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Chemical Compound Review

Congo red     disodium 4-amino-3-[4-[4-(1-amino-4...

Synonyms: Kongorot, Haemonorm, Solucongo, Hemorrhagyl, Haemomedical, ...
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Disease relevance of Congo red


Psychiatry related information on Congo red

  • After being stained with Congo red dye, the protein polymers from patients with Creutzfeldt-Jakob disease exhibited green birefringence when examined under polarized light [6].
  • These spherical amyloid deposits were very similar to Congo red-stained amyloid plaques in human Alzheimer's disease brain, and in vitro data suggest that they were probably formed in vivo following interactions with endogenous brain components [7].
  • At necropsy, a patient with dementia had multicentric and diffuse plaques stained with PrP antiserum, but not with haematoxylin and eosin or Congo red, in the cerebral and cerebellar cortices [8].
  • This strategy was used to examine the function of the major Congo red receptor of the myxobacterium Myxococcus xanthus, which has a developmental cycle that involves social interactions among cells [9].

High impact information on Congo red

  • Arrays of prion rods ultrastructurally resembled purified amyloid and showed green birefringence by polarization microscopy after staining with Congo red dye [10].
  • Numerous Abeta plaques that stained with Congo red dye were present in cortical and limbic structures of mice with elevated amounts of Abeta [11].
  • Significant increases in Congo red staining were observed in animals infused with A beta plus HSPG versus those infused with only A beta [7].
  • By 7 weeks, only animals infused with A beta plus HSPG demonstrated compaction of the Congo red material from amorphous, wispy deposits (at 1 week) to stellate deposits resembling a Maltese cross [7].
  • Using lacZ transcriptional fusions, we found that transcription of virA and four ipaH genes, but not that of the ipaBCDA and mxi operons, was markedly increased during growth in the presence of Congo red and in an ipaD mutant, two conditions in which secretion through the Mxi-Spa machinery is enhanced [12].

Chemical compound and disease context of Congo red


Biological context of Congo red


Anatomical context of Congo red

  • Calcofluor white and Congo red inhibit chitin microfibril assembly of Poterioochromonas: evidence for a gap between polymerization and microfibril formation [23].
  • Furthermore, cell culture studies revealed that the Congo red dye at micromolar concentrations reduced the extent of HD exon 1 aggregation in transiently transfected COS cells [24].
  • However, the removal of YGR189c and YEL040w, but not YLR213c, caused additive sensitivity to compounds that interfere with cell wall construction, such as Congo red and Calcofluor White, and overexpression of YEL040w led to resistance to these compounds [25].
  • In the sporadic form, ApoE-immunoreactive deposits colocalized with Congo red-positive deposits; however, in muscle fibers from patients with hereditary disease there was no congophilia [26].
  • Cytoplasmic hybrid ("cybrid") cells made from mitochondrial DNA of nonfamilial AD subjects show antioxidant-reversible lowering of mitochondrial membrane potential (delta(gYm), secrete twice as much Abeta(1-40) and Abeta(1-42), have increased intracellular Abeta(1-40) (1.7-fold), and develop Congo red-positive Abeta deposits [27].

Associations of Congo red with other chemical compounds

  • One hundred percent of animals receiving infusions of synthetic beta-amyloid protein (A beta 1-40) plus a specific heparan sulfate proteoglycan (HSPG) for 1 week or 7 weeks (following 2 week infusions) demonstrated Congo red and thioflavin S-positive deposits adjacent to the infusion site [7].
  • Furthermore, the fibrils exhibit Congo red birefringence, increased fluorescence with thioflavine T and cause a red-shift of the Congo red absorption spectrum [28].
  • These aggregates bind to amyloid-specific dyes Congo red and thioflavin T and to tPA [29].
  • The two components had different binding affinities for heparin and for the amyloid-specific dye Congo red, and the equilibrium between the two forms was dependent on solvent conditions [30].
  • In cerebellum, all plaques containing amyloid cores that were Congo red-positive were also positive for highly sulfated GAGs (by Alcian blue staining at 0.7 mol/L MgCl2) and HSPG (both core protein and GAG chain) immunoreactivity [31].

