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Chemical Compound Review

ACMC-20mlk5     5-hydroxy-1,7-bis(4-hydroxy- 3-methoxy...

Synonyms: SPBio_001728, AC1L9DEH, CTK0C6210, KBio1_001627, KBio3_003004, ...
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Disease relevance of curcumin

  • CONCLUSIONS: This study has shown for the first time that treatment with curcumin can prevent and improve murine experimental colitis [1].
  • The aim of this study was to determine whether treatment with curcumin prevents and ameliorates colonic inflammation in a mouse model of inflammatory bowel disease [1].
  • We report that topotecan, beta-lapachone, and curcumin are potent and selective inhibitors of HIV-1 LTR-directed gene expression, at concentrations that have minor effects on cells [2].
  • Our findings suggest that curcumin treatment is sufficient to relieve the toxic effect of mutant aggregation-induced apoptosis and may potentially have a therapeutic role in treating selected forms of inherited peripheral neuropathies [3].
  • Because of the central role of the transcription factor nuclear factor-kappaB (NF-kappaB) in cell survival and proliferation in human multiple myeloma (MM), we explored the possibility of using it as a target for MM treatment by using curcumin (diferuloylmethane), an agent known to have very little or no toxicity in humans [4].

Psychiatry related information on curcumin


High impact information on curcumin

  • Curcumin treatment in deltaF508-CFTR mice partially reversed the defect in ATP sensitivity [9].
  • Dietary curcumin and anti-TNF-alpha antibody counteracted the detrimental effect of TNBS on Phex gene expression [10].
  • Consistent with these findings, CD4(+) T-cell infiltration and NF-kappaB activation in colonic mucosa were suppressed in the curcumin-treated group [1].
  • METHODS: Mice with trinitrobenzene sulfonic acid (TNBS)-induced colitis were treated with 0.5%, 2.0%, or 5.0% curcumin in the diet, and changes in body weight together with histologic scores were evaluated [1].
  • In HeLa and MCF-7 cells, inhibition of CSN kinase by curcumin or Deltap53(145-164) results in accumulation of endogenous p53 [11].

Chemical compound and disease context of curcumin


Biological context of curcumin

  • Curcumin suppressed the constitutive IkappaBalpha phosphorylation through the inhibition of IKK activity [4].
  • The functional significance of a putative ARE in the GI-GPx promoter was validated by transcriptional activation of reporter gene constructs upon exposure to electrophiles (tBHQ, SFN, and curcumin) or overexpression of Nrf2 and by reversal of these effects by mutation of the ARE in the promoter and by overexpressed Keap1 [17].
  • The use of three inhibitors of ERalpha degradation that target different steps of the estrogen response pathway (inhibition of the CSN-associated kinase, nuclear export, and proteasome) suggests that a phosphorylation event inhibited by curcumin is necessary for ERalpha binding to its cognate DNA target [18].
  • As regards cell cycle arrest, the underlying mechanism in response to butyrate was most similar to that of the Caco-2 cell line that had spontaneously undergone a G0-G1 arrest and least similar to the G2-M arrest stimulated by curcumin [15].
  • Further investigations suggest that neutralization of tumor-induced oxidative stress and restoration of NF-kappaB activity along with the reeducation of the TNF-alpha signaling pathway can be the mechanism behind curcumin-mediated thymic protection [19].

