메뉴 건너뛰기




Volumn 1860, Issue 11, 2016, Pages 2377-2390

Andrographolide protects liver cells from H2O2 induced cell death by upregulation of Nrf-2/HO-1 mediated via adenosine A2a receptor signalling

Author keywords

GSK 3 ; HepG2 cells; MAP kinase; Nrf 2; Oxidative stress; Protein kinase A

Indexed keywords

ADENOSINE A2A RECEPTOR; ADENYLATE CYCLASE; ANDROGRAPHIS PANICULATA EXTRACT; ANDROGRAPHOLIDE; ANTIOXIDANT; CAFFEINE; CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE; G PROTEIN COUPLED RECEPTOR; GLYCOGEN SYNTHASE KINASE 3BETA; HEME OXYGENASE 1; HYDROGEN PEROXIDE; MITOGEN ACTIVATED PROTEIN KINASE P38; REACTIVE OXYGEN METABOLITE; TRANSCRIPTION FACTOR NRF2; DITERPENE; NFE2L2 PROTEIN, HUMAN;

EID: 84984652750     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2016.07.005     Document Type: Article
Times cited : (62)

References (64)
  • 1
    • 33947607132 scopus 로고    scopus 로고
    • Protective activity of andrographolide and arabinogalactan proteins from Andrographis paniculata Nees. against ethanol-induced toxicity in mice
    • [1] Singha, P.K., Roy, S., Dey, S., Protective activity of andrographolide and arabinogalactan proteins from Andrographis paniculata Nees. against ethanol-induced toxicity in mice. J. Ethnopharmacol. 111 (2007), 13–21.
    • (2007) J. Ethnopharmacol. , vol.111 , pp. 13-21
    • Singha, P.K.1    Roy, S.2    Dey, S.3
  • 2
    • 4644241127 scopus 로고    scopus 로고
    • Andrographolide attenuates inflammation by inhibition of NF-B activation through covalent modification of reduced cysteine 62 of p50
    • [2] Xia, Y.F., Ye, B.Q., Li, Y.D., Wang, J.G., He, X.J., Lin, X., Yao, X., Ma, D., Slungaard, A., Hebbel, R.P., Key, N.S., Geng, J.G., Andrographolide attenuates inflammation by inhibition of NF-B activation through covalent modification of reduced cysteine 62 of p50. J. Immunol. 173 (2004), 4207–4217.
    • (2004) J. Immunol. , vol.173 , pp. 4207-4217
    • Xia, Y.F.1    Ye, B.Q.2    Li, Y.D.3    Wang, J.G.4    He, X.J.5    Lin, X.6    Yao, X.7    Ma, D.8    Slungaard, A.9    Hebbel, R.P.10    Key, N.S.11    Geng, J.G.12
  • 3
    • 0141457852 scopus 로고    scopus 로고
    • Andrographolide, a potential cancer therapeutic agent isolated from Andrographis paniculata
    • [3] Rajagopal, S., Kumar, R.A., Deevi, D.S., Satyanarayana, C., Rajagopalan, R., Andrographolide, a potential cancer therapeutic agent isolated from Andrographis paniculata. J. Exp. Ther. Oncol. 3 (2003), 147–158.
    • (2003) J. Exp. Ther. Oncol. , vol.3 , pp. 147-158
    • Rajagopal, S.1    Kumar, R.A.2    Deevi, D.S.3    Satyanarayana, C.4    Rajagopalan, R.5
  • 4
    • 84907867462 scopus 로고    scopus 로고
    • Engineered andrographolide nanosystems for smart recovery in hepatotoxic conditions
    • [4] Mukherjee, A., Roy, P., Ghosh Auddy, R., Das, S., Engineered andrographolide nanosystems for smart recovery in hepatotoxic conditions. Int. J. Nanomedicine, 4723, 2014.