Gene context of Congo red

  • This gene was named RCR1 (resistance to Congo red 1) [20].
  • Deletion of the gene CWH36 resulted in a severe growth defect on iron-limited medium, as well as increased sensitivity to Congo red and calcofluor white [32].
  • Cultures grown to stationary phase in the presence of Congo red contain extracellular filaments whose composition and morphology are similar to those produced by the hypersecreting ipaB and ipaD mutants [33].
  • The number of neurons was significantly decreased in the areas containing the amyloid cores compared with all other areas and corresponding areas in non-transgenic littermates in sections visualized by Nissl plus Congo red double staining (p<0.001) [34].
  • Congo red binding, HeLa cell invasion, and Ipa excretion were restored in two avirulent mxiA fusion mutants when they were transformed with a cloned copy of the mxiA gene [35].

Analytical, diagnostic and therapeutic context of Congo red


  1. Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae. Glover, J.R., Kowal, A.S., Schirmer, E.C., Patino, M.M., Liu, J.J., Lindquist, S. Cell (1997) [Pubmed]
  2. Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders. Sánchez, I., Mahlke, C., Yuan, J. Nature (2003) [Pubmed]
  3. Amyloid fibril in hereditary cerebral hemorrhage with amyloidosis (HCHWA) is related to the gastroentero-pancreatic neuroendocrine protein, gamma trace. Cohen, D.H., Feiner, H., Jensson, O., Frangione, B. J. Exp. Med. (1983) [Pubmed]
  4. Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red. Lorenzo, A., Yankner, B.A. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  5. The 2,6-disubstituted naphthalene derivative FDDNP labeling reliably predicts Congo red birefringence of protein deposits in brain sections of selected human neurodegenerative diseases. Smid, L.M., Vovko, T.D., Popovic, M., Petric, A., Kepe, V., Barrio, J.R., Vidmar, G., Bresjanac, M. Brain Pathol. (2006) [Pubmed]
  6. Creutzfeldt-Jakob disease prion proteins in human brains. Bockman, J.M., Kingsbury, D.T., McKinley, M.P., Bendheim, P.E., Prusiner, S.B. N. Engl. J. Med. (1985) [Pubmed]
  7. An important role of heparan sulfate proteoglycan (Perlecan) in a model system for the deposition and persistence of fibrillar A beta-amyloid in rat brain. Snow, A.D., Sekiguchi, R., Nochlin, D., Fraser, P., Kimata, K., Mizutani, A., Arai, M., Schreier, W.A., Morgan, D.G. Neuron (1994) [Pubmed]
  8. A Japanese family with a variant of Gerstmann-Sträussler-Scheinker disease. Tanaka, Y., Minematsu, K., Moriyasu, H., Yamaguchi, T., Yutani, C., Kitamoto, T., Furukawa, H. J. Neurol. Neurosurg. Psychiatr. (1997) [Pubmed]
  9. Inhibition of cell-cell interactions in Myxococcus xanthus by congo red. Arnold, J.W., Shimkets, L.J. J. Bacteriol. (1988) [Pubmed]
  10. Scrapie prions aggregate to form amyloid-like birefringent rods. Prusiner, S.B., McKinley, M.P., Bowman, K.A., Bolton, D.C., Bendheim, P.E., Groth, D.F., Glenner, G.G. Cell (1983) [Pubmed]
  11. Correlative memory deficits, Abeta elevation, and amyloid plaques in transgenic mice. Hsiao, K., Chapman, P., Nilsen, S., Eckman, C., Harigaya, Y., Younkin, S., Yang, F., Cole, G. Science (1996) [Pubmed]
