iodipine and iodomycin

iodipine has been researched along with iodomycin* in 2 studies

Other Studies

2 other study(ies) available for iodipine and iodomycin

Article	Year
Iodomycin and iodipine, a structural analogue of azidopine, bind to a common domain in hamster P-glycoprotein. European journal of biochemistry, 1999, Volume: 264, Issue:3 Both the overexpression of P-glycoprotein and the broad range of substrates of this ATP-binding cassette (ABC) transporter induce the phenomenon of multidrug resistance, one major cause of the failure of cancer chemotherapy in humans. This study reports that [125I]iodipine, a structural analogue of the 1,4-dihydropyridine azidopine, shares a common binding site with iodomycin, a Bolton-Hunter derivative of the anthracycline daunomycin. This binding site is different from that described for iodoarylazidoprazosin, which is presumed to share a common binding site with azidopine. Edman sequencing revealed that [125I]iodipine had photolabelled the same peptide as iodomycin and spans the primary sequence of hamster isoform pgp1 from amino acid 230 to amino acid 312. Topics: Affinity Labels; Animals; ATP Binding Cassette Transporter, Subfamily B, Member 1; Azides; Binding Sites; CHO Cells; Cricetinae; Daunorubicin; Dihydropyridines; Drug Resistance, Multiple; Humans; Iodine Radioisotopes; Iodobenzenes	1999
Selection and characterization of verapamil-resistant multidrug resistant cells. Biochemical and biophysical research communications, 1995, Apr-17, Volume: 209, Issue:2 Multidrug resistant cells may become acutely sensitive to the calcium channel blocker verapamil, in spite of the fact that its accumulation by these cells is negligible. We selected verapamil-resistant mutants from multidrug resistant Chinese hamster ovary cells. Levels of P-glycoprotein expression and cross-resistance profiles remained unaltered in the verapamil-resistant multidrug resistant cells. As well, a photoactive verapamil analog specifically bound to P-glycoprotein in these cells. We had previously used a photoactive anthracycline to show that calcium antagonists and several anticancer drugs bind to P-glycoprotein at overlapping or interacting sites. Verapamil and its analogues no longer inhibit the binding of either anticancer drugs or calcium channel blockers to P-glycoprotein. Sequencing of P-glycoprotein revealed that no change had occurred in the coding sequence as a result of the selection procedure. Topics: Amino Acid Sequence; Animals; ATP Binding Cassette Transporter, Subfamily B, Member 1; CHO Cells; Cricetinae; Daunorubicin; Drug Resistance, Multiple; In Vitro Techniques; Iodobenzenes; Photochemistry; Protein Binding; Verapamil; Vinblastine	1995

Article

Year

Iodomycin and iodipine, a structural analogue of azidopine, bind to a common domain in hamster P-glycoprotein.

European journal of biochemistry, 1999, Volume: 264, Issue:3

Both the overexpression of P-glycoprotein and the broad range of substrates of this ATP-binding cassette (ABC) transporter induce the phenomenon of multidrug resistance, one major cause of the failure of cancer chemotherapy in humans. This study reports that [125I]iodipine, a structural analogue of the 1,4-dihydropyridine azidopine, shares a common binding site with iodomycin, a Bolton-Hunter derivative of the anthracycline daunomycin. This binding site is different from that described for iodoarylazidoprazosin, which is presumed to share a common binding site with azidopine. Edman sequencing revealed that [125I]iodipine had photolabelled the same peptide as iodomycin and spans the primary sequence of hamster isoform pgp1 from amino acid 230 to amino acid 312.

Topics: Affinity Labels; Animals; ATP Binding Cassette Transporter, Subfamily B, Member 1; Azides; Binding Sites; CHO Cells; Cricetinae; Daunorubicin; Dihydropyridines; Drug Resistance, Multiple; Humans; Iodine Radioisotopes; Iodobenzenes

1999

Selection and characterization of verapamil-resistant multidrug resistant cells.

Biochemical and biophysical research communications, 1995, Apr-17, Volume: 209, Issue:2

Multidrug resistant cells may become acutely sensitive to the calcium channel blocker verapamil, in spite of the fact that its accumulation by these cells is negligible. We selected verapamil-resistant mutants from multidrug resistant Chinese hamster ovary cells. Levels of P-glycoprotein expression and cross-resistance profiles remained unaltered in the verapamil-resistant multidrug resistant cells. As well, a photoactive verapamil analog specifically bound to P-glycoprotein in these cells. We had previously used a photoactive anthracycline to show that calcium antagonists and several anticancer drugs bind to P-glycoprotein at overlapping or interacting sites. Verapamil and its analogues no longer inhibit the binding of either anticancer drugs or calcium channel blockers to P-glycoprotein. Sequencing of P-glycoprotein revealed that no change had occurred in the coding sequence as a result of the selection procedure.

Topics: Amino Acid Sequence; Animals; ATP Binding Cassette Transporter, Subfamily B, Member 1; CHO Cells; Cricetinae; Daunorubicin; Drug Resistance, Multiple; In Vitro Techniques; Iodobenzenes; Photochemistry; Protein Binding; Verapamil; Vinblastine

1995