Corrigendum to “Curcumin protects rat liver from streptozotocin-induced diabetic pathophysiology by counteracting reactive oxygen species and inhibiting the activation of p53 and MAPKs mediated stress response pathways” [Toxicol. Rep. 2 (2015) 365–376, (S2214750014001711), (10.1016/j.toxrep.2014.12.017)];Curcumin protects rat liver from streptozotocin-induced diabetic pathophysiology by counteracting reactive oxygen species and inhibiting the activation of p53 and MAPKs mediated stress response pathways

Toxicology Reports

Volumn 2, Issue , 2015, Pages 365-376

  Ghosh, Shatadal ^a   Bhattacharyya, Sudip ^a   Rashid, Kahkashan ^a   Sil, Parames C ^a  

^a BOSE INSTITUTE   (India)

Author keywords

Antioxidant; Apoptosis; Curcumin; Diabetes; Liver; Reactive oxygen species; Streptozotocin

Indexed keywords

CASPASE 3; CURCUMIN; GLUTATHIONE; GLUTATHIONE DISULFIDE; JNK MITOGEN ACTIVATED PROTEIN KINASE USE: STRESS ACTIVATED PROTEIN KINASE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; NITRIC OXIDE; PROTEIN BCL 2; PROTEIN BCL XL; PROTEIN P53; REACTIVE OXYGEN METABOLITE; STREPTOZOCIN; UNCLASSIFIED DRUG;

ADULT; ALANINE AMINOTRANSFERASE BLOOD LEVEL; ALKALINE PHOSPHATASE BLOOD LEVEL; ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ANTIOXIDANT ACTIVITY; APOPTOSIS; ARTICLE; ASPARTATE AMINOTRANSFERASE BLOOD LEVEL; CELLULAR STRESS RESPONSE; CONTROLLED STUDY; DNA FRAGMENTATION; EXPERIMENTAL LIVER INJURY; FLOW CYTOMETRY; HYPERGLYCEMIA; IMMUNOBLOTTING; LACTATE DEHYDROGENASE BLOOD LEVEL; LIPID PEROXIDATION; LIVER DYSFUNCTION; MALE; MITOCHONDRIAL MEMBRANE POTENTIAL; NONHUMAN; OXIDATIVE STRESS; PATHOPHYSIOLOGY; PHASE 1 CLINICAL TRIAL (TOPIC); RAT; STREPTOZOTOCIN-INDUCED DIABETES MELLITUS; WEIGHT GAIN;

EID: 84925462872     PISSN: 22147500     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.toxrep.2023.11.006     Document Type: Erratum

References (77)

