azidopine and Neoplasms

azidopine has been researched along with Neoplasms* in 2 studies

Other Studies

2 other study(ies) available for azidopine and Neoplasms

ArticleYear
Schisandrin B--a novel inhibitor of P-glycoprotein.
    Biochemical and biophysical research communications, 2005, Sep-23, Volume: 335, Issue:2

    P-glycoprotein-mediated drug efflux is one of the major causes of the cancer multidrug resistance (MDR). Inhibition of P-glycoprotein could reverse cancer MDR. Here, we show that schisandrin B, a naturally occurring compound from Schisandra chinensis (Turcz.) Baill, bears strong potency to inhibit P-glycoprotein. Schisandrin B reversed the drug resistance of four MDR cell lines characterized with overexpression of P-glycoprotein and fully restored the intracellular drug accumulation by interacting with P-glycoprotein. Schisandrin B has a core structure of dibenzocyclooctadiene, representing a novel P-glycoprotein inhibitor. To our best knowledge, the role of schisandrin B to inhibit P-glycoprotein has not been reported.

    Topics: Affinity Labels; ATP Binding Cassette Transporter, Subfamily B; ATP Binding Cassette Transporter, Subfamily B, Member 1; Azides; Cell Line, Tumor; Cell Proliferation; Cyclooctanes; Daunorubicin; Dihydropyridines; Dose-Response Relationship, Drug; Drug Resistance, Multiple; Humans; Inhibitory Concentration 50; K562 Cells; Lignans; Models, Chemical; Neoplasms; Polycyclic Compounds; Protein Binding; Tetrazolium Salts; Thiazoles; Time Factors

2005
[A molecular basis for multidrug resistance and reversal of the resistance].
    Gan to kagaku ryoho. Cancer & chemotherapy, 1989, Volume: 16, Issue:4 Pt 2-1

    Multidrug-resistance is frequently characterized by enhanced drug efflux resulting from a membrane glycoprotein of 170,000 daltons (P-glycoprotein). Analysis of cloned cDNAs for the human MDR 1 gene, whose product is the P-glycoprotein, indicates that P-glycoprotein is an energy-dependent drug-efflux system for cytotoxic hydrophobic anticancer drugs. We have demonstrated that a photoanalog of a reversing agent, SDB-ethylenediamine, specifically binds to P-glycoprotein. The binding site on P-glycoprotein seems to be identical with that of anticancer agents and other reversing agents. On the other hand, the radioactive photoactive dihydropyridine calcium channel blocker, [3H] azidopine, photolabels P-glycoprotein in membrane vesicles from multidrug-resistant cells. This photolabeling is almost completely inhibited by excess dihydropyridine analogs that reverse or lower drug-resistance. In contrast, the labeling is not significantly inhibited by analogs that do not reverse resistance. These results suggest that it may be possible to quickly screen for dihydropyridine analogs that reverse multidrug resistance by measuring the inhibition of [3H] azidopine labeling of P-glycoprotein.

    Topics: Affinity Labels; Antineoplastic Agents; ATP Binding Cassette Transporter, Subfamily B, Member 1; Azides; Dihydropyridines; Drug Resistance; Humans; In Vitro Techniques; Membrane Glycoproteins; Neoplasms

1989