The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Chemical Compound Review

CHEMBL1088472     N'-(2-chloroethyl)-N-(6- chloro-2-methoxy...

Synonyms: ICR 191, LS-119768, BRN 0444928, AC1L1EX1, 17070-44-9, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of ICR 191


High impact information on ICR 191

  • A series of uniflagellar mutants isolated following mutagenesis of Chlamydomonas reinhardtii (strain 137c) with ICR-191 show a remarkable positional phenotype [5].
  • Heteroalleles were generated in the TK+/+ parent B-lymphoblast cell line WIL-2 by repeated exposure to the alkylating nitrogen mustard ICR-191, which preferentially causes +1 or -1 frameshifts [6].
  • Nitrosoguanidine, ethyl methanesulfonate, ICR 191, and x-rays were used [7].
  • Frame-restoring point mutations, restoration of original sequences, and phenocopy reversion by acquisition of aminopterin resistance were also found among X-ray-induced revertants, whereas the ICR-191-induced revertants examined show only loss of the exon 7 frameshift [8].
  • Line 4:2 reverts to TK+ at a lower spontaneous frequency than does 6:86 but can be induced with similar kinetics by ICR-191 [8].

Chemical compound and disease context of ICR 191


Biological context of ICR 191


Anatomical context of ICR 191

  • Despite the greater mutagenic potency in the absence of metabolic systems, ICR 191 was deactivated far more efficiently and rapidly than ICR 170 by a variety of mouse (liver greater than lung) and rat (liver greater than testis greater than kidney greater than lung greater than striated muscle greater than spleen) S-9 fractions [14].
  • In adult fish treated with 1 microM ICR-191 in a water bath for 18 h, a significant increase in MFs was observed in both gill (12 x 10(-5) and 44 x 10(-5) in control and treated fish, respectively), and hepatopancreas (5 x 10(-5) and 29 x 10(-5), respectively) 2 weeks after exposure [15].
  • A collection of HLA-DP mutants was generated, using ICR 191 as the mutagenic agent and resistance to lysis mediated by HLA-DPw2 allospecific cytotoxic T lymphocytes (CTLs) as the selection criterion [16].
  • Variation of the frameshift activity of a mutagen (ICR-191) following nitrosation in human gastric juice [17].

Associations of ICR 191 with other chemical compounds

  • Frame-shift mutants in Namalwa cell cultures were generated with ICR-191, and mutants were then selected for resistance to ricin or resistance to a conjugate of ricin with the anti-CALLA antibody J5 in the presence of lactose [18].
  • Accordingly, we have recently observed that base substitutions induced by the acridine half-mustard ICR-191 in the M13 double-stranded DNA transfection system are predominantly G:C-to-A:T transitions [1].
  • In contrast, ICR-191 and AFB1 are respectively less than 2 and 3% as efficient as MNNG for OUAr mutant induction relative to the activity of each agent for 6TGr mutagenesis [3].
  • 9-Aminoacridine was a potent inducer of +1G, -1G and -1A frameshifts, whereas ICR-191 induced all types of frameshift mutations [19].
  • Among the 8-AGr mutants tested, clone ICR-014 or ICR-172 showed a significant increase in reversion frequency over the control level only after treatment with ICR-191 or 2-NF, respectively; but not with the other two mutagens [20].

Gene context of ICR 191

  • Reversion to Lac+ promoted by ICR-191 results from the loss of a G residue from a GGG sequence located at the junction of lacZ and IS1 [21].
  • (ii) Mutations in mutR can be induced with the frameshift mutagen ICR-191 [22].
  • One frameshift strain, hisC3076, also showed increased sensitivity to mutagenesis by ICR-191 when it carried either of two different polA alleles, whereas the hisD3052 and hisC207 frameshifts reduced sensitivity to mutagenesis in the presence of these alleles [23].
  • Mutational spectrum of ICR-191 at the hprt locus in human lymphoblastoid cells [24].
  • The order of sensitivity to the toxic effect of ICR-191 was MIT-2 greater than WI-L2 greater than GM 130, while the order of sensitivity to the mutagenic effects of this frameshift mutagen was GM 130 greater than MIT-2 greater than WI-L2 [25].

Analytical, diagnostic and therapeutic context of ICR 191

  • In addition to these properties, the mutation lacZ::IS1-MS319 has the unique property of reversion to Lac+ (ts) spontaneously or after treatment with the frameshift mutagen ICR-191; such revertants retain the IS1 element [21].
  • Southern blot hybridization analyses revealed that most XPRT mutant cell lines which arose following treatment with EMS (20/22) or ICR 191 (20/24) exhibited no alterations of the gpt locus detectable by this technique [26].


