.

Human recombinant interferon alpha A/D (alpha A/D) was examined for its antitumor activity in several mouse tumor models using metastatic tumors, such as B16 melanoma F1, BL6 and F10, UV2237m fibrosarcoma, and K1735m melanoma. Therapeutic treatment with alpha A/D reduced the incidence of pulmonary metastasis and inhibited the tumor growth resulting in an increase of the mean survival time. Since alpha A/D also showed a prophylactic activity against the metastasis, its antitumor activity was suggested to be due to augmentation of the host defense systems. This was confirmed by the fact that alpha A/D inhibited the in vivo growth and incidence of pulmonary metastasis of B16 F1 sublines regardless of their sensitivity to the direct antiproliferative activity of the IFN in vitro.

Animals↗