    • (2014) Int. J. Nanomedicine , vol.4723
    • Mukherjee, A.1    Roy, P.2    Ghosh Auddy, R.3    Das, S.4
  • 5
    • 84875139247 scopus 로고    scopus 로고
    • Andrographolide protects against cigarette smoke-induced oxidative lung injury via augmentation of Nrf-2 activity: andrographolide attenuates oxidative lung injury
    • [5] Guan, S., Tee, W., Ng, D., Chan, T., Peh, H., Ho, W., Cheng, C., Mak, J., Wong, W., Andrographolide protects against cigarette smoke-induced oxidative lung injury via augmentation of Nrf-2 activity: andrographolide attenuates oxidative lung injury. Br. J. Pharmacol. 168 (2013), 1707–1718.
    • (2013) Br. J. Pharmacol. , vol.168 , pp. 1707-1718
    • Guan, S.1    Tee, W.2    Ng, D.3    Chan, T.4    Peh, H.5    Ho, W.6    Cheng, C.7    Mak, J.8    Wong, W.9
  • 6
    • 84908123327 scopus 로고    scopus 로고
    • Andrographolide prevents high-fat diet-induced obesity in C57BL/6 mice by suppressing the sterol regulatory element-binding protein pathway
    • [6] Ding, L., Li, J., Song, B., Xiao, X., Huang, W., Zhang, B., Tang, X., Qi, M., Yang, Q., Yang, Q., Yang, L., Wang, Z., Andrographolide prevents high-fat diet-induced obesity in C57BL/6 mice by suppressing the sterol regulatory element-binding protein pathway. J. Pharmacol. Exp. Ther. 351 (2014), 474–483.
    • (2014) J. Pharmacol. Exp. Ther. , vol.351 , pp. 474-483
    • Ding, L.1    Li, J.2    Song, B.3    Xiao, X.4    Huang, W.5    Zhang, B.6    Tang, X.7    Qi, M.8    Yang, Q.9    Yang, Q.10    Yang, L.11    Wang, Z.12
  • 7
    • 84876296042 scopus 로고    scopus 로고
    • Hypolipidemic effects of andrographolide and neoandrographolide in mice and rats: hypolipidemic effects of andrographolide and neoandrographolide
    • [7] Yang, T., Shi, H.-x., Wang, Z.-t., Wang, C.-h., Hypolipidemic effects of andrographolide and neoandrographolide in mice and rats: hypolipidemic effects of andrographolide and neoandrographolide. Phytother. Res. 27 (2013), 618–623.
    • (2013) Phytother. Res. , vol.27 , pp. 618-623
    • Yang, T.1    Shi, H.-X.2    Wang, Z.-T.3    Wang, C.-H.4
  • 8
    • 0034648298 scopus 로고    scopus 로고
    • The Haber-Weiss reaction and mechanisms of toxicity
    • [8] Kehrer, J.P., The Haber-Weiss reaction and mechanisms of toxicity. Toxicology 149 (2000), 43–50.
    • (2000) Toxicology , vol.149 , pp. 43-50
    • Kehrer, J.P.1
  • 9
    • 1542723493 scopus 로고    scopus 로고
    • Decline in transcriptional activity of Nrf-2 causes age-related loss of glutathione synthesis, which is reversible with lipoic acid
    • [9] Suh, J.H., Shenvi, S.V., Dixon, B.M., Liu, H., Jaiswal, A.K., Liu, R.M., Hagen, T.M., Decline in transcriptional activity of Nrf-2 causes age-related loss of glutathione synthesis, which is reversible with lipoic acid. Proc. Natl. Acad. Sci. 101 (2004), 3381–3386.
    • (2004) Proc. Natl. Acad. Sci. , vol.101 , pp. 3381-3386
    • Suh, J.H.1    Shenvi, S.V.2    Dixon, B.M.3    Liu, H.4    Jaiswal, A.K.5    Liu, R.M.6    Hagen, T.M.7
  • 10
    • 13944278132 scopus 로고    scopus 로고
    • Mitochondria, oxidants, and aging
    • [10] Balaban, R.S., Nemoto, S., Finkel, T., Mitochondria, oxidants, and aging. Cell 120 (2005), 483–495.