  12. Induction of type III secretion in Shigella flexneri is associated with differential control of transcription of genes encoding secreted proteins. Demers, B., Sansonetti, P.J., Parsot, C. EMBO J. (1998) [Pubmed]
  13. Inhibition of toxicity in the beta-amyloid peptide fragment beta -(25-35) using N-methylated derivatives: a general strategy to prevent amyloid formation. Hughes, E., Burke, R.M., Doig, A.J. J. Biol. Chem. (2000) [Pubmed]
  14. The potassium permanganate method. A reliable method for differentiating amyloid AA from other forms of amyloid in routine laboratory practice. van Rijswijk, M.H., van Heusden, C.W. Am. J. Pathol. (1979) [Pubmed]
  15. Candida albicans Pmr1p, a secretory pathway P-type Ca2+/Mn2+-ATPase, is required for glycosylation and virulence. Bates, S., MacCallum, D.M., Bertram, G., Munro, C.A., Hughes, H.B., Buurman, E.T., Brown, A.J., Odds, F.C., Gow, N.A. J. Biol. Chem. (2005) [Pubmed]
  16. Gastric emptying in patients with fundal gastritis and gastric cancer. Tatsuta, M., Iishi, H., Okuda, S. Gut (1990) [Pubmed]
  17. Opposite effects of dextran sulfate 500, the polyene antibiotic MS-8209, and Congo red on accumulation of the protease-resistant isoform of PrP in the spleens of mice inoculated intraperitoneally with the scrapie agent. Beringue, V., Adjou, K.T., Lamoury, F., Maignien, T., Deslys, J.P., Race, R., Dormont, D. J. Virol. (2000) [Pubmed]
  18. An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated beta-sheet structure for amyloid. Balbirnie, M., Grothe, R., Eisenberg, D.S. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  19. Congo red and protein aggregation in neurodegenerative diseases. Frid, P., Anisimov, S.V., Popovic, N. Brain Res. Brain Res. Rev. (2007) [Pubmed]
  20. A novel endoplasmic reticulum membrane protein Rcr1 regulates chitin deposition in the cell wall of Saccharomyces cerevisiae. Imai, K., Noda, Y., Adachi, H., Yoda, K. J. Biol. Chem. (2005) [Pubmed]
  21. Characterization of Shigella flexneri sequences encoding congo red binding (crb): conservation of multiple crb sequences and role of IS1 in loss of the Crb+ phenotype. Daskaleros, P.A., Payne, S.M. Infect. Immun. (1986) [Pubmed]
  22. Molecular cloning, nucleotide sequence, and characterization of lppB, encoding an antigenic 40-kilodalton lipoprotein of Haemophilus somnus. Theisen, M., Rioux, C.R., Potter, A.A. Infect. Immun. (1993) [Pubmed]
  23. Calcofluor white and Congo red inhibit chitin microfibril assembly of Poterioochromonas: evidence for a gap between polymerization and microfibril formation. Herth, W. J. Cell Biol. (1980) [Pubmed]
  24. Inhibition of huntingtin fibrillogenesis by specific antibodies and small molecules: implications for Huntington's disease therapy. Heiser, V., Scherzinger, E., Boeddrich, A., Nordhoff, E., Lurz, R., Schugardt, N., Lehrach, H., Wanker, E.E. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  25. A novel family of cell wall-related proteins regulated differently during the yeast life cycle. Rodríguez-Peña, J.M., Cid, V.J., Arroyo, J., Nombela, C. Mol. Cell. Biol. (2000) [Pubmed]
  26. Apolipoprotein E and apolipoprotein E messenger RNA in muscle of inclusion body myositis and myopathies. Mirabella, M., Alvarez, R.B., Engel, W.K., Weisgraber, K.H., Askanas, V. Ann. Neurol. (1996) [Pubmed]