Anatomical context of curcumin


Associations of curcumin with other chemical compounds


Gene context of curcumin


Analytical, diagnostic and therapeutic context of curcumin


  1. Curcumin prevents and ameliorates trinitrobenzene sulfonic acid-induced colitis in mice. Sugimoto, K., Hanai, H., Tozawa, K., Aoshi, T., Uchijima, M., Nagata, T., Koide, Y. Gastroenterology (2002) [Pubmed]
  2. Three inhibitors of type 1 human immunodeficiency virus long terminal repeat-directed gene expression and virus replication. Li, C.J., Zhang, L.J., Dezube, B.J., Crumpacker, C.S., Pardee, A.B. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  3. Curcumin treatment abrogates endoplasmic reticulum retention and aggregation-induced apoptosis associated with neuropathy-causing myelin protein zero-truncating mutants. Khajavi, M., Inoue, K., Wiszniewski, W., Ohyama, T., Snipes, G.J., Lupski, J.R. Am. J. Hum. Genet. (2005) [Pubmed]
  4. Curcumin (diferuloylmethane) down-regulates the constitutive activation of nuclear factor-kappa B and IkappaBalpha kinase in human multiple myeloma cells, leading to suppression of proliferation and induction of apoptosis. Bharti, A.C., Donato, N., Singh, S., Aggarwal, B.B. Blood (2003) [Pubmed]
  5. Phenolic anti-inflammatory antioxidant reversal of Abeta-induced cognitive deficits and neuropathology. Frautschy, S.A., Hu, W., Kim, P., Miller, S.A., Chu, T., Harris-White, M.E., Cole, G.M. Neurobiol. Aging (2001) [Pubmed]
  6. Neuroprotective mechanisms of curcumin against cerebral ischemia-induced neuronal apoptosis and behavioral deficits. Wang, Q., Sun, A.Y., Simonyi, A., Jensen, M.D., Shelat, P.B., Rottinghaus, G.E., MacDonald, R.S., Miller, D.K., Lubahn, D.E., Weisman, G.A., Sun, G.Y. J. Neurosci. Res. (2005) [Pubmed]
  7. Curcumin enhances the polyglutamine-expanded truncated N-terminal huntingtin-induced cell death by promoting proteasomal malfunction. Dikshit, P., Goswami, A., Mishra, A., Nukina, N., Jana, N.R. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  8. Risk reduction for DDT toxicity and carcinogenesis through dietary modification. Jaga, K., Duvvi, H. Journal of the Royal Society of Health. (2001) [Pubmed]
  9. CFTR is required for PKA-regulated ATP sensitivity of Kir1.1 potassium channels in mouse kidney. Lu, M., Leng, Q., Egan, M.E., Caplan, M.J., Boulpaep, E.L., Giebisch, G.H., Hebert, S.C. J. Clin. Invest. (2006) [Pubmed]
  10. The role of tumor necrosis factor alpha in down-regulation of osteoblast Phex gene expression in experimental murine colitis. Uno, J.K., Kolek, O.I., Hines, E.R., Xu, H., Timmermann, B.N., Kiela, P.R., Ghishan, F.K. Gastroenterology (2006) [Pubmed]
  11. COP9 signalosome-specific phosphorylation targets p53 to degradation by the ubiquitin system. Bech-Otschir, D., Kraft, R., Huang, X., Henklein, P., Kapelari, B., Pollmann, C., Dubiel, W. EMBO J. (2001) [Pubmed]
  12. Combined inhibitory effects of curcumin and phenethyl isothiocyanate on the growth of human PC-3 prostate xenografts in immunodeficient mice. Khor, T.O., Keum, Y.S., Lin, W., Kim, J.H., Hu, R., Shen, G., Xu, C., Gopalakrishnan, A., Reddy, B., Zheng, X., Conney, A.H., Kong, A.N. Cancer Res. (2006) [Pubmed]
  13. Inhibitory effects of curcumin on in vitro lipoxygenase and cyclooxygenase activities in mouse epidermis. Huang, M.T., Lysz, T., Ferraro, T., Abidi, T.F., Laskin, J.D., Conney, A.H. Cancer Res. (1991) [Pubmed]
  14. Dietary curcumin inhibits chemotherapy-induced apoptosis in models of human breast cancer. Somasundaram, S., Edmund, N.A., Moore, D.T., Small, G.W., Shi, Y.Y., Orlowski, R.Z. Cancer Res. (2002) [Pubmed]