    • (2005) Cell , vol.120 , pp. 483-495
    • Balaban, R.S.1    Nemoto, S.2    Finkel, T.3
  • 12
    • 28744438385 scopus 로고    scopus 로고
    • Introduction to serial review on the role of oxidative stress in diabetes mellitus
    • [12] Dennery, P.A., Introduction to serial review on the role of oxidative stress in diabetes mellitus. Free Radic. Biol. Med. 40 (2006), 1–2.
    • (2006) Free Radic. Biol. Med. , vol.40 , pp. 1-2
    • Dennery, P.A.1
  • 13
    • 77950023207 scopus 로고    scopus 로고
    • Oxidative stress and oxidative damage in carcinogenesis
    • [13] Klaunig, J.E., Kamendulis, L.M., Hocevar, B.A., Oxidative stress and oxidative damage in carcinogenesis. Toxicol. Pathol. 38 (2010), 96–109.
    • (2010) Toxicol. Pathol. , vol.38 , pp. 96-109
    • Klaunig, J.E.1    Kamendulis, L.M.2    Hocevar, B.A.3
  • 14
  • 15
    • 1942520367 scopus 로고    scopus 로고
    • Nrf-2 signaling in coordinated activation of antioxidant gene expression
    • [15] Jaiswal, A.K., Nrf-2 signaling in coordinated activation of antioxidant gene expression. Free Radic. Biol. Med. 36 (2004), 1199–1207.
    • (2004) Free Radic. Biol. Med. , vol.36 , pp. 1199-1207
    • Jaiswal, A.K.1
  • 16
    • 33947680664 scopus 로고    scopus 로고
    • Natural dietary anti-cancer chemopreventive compounds: redox-mediated differential signaling mechanisms in cytoprotection of normal cells versus cytotoxicity in tumor cells
    • [16] Nair, S., Li, W., Kong, A.-N.T., Natural dietary anti-cancer chemopreventive compounds: redox-mediated differential signaling mechanisms in cytoprotection of normal cells versus cytotoxicity in tumor cells. Acta Pharmacol. Sin. 28 (2007), 459–472.
    • (2007) Acta Pharmacol. Sin. , vol.28 , pp. 459-472
    • Nair, S.1    Li, W.2    Kong, A.-N.T.3
  • 17
    • 77957587417 scopus 로고    scopus 로고
    • Phytochemicals: cancer chemoprevention and suppression of tumor onset and metastasis
    • [17] Shu, L., Cheung, K.-L., Khor, T.O., Chen, C., Kong, A.-N., Phytochemicals: cancer chemoprevention and suppression of tumor onset and metastasis. Cancer Metastasis Rev. 29 (2010), 483–502.
    • (2010) Cancer Metastasis Rev. , vol.29 , pp. 483-502
    • Shu, L.1    Cheung, K.-L.2    Khor, T.O.3    Chen, C.4    Kong, A.-N.5
  • 18
  • 19
    • 0032827002 scopus 로고    scopus 로고
    • Regulatory mechanisms of cellular response to oxidative stress
    • [19] Itoh, K., Ishii, T., Wakabayashi, N., Yamamoto, M., Regulatory mechanisms of cellular response to oxidative stress. Free Radic. Res. 31 (1999), 319–324.
    • (1999) Free Radic. Res. , vol.31 , pp. 319-324
    • Itoh, K.1    Ishii, T.2    Wakabayashi, N.3    Yamamoto, M.4
  • 20
    • 0036783335 scopus 로고    scopus 로고
    • Pharmacogenomics, regulation and signaling pathways of phase I and II drug metabolizing enzymes
    • [20] Rushmore, T.H., Kong, A.-N.T., Pharmacogenomics, regulation and signaling pathways of phase I and II drug metabolizing enzymes. Curr. Drug Metab. 3 (2002), 481–490.
    • (2002) Curr. Drug Metab. , vol.3 , pp. 481-490
    • Rushmore, T.H.1    Kong, A.-N.T.2
  • 21
    • 0016275767 scopus 로고
    • Sequence of the reaction of heme catabolism catalyzed by the microsomal heme oxygenase system
    • [21] Yoshida, T., Kikuchi, G., Sequence of the reaction of heme catabolism catalyzed by the microsomal heme oxygenase system. FEBS Lett. 48 (1974), 256–261.
