fostriecin/סרטן

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In vitro activity of the novel antitumor antibiotic fostriecin (CI-920) in a human tumor cloning assay.

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התחבר הרשם

A human tumor cloning assay was utilized to evaluate the antineoplastic activity of the novel antitumor antibiotic fostriecin (CI-920). Initial screening with 10.0 mcg/ml continuous exposure against a variety of histologic tumor types resulted in 14/51 (27%) in vitro responses (defined as greater

Comparison of the effects of flavone acetic acid, fostriecin, homoharringtonine and tumour necrosis factor alpha on colon 38 tumours in mice.

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התחבר הרשם

Advanced subcutaneous Colon 38 tumours in mice were used for the assessment of activity of a number of anticancer drugs. Activity was measured by histological examination of tumours 24 h after a single dose of the drug and in some cases by tumour growth delay. Agents thought to exert their cytotoxic

Purification of protein phosphatase 4 catalytic subunit: inhibition by the antitumour drug fostriecin and other tumour suppressors and promoters.

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התחבר הרשם

Protein phosphatase 4 (PP4) is a protein serine/threonine phosphatase that predominantly localises to centrosomes and plays a role in microtubule organisation at centrosomes. Here, PP4 catalytic subunit has been purified from porcine testis to near homogeneity and a specific activity of 680 mU/mg

Total Synthesis of Fostriecin (CI-920) We thank Professor Andrew G. Myers and Scott E. Schaus for helpful discussions, and Dr. Alexandra E. Gould and Isabel K. Reichardt for important preliminary experimental work. We also thank Dr. Robert J. Schultz of the Drug Synthesis and Chemistry Branch, Developmental Therapeutics Program, Division of Cancer Treatment and Diagnosis, National Cancer institute, for a sample of natural fostriecin. This work was supported by the NIH (GM-59316), and by Beinecke Memorial and NSF predoctoral fellowships to D.E.C.

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התחבר הרשם

Chemical agents that promote chromatin compaction radiosensitize tumour cells.

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התחבר הרשם

OBJECTIVE Previous studies indicated that cells whose chromatin is naturally compacted at the time of radiation are hypersensitive to radiation-induced killing, primarily by single-hit inactivation. Some chemicals that are known to promote chromatin compaction in interphase cells are here

Phase I and pharmacokinetic study of the topoisomerase II catalytic inhibitor fostriecin.

רק משתמשים רשומים יכולים לתרגם מאמרים

התחבר הרשם

We conducted a phase I and pharmacokinetic study of the topoisomerase II catalytic inhibitor fostriecin. Fostriecin was administered intravenously over 60 min on days 1-5 at 4-week intervals. Dose was escalated from 2 mg m(-2) day(-1) to 20 mg m(-2) day(-1) in 20 patients. Drug pharmacokinetics was

The antitumor drug fostriecin induces vimentin hyperphosphorylation and intermediate filament reorganization.

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התחבר הרשם

Fostriecin is an antitumor drug in phase I clinical trials. We have recently shown that it is a potent inhibitor of protein phosphatases 1 and 2A in vitro, a property not previously described for an antitumor drug. We have investigated its effects on protein phosphorylation in baby hamster kidney

Fostriecin: a review of the preclinical data.

רק משתמשים רשומים יכולים לתרגם מאמרים

התחבר הרשם

Fostriecin is a novel antitumor antibiotic. In vitro studies showed that fostriecin inhibits DNA topoisomerase II (Topo II) catalytic activity, protein phosphatases involved with cell-cycle control and histone phosphatases. The relative contribution of these mechanisms to the antitumor activity has

Determination of fostriecin pharmacokinetics in plasma using high-pressure liquid chromatography assay.

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התחבר הרשם

Fostriecin is an antitumor antibiotic with marked activity against ovarian, breast, and lung cancer cell lines in the human tumor clonogenic assay. The mechanism of cytotoxicity in vivo is unknown; in vitro it has been shown to inhibit macromolecular synthesis, interact with the reduced folate

Antimycotic effects of the novel antitumor agents fostriecin (CI-920), PD 113,270 and PD 113,271.

רק משתמשים רשומים יכולים לתרגם מאמרים

התחבר הרשם

The novel fermentation products fostriecin and analogs PD 113,270 and PD 113,271 are structurally related polyene lactone phosphates that have antitumor activity in vitro and in vivo. They have no antibacterial effects, but they were inhibitory to yeasts (agar diffusion method) with MICs of 3

Phase I and pharmacokinetic study of fostriecin given as an intravenous bolus daily for five consecutive days.

רק משתמשים רשומים יכולים לתרגם מאמרים

התחבר הרשם

Fostriecin (CI-920) is a potent inhibitor of protein phosphatase 2A (PP2A) and protein phosphatase 4(PP4) found to have anticancer activity in preclinical testing. A phase I study was conducted to evaluate the maximum-tolerated dose (MTD), toxicity profile, and pharmacokinetics (PK) of this drug.

Suppression of Ser/Thr phosphatase 4 (PP4C/PPP4C) mimics a novel post-mitotic action of fostriecin, producing mitotic slippage followed by tetraploid cell death.

רק משתמשים רשומים יכולים לתרגם מאמרים

התחבר הרשם

Fostriecin is a natural product purified from Sterptomyces extracts with antitumor activity sufficient to warrant human clinical trials. Unfortunately, difficulties associated with supply and stable drug formulation stalled further development. At a molecular level, fostriecin is known to act as a

Catalytic topoisomerase II inhibitors in cancer therapy.

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התחבר הרשם

The nuclear enzyme DNA topoisomerase II is a major target for antineoplastic agents. All topoisomerase II-directed agents are able to interfere with at least one step of the catalytic cycle. Agents able to stabilize the covalent DNA topoisomerase II complex (also known as the cleavable complex) are

Type 2A protein phosphatase, the complex regulator of numerous signaling pathways.

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התחבר הרשם

Type 2A protein phosphatase (PP2A) comprises a diverse family of phosphoserine- and phosphothreonine-specific enzymes ubiquitously expressed in eukaryotic cells. Common to all forms of PP2A is a catalytic subunit (PP2Ac) which can form two distinct complexes, one with a structural subunit termed

Nuclear localization of protein phosphatase 5 is dependent on the carboxy-terminal region.

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התחבר הרשם

Endogenous and overexpressed protein phosphatase 5 (PP5) localizes to the nucleus and cytoplasm of HeLa cells, while the overexpressed TPR domain of PP5 is restricted to the cytoplasm. Deletion and mutational analysis of human PP5 demonstrates that the C-terminal amino acids 420-499 are essential

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Herbal & Natural Medicine

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