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Chemical Compound Review

CHEMBL9806     N-[4-(acridin-9- ylamino)phenyl]methanesulf...

Synonyms: CCRIS 4546, AG-F-83732, Neuro_000088, LS-90172, CTK4J8153, ...
 
 
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Disease relevance of AMSA

 

High impact information on AMSA

  • Murine P388 (P) leukemia cell lines resistant to amsacrine (P/AMSA), dactinomycin (P/DACT), and doxorubicin (P/DOX) were compared with the parental strain in their sensitivity to a number of derivatives of amsacrine [4].
  • CEM/VM-1, CEM/VM-1-5, and HL-60/AMSA human leukemic cell lines were used as controls; 3 of 3 known mutations were detected by migration differences of polymerase chain reaction products from the RNA extracted from these three lines [5].
  • Thus far, the HL-60/AMSA genotype has not been identified in the cells from any individual, suggesting that this genotype is indeed a mutation and not an allelic form of topoisomerase II [6].
  • Efficacy and clinical cross-resistance of a new combination therapy (AMSA/VP16) in previously treated patients with acute nonlymphocytic leukemia [7].
  • No base-pair specificity could be confirmed; however, a high affinity of AMSA to poly(A) chains was demonstrated [8].
 

Chemical compound and disease context of AMSA

 

Biological context of AMSA

  • Structure-activity relationships for thiolytic cleavage rates of antitumor drugs in the 4'-(9-acridinylamino)methanesulfonanilide series [14].
  • The intercalator resistance and etoposide sensitivity of the HL-60/AMSA cells themselves were confirmed, and the stability of this pharmacologic phenotype over many hundreds of cell generations was demonstrated [15].
  • Topo I/AMSA was found to be about 7-fold less sensitive to CPT than Topo I/p, suggesting the possible involvement of a mutation outside the gene region sequenced (codons 420 to 642) or post-translational modifications of the Topo I enzyme [16].
  • Interestingly this line was hypersensitive to camptothecin, a specific inhibitor of topoisomerase I. Restriction endonuclease patterns of the topoisomerase I and topoisomerase II loci were found to be identical in CALc18/AMSA and CALc18 with no evidence of gene amplification and rearrangements [17].
  • Effects of AMSA, an antineoplastic agent, on spermatogenesis in the mouse [18].
 

Anatomical context of AMSA

  • Investigation of the use of AMSA either prior to bone marrow transplantation in leukaemia or in association with autologous marrow transplant in neuroblastoma and other solid tumours may be of value [19].
  • Relative organ concentrations were similar to those found in mice, except that mice have high AMSA concentration in their spleens whereas our patients did not, even when the spleen was infiltrated with leukemic cells [20].
  • The sensitivity of germ cells to AMSA at other stages of differentiation was determined by semiquantitative histologic analysis at 11 days after treatment [18].
  • Both the SDS/KCl precipitation assay and the filter-binding assay detected etoposide-induced DNA-protein cross-links in HL-60 and HL-60/AMSA cells and detected a greater frequency of amsacrine-induced DNA-protein cross-links in HL-60 cells than in HL-60/AMSA cells [21].
  • One patient with ventricular fibrillation and seizures had high tissue AMSA concentrations in myocardium, but low concentrations in brain [20].
 

Associations of AMSA with other chemical compounds

 

Gene context of AMSA

  • The two drugs were selected on the basis of their activity in these clones, since AMSA is equally active in cells expressing mutated or wild-type (wt) p53, while DX was much less cytotoxic in cells expressing wt p53 [25].
  • In the case of ADR, the ability to circumvent the resistance of HL-60/AMSA suggests additional, non-topoisomerase II-mediated mechanisms of cytolysis that may also explain the broad spectrum of clinical activity of ADR [26].
  • Relative organ concentrations of AMSA varied from patient to patient; however, concentrations were generally highest in gallbladder, liver, and kidney, while low levels were generally but not invariably found in lung, testicle, muscle, fat, spleen, bladder, pancreas, colon, prostate, and brain [20].
  • Twenty-five consecutive leukemia patients (21 AML, 4 ALL) with either primary resistance (n = 22) or resistant relapse (n = 3) of all FAB subtypes were treated with 1 or 2 cycles of ID-ara C (1 g/m2 i.v. q 12 h, days 1-6) and AMSA (120 mg/m2 i.v., days 5-7) [27].
  • With this new advanced system in the maxillary arch, the AMSA injection offers clinical advantages over traditional anesthesia techniques, according to Dr. Mark Friedman, whom I consulted with earlier this year [28].
 