    • (1974) FEBS Lett. , vol.48 , pp. 256-261
    • Yoshida, T.1    Kikuchi, G.2
  • 22
    • 0019335801 scopus 로고
    • Inability of the NADH-cytochrome b5 reductase system to initiate heme degradation yielding biliverdin IX alpha from the oxygenated form of heme. heme oxygenase complex
    • [22] Yoshida, T., Noguchi, M., Kikuchi, G., Inability of the NADH-cytochrome b5 reductase system to initiate heme degradation yielding biliverdin IX alpha from the oxygenated form of heme. heme oxygenase complex. FEBS Lett. 115 (1980), 278–280.
    • (1980) FEBS Lett. , vol.115 , pp. 278-280
    • Yoshida, T.1    Noguchi, M.2    Kikuchi, G.3
  • 24
    • 0037059054 scopus 로고    scopus 로고
    • Biliverdin reductase: a major physiologic cytoprotectant
    • [24] Baranano, D.E., Rao, M., Ferris, C.D., Snyder, S.H., Biliverdin reductase: a major physiologic cytoprotectant. Proc. Natl. Acad. Sci. 99 (2002), 16093–16098.
    • (2002) Proc. Natl. Acad. Sci. , vol.99 , pp. 16093-16098
    • Baranano, D.E.1    Rao, M.2    Ferris, C.D.3    Snyder, S.H.4
  • 26
    • 70249087960 scopus 로고    scopus 로고
    • The role of c-Jun phosphorylation in EpRE activation of phase II genes
    • [26] Levy, S., Jaiswal, A.K., Forman, H.J., The role of c-Jun phosphorylation in EpRE activation of phase II genes. Free Radic. Biol. Med. 47 (2009), 1172–1179.
    • (2009) Free Radic. Biol. Med. , vol.47 , pp. 1172-1179
    • Levy, S.1    Jaiswal, A.K.2    Forman, H.J.3
  • 27
    • 79953810587 scopus 로고    scopus 로고
    • Oltipraz upregulates the nuclear factor (erythroid-derived 2)-like 2 [corrected](NRF2) antioxidant system and prevents insulin resistance and obesity induced by a high-fat diet in C57BL/6J mice
    • [27] Yu, Z., Shao, W., Chiang, Y., Foltz, W., Zhang, Z., Ling, W., Fantus, I.G., Jin, T., Oltipraz upregulates the nuclear factor (erythroid-derived 2)-like 2 [corrected](NRF2) antioxidant system and prevents insulin resistance and obesity induced by a high-fat diet in C57BL/6J mice. Diabetologia 54 (2011), 922–934.
    • (2011) Diabetologia , vol.54 , pp. 922-934
    • Yu, Z.1    Shao, W.2    Chiang, Y.3    Foltz, W.4    Zhang, Z.5    Ling, W.6    Fantus, I.G.7    Jin, T.8
  • 28
    • 84872333308 scopus 로고    scopus 로고
    • Protection by chrysin, apigenin, and luteolin against oxidative stress is mediated by the Nrf-2-dependent up-regulation of heme oxygenase 1 and glutamate cysteine ligase in rat primary hepatocytes
    • [28] Huang, C.-S., Lii, C.-K., Lin, A.-H., Yeh, Y.-W., Yao, H.-T., Li, C.-C., Wang, T.-S., Chen, H.-W., Protection by chrysin, apigenin, and luteolin against oxidative stress is mediated by the Nrf-2-dependent up-regulation of heme oxygenase 1 and glutamate cysteine ligase in rat primary hepatocytes. Arch. Toxicol. 87 (2013), 167–178.
