K1115 A, a New Anthraquinone Derivative that Inhibits the Binding of Activator Protein-1 (AP-1) to its Recognition Sites I. Biological Activities

MASAKI GOTO; MASA-AKI MASEGI; TOSHIHIKO YAMAUCHI; KEN-ICHI CHIBA; YOSHIKAZU KUBOI; KOUKICHI HARADA; NOBUAKI NARUSE

doi:10.7164/antibiotics.51.539

K1115 A, a New Anthraquinone Derivative that Inhibits the Binding of Activator Protein-1 (AP-1) to its Recognition Sites

I. Biological Activities

MASAKI GOTO, MASA-AKI MASEGI, TOSHIHIKO YAMAUCHI, KEN-ICHI CHIBA, YOSHIKAZU KUBOI, KOUKICHI HARADA, NOBUAKI NARUSE

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JOURNAL FREE ACCESS

1998 Volume 51 Issue 6 Pages 539-544

DOI https://doi.org/10.7164/antibiotics.51.539

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Abstract

K1115 A, a new anthraquinone derivative, was isolated from the culture broth of Streptomyces griseorubiginosus (Mer-K1115). K1115A inhibited the direct binding of activator protein-1 (AP-1) to AP-1 oligonucleotide (IC₅₀ = 100 μM), and the production of collagenase in IL-1α-stimulated rat synovial cells (IC₅₀ = 60 μM). In vivo, the application of K1115 A decreased phorbol myristate acetate (PMA)-induced mouse ornithine decarboxylase (ODC) activity. These results indicated that K1115 A is able to attenuate the inflammatory response mediated by AP-1.

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