  1. Specificity of base substitutions induced by the acridine mutagen ICR-191: mispairing by guanine N7 adducts as a mutagenic mechanism. Sahasrabudhe, S.R., Luo, X., Humayun, M.Z. Genetics (1991) [Pubmed]
  2. Mutation induction in Haemophilus influenzae by ICR-191. II. Role of DNA replication and repair. Kimball, R.F., Perdue, S.W. Mutat. Res. (1981) [Pubmed]
  3. Quantitative forward-mutation specificity of mono-functional alkylating agents, ICR-191, and aflatoxin B1 in mouse lymphoma cells. MacInnes, M.A., Friedrich, U., van Daalen Wetters, T., Coffino, P. Mutat. Res. (1982) [Pubmed]
  4. Comparative mutagenicity of ICR-191 to S. typhimurium and diploid human lymphoblasts. Deluca, J.G., Kaden, D.A., Krolewski, J., Skopek, T.R., Thilly, W.G. Mutat. Res. (1977) [Pubmed]
  5. Uniflagellar mutants of Chlamydomonas: evidence for the role of basal bodies in transmission of positional information. Huang, B., Ramanis, Z., Dutcher, S.K., Luck, D.J. Cell (1982) [Pubmed]
  6. A system for assaying homologous recombination at the endogenous human thymidine kinase gene. Benjamin, M.B., Potter, H., Yandell, D.W., Little, J.B. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  7. Mutagenesis in S49 mouse lymphoma cells: induction of resistance to ouabain, 6-thioguanine, and dibutyryl cyclic AMP. Friedrich, U., Coffino, P. Proc. Natl. Acad. Sci. U.S.A. (1977) [Pubmed]
  8. X rays induce interallelic homologous recombination at the human thymidine kinase gene. Benjamin, M.B., Little, J.B. Mol. Cell. Biol. (1992) [Pubmed]
  9. Induction of G.C to A.T transitions by the acridine half-mustard ICR-191 supports a mispairing mechanism for mutagenesis by some bulky mutagens. Sahasrabudhe, S.R., Luo, X., Humayun, M.Z. Biochemistry (1990) [Pubmed]
  10. Isolation of fluoropyrimidine-resistant murine leukemic cell lines by one-step mutation and selection. Mulkins, M.A., Heidelberger, C. Cancer Res. (1982) [Pubmed]
  11. Heavy chain-producing variants of a mouse myeloma cell line. Morrison, S.L., Scharff, M.D. J. Immunol. (1975) [Pubmed]
  12. Genetic and sequence analysis of frameshift mutations induced by ICR-191. Calos, M.P., Miller, J.H. J. Mol. Biol. (1981) [Pubmed]
  13. Effects of an acridine half-mustard (ICR 191) on growth and ploidy of frog cells in culture. Viceps-Madore, D. J. Cell. Physiol. (1978) [Pubmed]
  14. Selective deactivation of ICR mutagens as related to their distinctive pulmonary carcinogenicity. De Flora, S., Morelli, A., Zanacchi, P., Bennicelli, C., De Flora, A. Carcinogenesis (1982) [Pubmed]
  15. Frameshift mutations induced by the acridine mustard ICR-191 in embryos and in the adult gill and hepatopancreas of rpsL transgenic zebrafish. Nakamura, T., Amanuma, K., Aoki, Y. Mutat. Res. (2005) [Pubmed]
  16. Molecular analysis of an HLA-DP mutant cell line selected for its resistance to killing by HLA-DPw2-specific T-cell clones. Arroyo, J., Díez-Orejas, R., Alvarez, A.M., Shaw, S., Sánchez-Pérez, M. Immunogenetics (1994) [Pubmed]
  17. Variation of the frameshift activity of a mutagen (ICR-191) following nitrosation in human gastric juice. De Flora, S., De Flora, A. Cancer Lett. (1981) [Pubmed]
  18. Somatic cell mutants resistant to ricin, diphtheria toxin, and to immunotoxins. Goldmacher, V.S., Anderson, J., Schulz, M.L., Blättler, W.A., Lambert, J.M. J. Biol. Chem. (1987) [Pubmed]
  19. Effects of the umuDC, mucAB, and samAB operons on the mutational specificity of chemical mutagenesis in Escherichia coli: I. Frameshift mutagenesis. Watanabe, M., Nohmi, T., Ohta, T. Mutat. Res. (1994) [Pubmed]
  20. Induction and isolation of frameshift mutants in cultured Chinese hamster DON cells. Hamada, K., Isomura, K., Teranishi, K., Watanabe, H. Mutat. Res. (1978) [Pubmed]
  21. A frameshift mutation at the junction of an IS1 insertion within lacZ restores beta-galactosidase activity via formation of an active lacZ-IS1 fusion protein. Malamy, M.H., Rahaim, P.T., Hoffman, C.S., Baghdoyan, D., O'Connor, M.B., Miller, J.F. J. Mol. Biol. (1985) [Pubmed]
  22. Further characterization of a non-essential mutator gene in Escherichia coli K-12. Hoess, R.H., Fan, D.P. J. Bacteriol. (1975) [Pubmed]
  23. Spontaneous and induced mutability or frameshift strains of Salmonella typhimurium carrying uvrB and polA mutations. Imray, F.P., Macphee, D.G. Mutat. Res. (1976) [Pubmed]
  24. Mutational spectrum of ICR-191 at the hprt locus in human lymphoblastoid cells. Taft, S.A., Liber, H.L., Skopek, T.R. Environ. Mol. Mutagen. (1994) [Pubmed]
  25. Comparison of toxicity and mutagenicity of methylnitrosourea, methylnitronitrosoguanidine and ICR-191 among human lymphoblast lines. Slapikoff, S.A., Andon, B.M., Thilly, W.G. Mutat. Res. (1980) [Pubmed]
  26. Quantitative and molecular analyses of ethyl methanesulfonate- and ICR 191-induced mutation in AS52 cells. Stankowski, L.F., Tindall, K.R., Hsie, A.W. Mutat. Res. (1986) [Pubmed]
WikiGenes - Universities