    • (2013) Arch. Toxicol. , vol.87 , pp. 167-178
    • Huang, C.-S.1    Lii, C.-K.2    Lin, A.-H.3    Yeh, Y.-W.4    Yao, H.-T.5    Li, C.-C.6    Wang, T.-S.7    Chen, H.-W.8
  • 30
    • 84873825700 scopus 로고    scopus 로고
    • Heme oxygenase-1-mediated reactive oxygen species reduction is involved in the inhibitory effect of curcumin on lipopolysaccharide-induced monocyte chemoattractant protein-1 production in RAW264.7 macrophages
    • [30] Zhong, Y., Liu, T., Lai, W., Tan, Y., Tian, D., Guo, Z., Heme oxygenase-1-mediated reactive oxygen species reduction is involved in the inhibitory effect of curcumin on lipopolysaccharide-induced monocyte chemoattractant protein-1 production in RAW264.7 macrophages. Mol. Med. Rep. 7 (2013), 242–246.
    • (2013) Mol. Med. Rep. , vol.7 , pp. 242-246
    • Zhong, Y.1    Liu, T.2    Lai, W.3    Tan, Y.4    Tian, D.5    Guo, Z.6
  • 31
    • 84905494513 scopus 로고    scopus 로고
    • Andrographolide inhibits TNFα-induced ICAM-1 expression via suppression of NADPH oxidase activation and induction of HO-1 and GCLM expression through the PI3K/Akt/Nrf-2 and PI3K/Akt/AP-1 pathways in human endothelial cells
    • [31] Lu, C.-Y., Yang, Y.-C., Li, C.-C., Liu, K.-L., Lii, C.-K., Chen, H.-W., Andrographolide inhibits TNFα-induced ICAM-1 expression via suppression of NADPH oxidase activation and induction of HO-1 and GCLM expression through the PI3K/Akt/Nrf-2 and PI3K/Akt/AP-1 pathways in human endothelial cells. Biochem. Pharmacol. 91 (2014), 40–50.
    • (2014) Biochem. Pharmacol. , vol.91 , pp. 40-50
    • Lu, C.-Y.1    Yang, Y.-C.2    Li, C.-C.3    Liu, K.-L.4    Lii, C.-K.5    Chen, H.-W.6
  • 32
    • 84901944754 scopus 로고    scopus 로고
    • Dietary phytochemicals activate the redox-sensitive transcription factor NRF-2
    • [32] Alrawaiq, N., Abdullah, A., Dietary phytochemicals activate the redox-sensitive transcription factor NRF-2. Int J Pharm Pharm Sci, 6, 2014.
    • (2014) Int J Pharm Pharm Sci , vol.6
    • Alrawaiq, N.1    Abdullah, A.2
  • 33
    • 33646357923 scopus 로고    scopus 로고
    • Calcium-permeable acid-sensing ion channel is a molecular target of the neurotoxic metal ion lead
    • [33] Wang, W., Duan, B., Xu, H., Xu, L., Xu, T.-L., Calcium-permeable acid-sensing ion channel is a molecular target of the neurotoxic metal ion lead. J. Biol. Chem. 281 (2006), 2497–2505.
    • (2006) J. Biol. Chem. , vol.281 , pp. 2497-2505
    • Wang, W.1    Duan, B.2    Xu, H.3    Xu, L.4    Xu, T.-L.5
  • 35
    • 0036740112 scopus 로고    scopus 로고
    • Tea catechins protect against lead-induced cytotoxicity, lipid peroxidation, and membrane fluidity in HepG2 cells
    • [35] Chen, L., Yang, X., Jiao, H., Zhao, B., Tea catechins protect against lead-induced cytotoxicity, lipid peroxidation, and membrane fluidity in HepG2 cells. Toxicol. Sci. 69 (2002), 149–156.
    • (2002) Toxicol. Sci. , vol.69 , pp. 149-156
    • Chen, L.1    Yang, X.2    Jiao, H.3    Zhao, B.4
  • 36
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • [36] 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. 72 (1976), 248–254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 37
    • 84907371574 scopus 로고    scopus 로고
    • Dose-dependent differential response of mammalian cells to cytoplasmic stress is mediated through the heme-regulated eIF2α kinase
    • [37] Mittal, S.P.K., Kulkarni, A.P., Mathai, J., Chattopadhyay, S., Pal, J.K., Dose-dependent differential response of mammalian cells to cytoplasmic stress is mediated through the heme-regulated eIF2α kinase. Int. J. Biochem. Cell Biol. 54 (2014), 186–197.