  15. Genetic reprogramming in pathways of colonic cell maturation induced by short chain fatty acids: comparison with trichostatin A, sulindac, and curcumin and implications for chemoprevention of colon cancer. Mariadason, J.M., Corner, G.A., Augenlicht, L.H. Cancer Res. (2000) [Pubmed]
  16. Enzyme induction and dietary chemicals as approaches to cancer chemoprevention: the Seventh DeWitt S. Goodman Lecture. Conney, A.H. Cancer Res. (2003) [Pubmed]
  17. The GI-GPx gene is a target for Nrf2. Banning, A., Deubel, S., Kluth, D., Zhou, Z., Brigelius-Flohé, R. Mol. Cell. Biol. (2005) [Pubmed]
  18. CSN5/Jab1 is involved in ligand-dependent degradation of estrogen receptor {alpha} by the proteasome. Calligé, M., Kieffer, I., Richard-Foy, H. Mol. Cell. Biol. (2005) [Pubmed]
  19. Tumor-Induced Oxidative Stress Perturbs Nuclear Factor-{kappa}B Activity-Augmenting Tumor Necrosis Factor-{alpha}-Mediated T-Cell Death: Protection by Curcumin. Bhattacharyya, S., Mandal, D., Sen, G.S., Pal, S., Banerjee, S., Lahiry, L., Finke, J.H., Tannenbaum, C.S., Das, T., Sa, G. Cancer Res. (2007) [Pubmed]
  20. Suppression of c-Jun/AP-1 activation by an inhibitor of tumor promotion in mouse fibroblast cells. Huang, T.S., Lee, S.C., Lin, J.K. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  21. Inhibition of NAD(P)H:quinone oxidoreductase 1 activity and induction of p53 degradation by the natural phenolic compound curcumin. Tsvetkov, P., Asher, G., Reiss, V., Shaul, Y., Sachs, L., Lotem, J. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  22. Nuclear factor-kappaB and STAT3 are constitutively active in CD138+ cells derived from multiple myeloma patients, and suppression of these transcription factors leads to apoptosis. Bharti, A.C., Shishodia, S., Reuben, J.M., Weber, D., Alexanian, R., Raj-Vadhan, S., Estrov, Z., Talpaz, M., Aggarwal, B.B. Blood (2004) [Pubmed]
  23. The constitutive photomorphogenesis 9 signalosome directs vascular endothelial growth factor production in tumor cells. Pollmann, C., Huang, X., Mall, J., Bech-Otschir, D., Naumann, M., Dubiel, W. Cancer Res. (2001) [Pubmed]
  24. Curcumin activates the aryl hydrocarbon receptor yet significantly inhibits (-)-benzo(a)pyrene-7R-trans-7,8-dihydrodiol bioactivation in oral squamous cell carcinoma cells and oral mucosa. Rinaldi, A.L., Morse, M.A., Fields, H.W., Rothas, D.A., Pei, P., Rodrigo, K.A., Renner, R.J., Mallery, S.R. Cancer Res. (2002) [Pubmed]
  25. Interleukin-1 beta-mediated suppression of RXR:RAR transactivation of the Ntcp promoter is JNK-dependent. Li, D., Zimmerman, T.L., Thevananther, S., Lee, H.Y., Kurie, J.M., Karpen, S.J. J. Biol. Chem. (2002) [Pubmed]
  26. Chemoprevention of colon carcinogenesis by dietary curcumin, a naturally occurring plant phenolic compound. Rao, C.V., Rivenson, A., Simi, B., Reddy, B.S. Cancer Res. (1995) [Pubmed]
  27. Inhibitory effects of dietary curcumin on forestomach, duodenal, and colon carcinogenesis in mice. Huang, M.T., Lou, Y.R., Ma, W., Newmark, H.L., Reuhl, K.R., Conney, A.H. Cancer Res. (1994) [Pubmed]
  28. Sensitization of taxol-induced apoptosis by curcumin involves down-regulation of nuclear factor-kappaB and the serine/threonine kinase Akt and is independent of tubulin polymerization. Bava, S.V., Puliappadamba, V.T., Deepti, A., Nair, A., Karunagaran, D., Anto, R.J. J. Biol. Chem. (2005) [Pubmed]
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