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Protease inhibitor produced by Streptomyces toyocaensis with antimetastatic activity in mice (CROSBI ID 77574)

Prilog u časopisu | izvorni znanstveni rad | međunarodna recenzija

Abramić, Marija ; Gianni, Sava ; Zubanović, Marija ; Vitale, Ljubinka Protease inhibitor produced by Streptomyces toyocaensis with antimetastatic activity in mice // Periodicum biologorum, 98 (1996), 3; 353-360

Podaci o odgovornosti

Abramić, Marija ; Gianni, Sava ; Zubanović, Marija ; Vitale, Ljubinka

engleski

Protease inhibitor produced by Streptomyces toyocaensis with antimetastatic activity in mice

Background and purpose: In multistep processes of tumor invasion and metastasis, the combined action of various proteolytic enzymes has been recognized, making them targets for antiinvasive and antimetastatic therapy. One of the possible approaches to suppress the enhanced proteolysis occurring during cancer progression is the use of low molecular weight protease inhibitors of the microbial origin. In search of serine proteinase inhibitors, we have found that culture filtrate of Streptomyces toyocaensis is a rich source of a trypsin inhibitor. The aim of this study was to isolate protease inhibitor excreted by S. toyocaensis, and to elucidate its structure as well as some of its biological properties. Materials and methods: The inhibitor was purified by ultrafiltration, ion-exchange and adsorption chromatography, solvent extraction and gel filtration procedures, monitoring its activity towards trypsin. TLC, IR and ^1 H NMR spectroscopy, and amino acid analysis, were applied for structure determination of the purified compound. Lewis lung carcinoma model was used for the in vivo antimetastatic studies: following the s.c. implantation of carcinoma tissue into BD2F1 mice, the animals were given isolated compound i.p. Results: The isolated inhibitor was found to be: acetyl-leucyl-valyl(or isoleucyl)-argininal. In vitro it strongly inhibited trypsin, papain and cathepsin B. In mice bearing Lewis lung carcinoma it significantly reduced the number and weight of spontaneous lung metastases, whereas leupeptin was ineffective. Conclusions: This is the first report of isolation and characterization of a protease inhibitor from S. toyocaensis. Although its structure was analogous to that of leupeptin, it differed from this already known microbial protease inhibitor by its potent antimetastatic activity. Therefore, further investigation of biological actions of this newly isolated inhibitor would be of interest.

protease inhibitor; trypsin inhibitor; Streptomyces toyocaensis; Lewis lung carcinoma; antimetastatic activity

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Podaci o izdanju

98 (3)

1996.

353-360

objavljeno

0031-5362

Povezanost rada

Kemija

Indeksiranost