    • (2014) Int. J. Biochem. Cell Biol. , vol.54 , pp. 186-197
    • Mittal, S.P.K.1    Kulkarni, A.P.2    Mathai, J.3    Chattopadhyay, S.4    Pal, J.K.5
  • 38
    • 84924043221 scopus 로고    scopus 로고
    • Rapid preparation of high purity nuclear proteins from a small number of cultured cells for use in electrophoretic mobility shift assays
    • [38] Luo, Y., Hara, T., Ishido, Y., Yoshihara, A., Oda, K., Makino, M., Ishii, N., Hiroi, N., Suzuki, K., Rapid preparation of high purity nuclear proteins from a small number of cultured cells for use in electrophoretic mobility shift assays. BMC Immunol. 15 (2014), 586–591.
    • (2014) BMC Immunol. , vol.15 , pp. 586-591
    • Luo, Y.1    Hara, T.2    Ishido, Y.3    Yoshihara, A.4    Oda, K.5    Makino, M.6    Ishii, N.7    Hiroi, N.8    Suzuki, K.9
  • 40
    • 84893313155 scopus 로고    scopus 로고
    • Exploring mode of phosphoramidon and Aβ peptide binding to hECE-1 by molecular dynamics and docking studies
    • [40] Barage, S.H., Sonawane, K.D., Exploring mode of phosphoramidon and Aβ peptide binding to hECE-1 by molecular dynamics and docking studies. Protein Pept. Lett. 21 (2014), 140–152.
    • (2014) Protein Pept. Lett. , vol.21 , pp. 140-152
    • Barage, S.H.1    Sonawane, K.D.2
  • 43
    • 84924599431 scopus 로고    scopus 로고
    • Andrographolide Enhances Proliferation and Prevents Dedifferentiation of Rabbit Articular Chondrocytes: An In Vitro Study, Evidence-Based Complementary and Alternative Medicine
    • [43] Luo, L.-K., Wei, Q.-J., Liu, L., Zheng, L., Zhao, J.-M., Andrographolide Enhances Proliferation and Prevents Dedifferentiation of Rabbit Articular Chondrocytes: An In Vitro Study, Evidence-Based Complementary and Alternative Medicine. 2015.
    • (2015)
    • Luo, L.-K.1    Wei, Q.-J.2    Liu, L.3    Zheng, L.4    Zhao, J.-M.5
  • 44
    • 3142570440 scopus 로고    scopus 로고
    • The pathways and molecular mechanisms regulating Nrf-2 activation in response to chemical stress
    • [44] Nguyen, T., Yang, C.S., Pickett, C.B., The pathways and molecular mechanisms regulating Nrf-2 activation in response to chemical stress. Free Radic. Biol. Med. 37 (2004), 433–441.
    • (2004) Free Radic. Biol. Med. , vol.37 , pp. 433-441
    • Nguyen, T.1    Yang, C.S.2    Pickett, C.B.3
  • 45
    • 0035870298 scopus 로고    scopus 로고
    • The Cap'n'Collar basic leucine zipper transcription factor Nrf-2 (NF-E2 p45-related factor 2) controls both constitutive and inducible expression of intestinal detoxification and glutathione biosynthetic enzymes
    • [45] McMahon, M., Itoh, K., Yamamoto, M., Chanas, S.A., Henderson, C.J., McLellan, L.I., Wolf, C.R., Cavin, C., Hayes, J.D., The Cap'n'Collar basic leucine zipper transcription factor Nrf-2 (NF-E2 p45-related factor 2) controls both constitutive and inducible expression of intestinal detoxification and glutathione biosynthetic enzymes. Cancer Res. 61 (2001), 3299–3307.