  27. Alzheimer's disease cybrids replicate beta-amyloid abnormalities through cell death pathways. Khan, S.M., Cassarino, D.S., Abramova, N.N., Keeney, P.M., Borland, M.K., Trimmer, P.A., Krebs, C.T., Bennett, J.C., Parks, J.K., Swerdlow, R.H., Parker, W.D., Bennett, J.P. Ann. Neurol. (2000) [Pubmed]
  28. Designing conditions for in vitro formation of amyloid protofilaments and fibrils. Chiti, F., Webster, P., Taddei, N., Clark, A., Stefani, M., Ramponi, G., Dobson, C.M. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  29. Glycation induces formation of amyloid cross-beta structure in albumin. Bouma, B., Kroon-Batenburg, L.M., Wu, Y.P., Brünjes, B., Posthuma, G., Kranenburg, O., de Groot, P.G., Voest, E.E., Gebbink, M.F. J. Biol. Chem. (2003) [Pubmed]
  30. Cleaved beta 2-microglobulin partially attains a conformation that has amyloidogenic features. Heegaard, N.H., Roepstorff, P., Melberg, S.G., Nissen, M.H. J. Biol. Chem. (2002) [Pubmed]
  31. Heparan sulfate proteoglycan in diffuse plaques of hippocampus but not of cerebellum in Alzheimer's disease brain. Snow, A.D., Sekiguchi, R.T., Nochlin, D., Kalaria, R.N., Kimata, K. Am. J. Pathol. (1994) [Pubmed]
  32. Genome-wide analysis of iron-dependent growth reveals a novel yeast gene required for vacuolar acidification. Davis-Kaplan, S.R., Ward, D.M., Shiflett, S.L., Kaplan, J. J. Biol. Chem. (2004) [Pubmed]
  33. Enhanced secretion through the Shigella flexneri Mxi-Spa translocon leads to assembly of extracellular proteins into macromolecular structures. Parsot, C., Ménard, R., Gounon, P., Sansonetti, P.J. Mol. Microbiol. (1995) [Pubmed]
  34. Brain Abeta amyloidosis in APPsw mice induces accumulation of presenilin-1 and tau. Tomidokoro, Y., Harigaya, Y., Matsubara, E., Ikeda, M., Kawarabayashi, T., Shirao, T., Ishiguro, K., Okamoto, K., Younkin, S.G., Shoji, M. J. Pathol. (2001) [Pubmed]
  35. mxiA of Shigella flexneri 2a, which facilitates export of invasion plasmid antigens, encodes a homolog of the low-calcium-response protein, LcrD, of Yersinia pestis. Andrews, G.P., Maurelli, A.T. Infect. Immun. (1992) [Pubmed]
  36. Amyloid beta-protein (Abeta) 1-40 but not Abeta1-42 contributes to the experimental formation of Alzheimer disease amyloid fibrils in rat brain. Shin, R.W., Ogino, K., Kondo, A., Saido, T.C., Trojanowski, J.Q., Kitamoto, T., Tateishi, J. J. Neurosci. (1997) [Pubmed]
  37. Is Congo red an amyloid-specific dye? Khurana, R., Uversky, V.N., Nielsen, L., Fink, A.L. J. Biol. Chem. (2001) [Pubmed]
  38. Ultrastructural immunohistochemical localization of polyclonal IgG, C3, and amyloid P component on the congo red-negative amyloid-like fibrils of fibrillary glomerulopathy. Yang, G.C., Nieto, R., Stachura, I., Gallo, G.R. Am. J. Pathol. (1992) [Pubmed]
  39. Sulfate content and specific glycosaminoglycan backbone of perlecan are critical for perlecan's enhancement of islet amyloid polypeptide (amylin) fibril formation. Castillo, G.M., Cummings, J.A., Yang, W., Judge, M.E., Sheardown, M.J., Rimvall, K., Hansen, J.B., Snow, A.D. Diabetes (1998) [Pubmed]
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