1. Ghosh J., Das J., Manna P., Sil P.C. The protective role of arjunolic acid against doxorubicin induced intracellular ROS dependent JNK-p38 and p53-mediated cardiac apoptosis. Biomaterials 2011, 32(21):4857-4866.
2. Das J., Roy A., Sil P.C. Mechanism of the protective action of taurine in toxin and drug induced organ pathophysiology and diabetic complications: a review. Food Funct 2012, 2(12):1251-1264.
3. Maritim A.C., Sanders R.A., Watkins J.B. Diabetes, oxidative stress, and antioxidants: a review. J. Biochem. Mol. Toxicol. 2003, 17(1):24-38.
4. Giacco F., Brownlee M. Oxidative stress and diabetic complications. Circulation research 2010, 107(9):1058-1070.
5. Das J., Sil P.C. Taurine ameliorates alloxan-induced diabetic renal injury, oxidative stress-related signaling pathways and apoptosis in rats. Amino Acids 2012, 43(4):1509-1523.
6. Lin J., Zheng S., Chen A. Curcumin attenuates the effects of insulin on stimulating hepatic stellate cell activation by interrupting insulin signaling and attenuating oxidative stress. Lab. Invest. 2009, 89(12):1397-1409.
7. Schraufstatter E., Bernt H. Antibacterial action of curcumin and related compounds. Nature 1949, 164(4167):456.
8. Sharma O.P. Antioxidant activity of curcumin and related compounds. Biochem. Pharmacol. 1976, 25(15):1811-1812.
9. Sharma S., Kulkarni S.K., Chopra K. Curcumin, the active principle of turmeric (Curcuma longa), ameliorates diabetic nephropathy in rats. Clin. Exp. Pharmacol. Physiol. 2006, 33(10):940-945.
10. Nishiyama T., Mae T., Kishida H., Tsukagawa M., Mimaki Y., Kuroda M., Sashida Y., Takahashi K., Kawada T., Nakagawa K., Kitahara M. Curcuminoids and sesquiterpenoids in turmeric (Curcuma longa L.) suppress an increase in blood glucose level in type 2 diabetic KK-Ay mice. J. Agric. Food Chem. 2005, 53(4):959-963.
11. Aggarwal B.B., Sung B. Pharmacological basis for the role of curcumin in chronic diseases: an age-old spice with modern targets. Trends Pharmacol. Sci. 2009, 30(2):85-94.
12. Gupta S.C., Prasad S., Kim J.H., Patchva S., Webb L.J., Priyadarsini I.K., Aggarwal B.B. Multitargeting by curcumin as revealed by molecular interaction studies. Nat. Prod. Rep. 2011, 28(12):1937-1955.
13. Dhillon N., Aggarwal B.B., Newman R.A., Wolff R.A., Kunnumakkara A.B., Abbruzzese J.L., Ng C.S., Badmaev V., Kurzrock R. Phase II trial of curcumin in patients with advanced pancreatic cancer. Clin. Cancer Res. 2008, 14(14):4491-4499.
14. Kim S.G., Veena M.S., Basak S.K., Han E., Tajima T., Gjertson D.W., Starr J., Eidelman O., Pollard H.B., Srivastava M., Srivatsan E.S., Wang M.B. Curcumin treatment suppresses IKKbeta kinase activity of salivary cells of patients with head and neck cancer: a pilot study. Clin. Cancer Res. 2011, 17(18):5953-5961.
15. Holt P.R., Katz S., Kirshoff R. Curcumin therapy in inflammatory bowel disease: a pilot study. Dig. Dis. Sci. 2005, 50(11):2191-2193.
16. Sharma R.A., Ireson C.R., Verschoyle R.D., Hill K.A., Williams M.L., Leuratti C., Manson M.M., Marnett L.J., Steward W.P., Gescher A. Effects of dietary curcumin on glutathione S-transferase and malondialdehyde-DNA adducts in rat liver and colon mucosa: relationship with drug levels. Clin. Cancer Res. 2001, 7(5):1452-1458.
17. Sharma R.A., McLelland H.R., Hill K.A., Ireson C.R., Euden S.A., Manson M.M., Pirmohamed M., Marnett L.J., Gescher A.J., Steward W.P. Pharmacodynamic and pharmacokinetic study of oral Curcuma extract in patients with colorectal cancer. Clin. Cancer Res. 2001, 7(7):1894-1900.
18. He Z.Y., Shi C.B., Wen H., Li F.L., Wang B.L., Wang J. Upregulation of p53 expression in patients with colorectal cancer by administration of curcumin. Cancer Invest. 2011, 29(3):208-213.