Analytical, diagnostic and therapeutic context of AMSA

  • A number of different dose schedules of AMSA were explored, and we conclude that the optimum dose of AMSA for remission induction in acute leukemia is 120 mg/sq m/day for 5 days [3].
  • N417/AMSA cells, about 80-fold resistant to mAMSA [4'-(9-acridinylamino)-methanesulfon-m-anisidide], were obtained by serial passages of the parental human small cell lung carcinoma NCI-N417 (N417/p) in stepwise drug concentrations [16].
  • The 36 patients (23%) with inadequate cytoreduction after the 6 d of ara-C alone were randomly assigned either to no further chemotherapy (21 patients) or to 3 d of AMSA (15 patients) [29].
  • High tissue concentrations of AMSA were still present 2 weeks after treatment [20].
  • Concentrations of AMSA were determined by HPLC in autopsy tissue samples from five patients who had received the drug antemortem [20].

References

  1. Ventricular fibrillation, hypokalemia, and AMSA therapy. Foldes, J.A., Yagil, Y., Kornberg, A. Ann. Intern. Med. (1982) [Pubmed]
  2. Initial experience with AMSA as single agent treatment against malignant lymphoproliferative disorders. Cabanillas, F., Legha, S.S., Bodey, G.P., Freireich, E.J. Blood (1981) [Pubmed]
  3. Evaluation of AMSA in previously treated patients with acute leukemia: results of therapy in 109 adults. Legha, S.S., Keating, M.J., McCredie, K.B., Bodey, G.P., Freireich, E.J. Blood (1982) [Pubmed]
  4. Design of DNA intercalators to overcome topoisomerase II-mediated multidrug resistance. Baguley, B.C., Holdaway, K.M., Fray, L.M. J. Natl. Cancer Inst. (1990) [Pubmed]
  5. Single-strand conformational polymorphism analysis of the M(r) 170,000 isozyme of DNA topoisomerase II in human tumor cells. Danks, M.K., Warmoth, M.R., Friche, E., Granzen, B., Bugg, B.Y., Harker, W.G., Zwelling, L.A., Futscher, B.W., Suttle, D.P., Beck, W.T. Cancer Res. (1993) [Pubmed]
  6. Identification of a point mutation in the topoisomerase II gene from a human leukemia cell line containing an amsacrine-resistant form of topoisomerase II. Hinds, M., Deisseroth, K., Mayes, J., Altschuler, E., Jansen, R., Ledley, F.D., Zwelling, L.A. Cancer Res. (1991) [Pubmed]
  7. Efficacy and clinical cross-resistance of a new combination therapy (AMSA/VP16) in previously treated patients with acute nonlymphocytic leukemia. Tschopp, L., von Fliedner, V.E., Sauter, C., Maurice, P., Gratwohl, A., Fopp, M., Cavalli, F. J. Clin. Oncol. (1986) [Pubmed]
  8. Interaction of the antitumour drug 4'-(9-acridinylamino)-methanesulfon-m-anisidine.HCl (m-AMSA) with nucleic acids. Hudecz, F., Kajtár, J., Szekerke, M. Nucleic Acids Res. (1981) [Pubmed]
  9. Phase II study of AMSA and doxorubicin to treat metastatic breast cancer. Casimir, M.T., Buzdar, A.U., Blumenschein, G.R., Hortobagyi, G.N., Bodey, G.P. Oncology (1986) [Pubmed]
  10. Phase II study of AMSA alone and in combination with DTIC in patients with metastatic melanoma. Polyzos, A., Legha, S.S., Burgess, A.M., Benjamin, R.S., Bodey, G.P. Investigational new drugs. (1988) [Pubmed]
  11. Quantitation of drug sensitivity by human metastatic melanoma colony-forming units. Meyskens, F.L., Moon, T.E., Dana, B., Gilmartin, E., Casey, W.J., Chen, H.S., Franks, D.H., Young, L., Salmon, S.E. Br. J. Cancer (1981) [Pubmed]
  12. Pilot studies of various combinations of dibromodulcitol, VP-16, and AMSA. Eagan, R.T. Oncology (1982) [Pubmed]
  13. Frameshift mutagenesis by 9-aminoacridine, ICR191, AMSA and related experimental antitumour acridines in recA+ and recA1 strains of Salmonella typhimurium. Ferguson, L.R., MacPhee, D.G. Mutat. Res. (1983) [Pubmed]