    • (2001) Cancer Res. , vol.61 , pp. 3299-3307
    • McMahon, M.1    Itoh, K.2    Yamamoto, M.3    Chanas, S.A.4    Henderson, C.J.5    McLellan, L.I.6    Wolf, C.R.7    Cavin, C.8    Hayes, J.D.9
  • 49
    • 33744950387 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3beta inhibits the xenobiotic and antioxidant cell response by direct phosphorylation and nuclear exclusion of the transcription factor Nrf-2
    • [49] Salazar, M., Rojo, A.I., Velasco, D., de Sagarra, R.M., Cuadrado, A., Glycogen synthase kinase-3beta inhibits the xenobiotic and antioxidant cell response by direct phosphorylation and nuclear exclusion of the transcription factor Nrf-2. J. Biol. Chem. 281 (2006), 14841–14851.
    • (2006) J. Biol. Chem. , vol.281 , pp. 14841-14851
    • Salazar, M.1    Rojo, A.I.2    Velasco, D.3    de Sagarra, R.M.4    Cuadrado, A.5
  • 50
    • 83355163388 scopus 로고    scopus 로고
    • Mechanical stretch upregulates microRNA-26a and induces human airway smooth muscle hypertrophy by suppressing glycogen synthase kinase-3β
    • [50] Mohamed, J.S., Lopez, M.A., Boriek, A.M., Mechanical stretch upregulates microRNA-26a and induces human airway smooth muscle hypertrophy by suppressing glycogen synthase kinase-3β. J. Biol. Chem. 286 (2011), 43394–43404.
    • (2011) J. Biol. Chem. , vol.286 , pp. 43394-43404
    • Mohamed, J.S.1    Lopez, M.A.2    Boriek, A.M.3
  • 51
  • 53
    • 0025242387 scopus 로고
    • Hepatoprotective activity of andrographolide from Andrographis paniculata against carbontetrachloride
    • [53] Handa, S.S., Sharma, A., Hepatoprotective activity of andrographolide from Andrographis paniculata against carbontetrachloride. Indian J. Med. Res. 92 (1990), 276–283.
    • (1990) Indian J. Med. Res. , vol.92 , pp. 276-283
    • Handa, S.S.1    Sharma, A.2
  • 54
    • 84857381831 scopus 로고    scopus 로고
    • Andrographolide and its analogues: versatile bioactive molecules for combating inflammation and cancer: andrographolide for inflammation and cancer
    • [54] Lim, J.C.W., Chan, T.K., Ng, D.S.W., Sagineedu, S.R., Stanslas, J., Wong, W.S.F., Andrographolide and its analogues: versatile bioactive molecules for combating inflammation and cancer: andrographolide for inflammation and cancer. Clin. Exp. Pharmacol. Physiol. 39 (2012), 300–310.
    • (2012) Clin. Exp. Pharmacol. Physiol. , vol.39 , pp. 300-310
    • Lim, J.C.W.1    Chan, T.K.2    Ng, D.S.W.3    Sagineedu, S.R.4    Stanslas, J.5    Wong, W.S.F.6
  • 55
    • 84940547876 scopus 로고    scopus 로고
    • Andrographis paniculata transcriptome provides molecular insights into tissue-specific accumulation of medicinal diterpenes
    • [55] Garg, A., Agarwal, L., Misra, R.C., Sharma, S., Ghosh, S., Andrographis paniculata transcriptome provides molecular insights into tissue-specific accumulation of medicinal diterpenes. BMC Genomics, 16, 2015, 659.
    • (2015) BMC Genomics , vol.16 , pp. 659
    • Garg, A.1    Agarwal, L.2    Misra, R.C.3    Sharma, S.4    Ghosh, S.5
  • 56
    • 11244289081 scopus 로고    scopus 로고
    • Solid–liquid extraction of andrographolide from plants—experimental study, kinetic reaction and model
    • [56] Wongkittipong, R., Prat, L., Damronglerd, S., Gourdon, C., Solid–liquid extraction of andrographolide from plants—experimental study, kinetic reaction and model. Sep. Purif. Technol. 40 (2004), 147–154.