19. Kalpravidh R.W., Siritanaratkul N., Insain P., Charoensakdi R., Panichkul N., Hatairaktham S., Srichairatanakool S., Phisalaphong C., Rachmilewitz E., Fucharoen S. Improvement in oxidative stress and antioxidant parameters in beta-thalassemia/Hb E patients treated with curcuminoids. Clin. Biochem. 2010, 43(4-5):424-429.
20. Heng M.C., Song M.K., Harker J., Heng M.K. Drug-induced suppression of phosphorylase kinase activity correlates with resolution of psoriasis as assessed by clinical, histological and immunohistochemical parameters. Br. J. Dermatol. 2000, 143(5):937-949.
21. Shoskes D., Lapierre C., Cruz-Correa M., Muruve N., Rosario R., Fromkin B., Braun M., Copley J. Beneficial effects of the bioflavonoids curcumin and quercetin on early function in cadaveric renal transplantation: a randomized placebo controlled trial. Transplantation 2005, 80(11):1556-1559.
22. Gupta S.C., Patchva S., Aggarwal B.B. Therapeutic roles of curcumin: lessons learned from clinical trials. AAPS J. 2013, 15(1):195-218.
23. Palma H.E., Wolkmer P., Gallio M., Correa M.M., Schmatz R., Thome G.R., Pereira L.B., Castro V.S., Pereira A.B., Bueno A., de Oliveira L.S., Rosolen D., Mann T.R., de Cecco B.S., Graca D.L., Lopes S.T., Mazzanti C.M. Oxidative stress parameters in blood, liver, and kidney of diabetic rats treated with curcumin and/or insulin. Mol. Cell. Biochem. 2014, 386(1-2):199-210.
24. Sun C., Zhang Y., Kong T., Li Y., Feng R., Wang G. Effects of curcumin intake on kidney and liver pathological changes in T2DM rats. Wei Sheng Yan Jiu 2013, 42(1):6-9.
25. Abdel Aziz M.T., El-Asmar M.F., El-Ibrashy I.N., Rezq A.M., Al-Malki A.L., Wassef M.A., Fouad H.H., Ahmed H.H., Taha F.M., Hassouna A.A., Morsi H.M. Effect of novel water soluble curcumin derivative on experimental type-1 diabetes mellitus (short term study). Diabetol. Metab. Syndr. 2012, 4(1):30.
26. Pari L., Karthikesan K., Menon V.P. Comparative and combined effect of chlorogenic acid and tetrahydrocurcumin on antioxidant disparities in chemical induced experimental diabetes. Mol. Cell. Biochem. 2010, 341(1-2):109-117.
27. Ganda O.P., Rossini A.A., Like A.A. Studies on streptozotocin diabetes. Diabetes 1976, 25(7):595-603.
28. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
29. Kornberg A. Lactic dehydrogenase of muscle. Methods in Enzymology 1955, 441-443. Academic press, New York. S.P. Colowick, N.O. Kaplan (Eds.).
30. 15N]nitrate in biological fluids. Anal. Biochem. 1982, 126(1):131-138.
31. Suresh Y., Das U.N. Differential effect of saturated, monounsaturated, and polyunsaturated fatty acids on alloxan-induced diabetes mellitus. Prostaglandins Leukot. Essent. Fatty Acids 2006, 74(3):199-213.
32. Esterbauer H., Cheeseman K.H. Determination of aldehydic lipid peroxidation products: malonaldehyde and 4-hydroxynonenal. Methods Enzymol. 1990, 186:407-421.
33. Ellman G.L. Tissue sulfhydryl groups. Arch. Biochem. Biophys. 1959, 82(1):70-77.
34. Hissin P.J., Hilf R. A fluorometric method for determination of oxidized and reduced glutathione in tissues. Anal. Biochem. 1976, 74(1):214-226.
35. Benzie I.F., Strain J.J. Ferric reducing/antioxidant power assay: direct measure of total antioxidant activity of biological fluids and modified version for simultaneous measurement of total antioxidant power and ascorbic acid concentration. Methods Enzymol. 1999, 299:15-27.
36. Manna P., Sinha M., Sil P.C. Protection of arsenic-induced testicular oxidative stress by arjunolic acid. Redox Rep. 2008, 13(2):67-77.
37. Bonaventura J., Schroeder W.A., Fang S. Human erythrocyte catalase: an improved method of isolation and a reevaluation of reported properties. Arch. Biochem. Biophys. 1972, 150(2):606-617.