  14. Structure-activity relationships for thiolytic cleavage rates of antitumor drugs in the 4'-(9-acridinylamino)methanesulfonanilide series. Cain, B.R., Wilson, W.R., Baguley, B.C. Mol. Pharmacol. (1976) [Pubmed]
  15. Further characterization of an amsacrine-resistant line of HL-60 human leukemia cells and its topoisomerase II. Effects of ATP concentration, anion concentration, and the three-dimensional structure of the DNA target. Mayes, J., Hinds, M., Soares, L., Altschuler, E., Kim, P., Zwelling, L.A. Biochem. Pharmacol. (1993) [Pubmed]
  16. A human small cell lung carcinoma cell line, resistant to 4'-(9-acridinylamino)-methanesulfon-m-anisidide and cross-resistant to camptothecin with a high level of topoisomerase I. Prost, S., Riou, G. Biochem. Pharmacol. (1994) [Pubmed]
  17. Study of molecular markers of resistance to m-AMSA in a human breast cancer cell line. Decrease of topoisomerase II and increase of both topoisomerase I and acidic glutathione S transferase. Lefevre, D., Riou, J.F., Ahomadegbe, J.C., Zhou, D.Y., Benard, J., Riou, G. Biochem. Pharmacol. (1991) [Pubmed]
  18. Effects of AMSA, an antineoplastic agent, on spermatogenesis in the mouse. da Cunha, M.F., Meistrich, M.L., Finch-Neimeyer, M.V. J. Androl. (1985) [Pubmed]
  19. Phase I and II study of AMSA in childhood tumours. Goldman, A., Malpas, J.S. Cancer Chemother. Pharmacol. (1982) [Pubmed]
  20. Human tissue distribution of 4'-(9-acridinylamino)-methanesulfon-m-anisidide (NSC 141549, AMSA). Stewart, D.J., Zhengang, G., Lu, K., Savaraj, N., Feun, L.G., Luna, M., Benjamin, R.S., Keating, M.J., Loo, T.L. Cancer Chemother. Pharmacol. (1984) [Pubmed]
  21. Quantification of topoisomerase-DNA complexes in leukemia cells from patients undergoing therapy with a topoisomerase-directed agent. Ellis, A.L., Nowak, B., Plunkett, W., Zwelling, L.A. Cancer Chemother. Pharmacol. (1994) [Pubmed]
  22. Characterization of an amsacrine-resistant line of human leukemia cells. Evidence for a drug-resistant form of topoisomerase II. Zwelling, L.A., Hinds, M., Chan, D., Mayes, J., Sie, K.L., Parker, E., Silberman, L., Radcliffe, A., Beran, M., Blick, M. J. Biol. Chem. (1989) [Pubmed]
  23. In vitro evaluation of the cardiotoxic potential of AMSA. Lowe, M.C. Cancer treatment reports. (1982) [Pubmed]
  24. Innovations in integrative healthcare education: the AMSA CAM education projects and the University of New Mexico Integrative Medicine Program. Sierpina, V., Kreitzer, M.J., Rakel, D., Shelley, B., Hedgecock, J., Prasad, A. Explore (New York, N.Y.) (2006) [Pubmed]
  25. Changes in cyclins and cyclin-dependent kinases induced by DNA damaging agents in a human ovarian cancer cell line expressing mutated or wild-type P53. Vikhanskaya, F., Erba, E., D'Incalci, M., Broggini, M. Exp. Cell Res. (1996) [Pubmed]
  26. Circumvention of resistance by doxorubicin, but not by idarubicin, in a human leukemia cell line containing an intercalator-resistant form of topoisomerase II: evidence for a non-topoisomerase II-mediated mechanism of doxorubicin cytotoxicity. Zwelling, L.A., Bales, E., Altschuler, E., Mayes, J. Biochem. Pharmacol. (1993) [Pubmed]
  27. Phase-II study of treatment of refractory acute leukemia with intermediate-dose cytosine arabinoside and amsacrine. Jehn, U., Heinemann, V. Ann. Hematol. (1993) [Pubmed]
  28. New horizons in local anesthesia. Lackey, A.D. Dentistry today. (1998) [Pubmed]
  29. The selective use of AMSA following high-dose cytarabine in patients with acute myeloid leukaemia in relapse: a Leukemia Intergroup study. Larson, R.A., Day, R.S., Azarnia, N., Bennett, J.M., Browman, G., Goldberg, J., Gottlieb, A., Grunwald, H., Miller, K., Raza, A. Br. J. Haematol. (1992) [Pubmed]
 
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