    • (2004) Sep. Purif. Technol. , vol.40 , pp. 147-154
    • Wongkittipong, R.1    Prat, L.2    Damronglerd, S.3    Gourdon, C.4
  • 57
    • 84899651898 scopus 로고    scopus 로고
    • Synthesis, structure–activity relationships and biological evaluation of dehydroandrographolide and andrographolide derivatives as novel anti-hepatitis B virus agents
    • [57] Chen, H., Ma, Y.-B., Huang, X.-Y., Geng, C.-A., Zhao, Y., Wang, L.-J., Guo, R.-H., Liang, W.-J., Zhang, X.-M., Chen, J.-J., Synthesis, structure–activity relationships and biological evaluation of dehydroandrographolide and andrographolide derivatives as novel anti-hepatitis B virus agents. Bioorg. Med. Chem. Lett. 24 (2014), 2353–2359.
    • (2014) Bioorg. Med. Chem. Lett. , vol.24 , pp. 2353-2359
    • Chen, H.1    Ma, Y.-B.2    Huang, X.-Y.3    Geng, C.-A.4    Zhao, Y.5    Wang, L.-J.6    Guo, R.-H.7    Liang, W.-J.8    Zhang, X.-M.9    Chen, J.-J.10
  • 58
    • 84890284225 scopus 로고    scopus 로고
    • Andrographolide exerts anti-hepatitis C virus activity by up-regulating haeme oxygenase-1 via the p38 MAPK/Nrf-2 pathway in human hepatoma cells: anti-HCV activity of andrographolide
    • [58] Lee, J.-C., Tseng, C.-K., Young, K.-C., Sun, H.-Y., Wang, S.-W., Chen, W.-C., Lin, C.-K., Wu, Y.-H., Andrographolide exerts anti-hepatitis C virus activity by up-regulating haeme oxygenase-1 via the p38 MAPK/Nrf-2 pathway in human hepatoma cells: anti-HCV activity of andrographolide. Br. J. Pharmacol. 171 (2014), 237–252.
    • (2014) Br. J. Pharmacol. , vol.171 , pp. 237-252
    • Lee, J.-C.1    Tseng, C.-K.2    Young, K.-C.3    Sun, H.-Y.4    Wang, S.-W.5    Chen, W.-C.6    Lin, C.-K.7    Wu, Y.-H.8
  • 59
    • 33644856080 scopus 로고    scopus 로고
    • The double-edged sword of Nrf-2: subversion of redox homeostasis during the evolution of cancer
    • [59] Hayes, J.D., McMahon, M., The double-edged sword of Nrf-2: subversion of redox homeostasis during the evolution of cancer. Mol. Cell 21 (2006), 732–734.
    • (2006) Mol. Cell , vol.21 , pp. 732-734
    • Hayes, J.D.1    McMahon, M.2
  • 62
    • 0037705359 scopus 로고    scopus 로고
    • Transcriptional regulation of heme oxygenase-1 gene expression by MAP kinases of the JNK and p38 pathways in primary cultures of rat hepatocytes
    • [62] Kietzmann, T., Samoylenko, A., Immenschuh, S., Transcriptional regulation of heme oxygenase-1 gene expression by MAP kinases of the JNK and p38 pathways in primary cultures of rat hepatocytes. J. Biol. Chem. 278 (2003), 17927–17936.
    • (2003) J. Biol. Chem. , vol.278 , pp. 17927-17936
    • Kietzmann, T.1    Samoylenko, A.2    Immenschuh, S.3
  • 63
    • 0037383322 scopus 로고    scopus 로고
    • GSK-3: tricks of the trade for a multi-tasking kinase
    • [63] Doble, B.W., GSK-3: tricks of the trade for a multi-tasking kinase. J. Cell Sci. 116 (2003), 1175–1186.
    • (2003) J. Cell Sci. , vol.116 , pp. 1175-1186
    • Doble, B.W.1
  • 64
    • 0442276554 scopus 로고    scopus 로고
    • The glamour and gloom of glycogen synthase kinase-3
    • [64] Jope, R.S., Johnson, G.V.W., The glamour and gloom of glycogen synthase kinase-3. Trends Biochem. Sci. 29 (2004), 95–102.
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 95-102
    • Jope, R.S.1    Johnson, G.V.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.