38. Habig W.H., Pabst M.J., Jakoby W.B. Glutathione S-transferases. The first enzymatic step in mercapturic acid formation. J. Biol. Chem. 1974, 249(22):7130-7139.
39. Smith I.K., Vierheller T.L., Thorne C.A. Assay of glutathione reductase in crude tissue homogenates using 5,5'-dithiobis(2-nitrobenzoic acid). Anal. Biochem. 1988, 175(2):408-413.
40. Flohe L., Gunzler W.A. Assays of glutathione peroxidase. Methods Enzymol. 1984, 105:114-121.
41. Hodarnau A., Dancea S., Barzu O. Isolation of highly purified mitochondria from rat pancreas. J. Cell Biol. 1973, 59(1):222-227.
42. Pari L., Murugan P. Antihyperlipidemic effect of curcumin and tetrahydrocurcumin in experimental type 2 diabetic rats. Ren Fail 2007, 29(7):881-889.
43. Bonner-Weir S., Trent D.F., Honey R.N., Weir G.C. Responses of neonatal rat islets to streptozotocin: limited B-cell regeneration and hyperglycemia. Diabetes 1981, 30(1):64-69.
44. Fernandez-Alvarez J., Barbera A., Nadal B., Barcelo-Batllori S., Piquer S., Claret M., Guinovart J.J., Gomis R. Stable and functional regeneration of pancreatic beta-cell population in nSTZ-rats treated with tungstate. Diabetologia 2004, 47(3):470-477.
45. Srinivasan K., Ramarao P. Animal models in type 2 diabetes research: an overview. Indian J Med Res. 2007, 125(3):451-472.
46. Srinivasan K., Viswanad B., Asrat L., Kaul C.L., Ramarao P. Combination of high-fat diet-fed and low-dose streptozotocin-treated rat: a model for type 2 diabetes and pharmacological screening. Pharmacol Res. 2005, 52(4):313-320.
47. Szkudelski T. The mechanism of alloxan and streptozotocin action in B cells of the rat pancreas. Physiol. Res. 2001, 50(6):537-546.
48. Clinical development plan: curcumin. J. Cell. Biochem. Suppl. 1996, 26:72-85.
49. Perkins S., Verschoyle R.D., Hill K., Parveen I., Threadgill M.D., Sharma R.A., Williams M.L., Steward W.P., Gescher A.J. Chemopreventive efficacy and pharmacokinetics of curcumin in the min/+ mouse, a model of familial adenomatous polyposis. Cancer Epidemiol. Biomark. Prev. 2002, 11(6):535-540.
50. Anand P., et al. Bioavailability of curcumin: problems and promises. Mol. Pharm. 2007, 4(6):807-818.
51. Shoba G., et al. Influence of piperine on the pharmacokinetics of curcumin in animals and human volunteers. Planta Med. 1998, 64(4):353-356.
52. Chainani-Wu N. Safety and anti-inflammatory activity of curcumin: a component of tumeric (Curcuma longa). J. Altern. Complement. Med. 2003, 9(1):161-168.
53. Cheng A.L., et al. Phase I clinical trial of curcumin, a chemopreventive agent, in patients with high-risk or pre-malignant lesions. Anticancer Res. 2001, 21(4B):2895-2900.
54. Bisht S., et al. Polymeric nanoparticle-encapsulated curcumin (nanocurcumin): a novel strategy for human cancer therapy. J. Nanobiotechnol. 2007, 5:3.
55. Maiti K., et al. Curcumin-phospholipid complex: preparation, therapeutic evaluation and pharmacokinetic study in rats. Int. J. Pharm. 2007, 330(1-2):155-163.
56. Tiyaboonchai W., Tungpradit W., Plianbangchang P. Formulation and characterization of curcuminoids loaded solid lipid nanoparticles. Int. J. Pharm. 2007, 337(1-2):299-306.
57. Kroncke K.D., Fehsel K., Sommer A., Rodriguez M.L., Kolb-Bachofen V. Nitric oxide generation during cellular metabolization of the diabetogenic N-methyl-N-nitroso-urea streptozotozin contributes to islet cell DNA damage. Biol. Chem. Hoppe-Seyler 1995, 376(3):179-185.
58. Morgan N.G., Cable H.C., Newcombe N.R., Williams G.T. Treatment of cultured pancreatic B-cells with streptozotocin induces cell death by apoptosis. Biosci. Rep. 1994, 14(5):243-250.
59. Turk J., Corbett J.A., Ramanadham S., Bohrer A., McDaniel M.L. Biochemical evidence for nitric oxide formation from streptozotocin in isolated pancreatic islets. Biochem. Biophys. Res. Commun. 1993, 197(3):1458-1464.
60. Marnett L.J. Lipid peroxidation-DNA damage by malondialdehyde. Mutat. Res. 1999, 424(1-2):83-95.
61. Meister A., Anderson M.E. Glutathione. Annu. Rev. Biochem. 1983, 52:711-760.
62. Meister A. Glutathione metabolism and its selective modification. J. Biol. Chem. 1988, 263(33):17205-17208.
63. Nithipongvanitch R., Ittarat W., Velez J.M., Zhao R., St Clair D.K., Oberley T.D. Evidence for p53 as guardian of the cardiomyocyte mitochondrial genome following acute adriamycin treatment. J. Histochem. Cytochem. 2007, 55(6):629-639.
64. Nakamura H., Matoba S., Iwai-Kanai E., Kimata M., Hoshino A., Nakaoka M., Katamura M., Okawa Y., Ariyoshi M., Mita Y., Ikeda K., Okigaki M., Adachi S., Tanaka H., Takamatsu T., Matsubara H. p53 promotes cardiac dysfunction in diabetic mellitus caused by excessive mitochondrial respiration-mediated reactive oxygen species generation and lipid accumulation. Circ. Heart Fail. 2012, 5(1):106-115.
65. Jazayeri L., Callaghan M.J., Grogan R.H., Hamou C.D., Thanik V., Ingraham C.R., Capell B.C., Pelo C.R., Gurtner G.C. Diabetes increases p53-mediated apoptosis following ischemia. Plast. Reconstr. Surg. 2008, 121(4):1135-1143.
66. Hoshino A., Ariyoshi M., Okawa Y., Kaimoto S., Uchihashi M., Fukai K., Iwai-Kanai E., Ikeda K., Ueyama T., Ogata T., Matoba S. Inhibition of p53 preserves Parkin-mediated mitophagy and pancreatic beta-cell function in diabetes. Proc. Natl. Acad. Sci. U. S. A. 2014, 111(8):3116-3121.
67. Deshpande S.D., Putta S., Wang M., Lai J.Y., Bitzer M., Nelson R.G., Lanting L.L., Kato M., Natarajan R. Transforming growth factor-beta-induced cross talk between p53 and a microRNA in the pathogenesis of diabetic nephropathy. Diabetes 2013, 62(9):3151-3162.
68. Singh S., Raina V., Chavali P.L., Dubash T., Kadreppa S., Parab P., Chattopadhyay S. Regulation of GAD65 expression by SMAR1 and p53 upon Streptozotocin treatment. BMC Mol. Biol. 2012, 13:28.
69. Manna P., Das J., Ghosh J., Sil P.C. Contribution of type 1 diabetes to rat liver dysfunction and cellular damage via activation of NOS, PARP, IkappaBalpha/NF-kappaB, MAPKs, and mitochondria-dependent pathways: prophylactic role of arjunolic acid. Free Radic. Biol. Med. 2010, 48(11):1465-1484.
70. Roux P.P., Blenis J. ERK and p38 MAPK-activated protein kinases: a family of protein kinases with diverse biological functions. Microbiol. Mol. Biol. Rev. 2004, 68(2):320-344.
71. Khatun S., Chaube S.K., Bhattacharyya C.N. p53 activation and mitochondria-mediated pathway are involved during hanging death-induced neuronal cell apoptosis in dentate gyrus region of the rat brain. Springerplus 2013, 2:407.
72. Das J., Ghosh J., Manna P., Sil P.C. Taurine protects rat testes against doxorubicin-induced oxidative stress as well as p53, Fas and caspase 12-mediated apoptosis. Amino Acids 2012, 42(5):1839-1855.
73. Lai H.C., Liu T.J., Ting C.T., Sharma P.M., Wang P.H. Insulin-like growth factor-1 prevents loss of electrochemical gradient in cardiac muscle mitochondria via activation of PI 3 kinase/Akt pathway. Mol. Cell. Endocrinol. 2003, 205(1-2):99-106.
74. Li P., Nijhawan D., Wang X. Mitochondrial activation of apoptosis. Cell 2004, 116(2 Suppl.):S57-S59. 52 pp. following S59.
75. Li P., Nijhawan D., Budihardjo I., Srinivasula S.M., Ahmad M., Alnemri E.S., Wang X. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 1997, 91(4):479-489.
76. Salvesen G.S. Caspases: opening the boxes and interpreting the arrows. Cell Death Differ. 2002, 9(1):3-5.
77. Walters J., Pop C., Scott F.L., Drag M., Swartz P., Mattos C., Salvesen G.S., Clark A.C. A constitutively active and uninhibitable caspase-3 zymogen efficiently induces apoptosis. Biochem. J. 2009, 424(3):335-345.