Juglanthraquinone C, a novel natural compound derived from Juglans mandshurica Maxim, induces S phase arrest and apoptosis in HepG2 cells

Springer Science and Business Media LLC - Tập 17 Số 8 - Trang 832-841 - 2012
Yao Yao1, Yu-Wei Zhang1, Luguo Sun2, Biao Liu3, Yongli Bao1, Hua Lin2, Yu Zhang1, Lihua Zheng2, Yu Sun2, Chunlei Yu1, Yin Wu1, Guan‐Nan Wang1, Yuxin Li2
1National Engineering Laboratory for Druggable Gene and Protein Screening, Northeast Normal University, Changchun, China
2Research Center of Agriculture and Medicine Gene Engineering of Ministry of Education, Northeast Normal University, Changchun, China
3Department of Hand Surgery, China–Japan Union Hospital, Jilin University, Changchun, China

Tóm tắt

Từ khóa


Tài liệu tham khảo

Min BS, Lee SY, Kim JH, Lee JK, Kim TJ, Kim DH, Kim YH, Joung H, Lee HK, Nakamura N, Miyashiro H, Hattori M (2003) Anti-complement activity of constituents from the stem-bark of Juglans mandshurica. Biol Pharm Bull 26:1042–1044

Li G, Lee SY, Lee KS, Lee SW, Kim SH, Lee SH, Lee CS, Woo MH, Son JK (2003) DNA topoisomerases I and II inhibitory activity of constituents isolated from Juglans mandshurica. Arch Pharm Res 26:466–470

Kim SH, Lee KS, Son JK, Je GH, Lee JS, Lee CH, Cheong CJ (1998) Cytotoxic compounds from the roots of Juglans mandshurica. J Nat Prod 61:643–645

Lee KS, Li G, Kim SH, Lee CS, Woo MH, Lee SH, Jhang YD, Son JK (2002) Cytotoxic diarylheptanoids from the roots of Juglans mandshurica. J Nat Prod 65:1707–1708

Min BS, Nakamura N, Miyashiro H, Kim YH, Hattori M (2000) Inhibition of human immunodeficiency virus type 1 reverse transcriptase and ribonuclease H activities by constituents of Juglans mandshurica. Chem Pharm Bull (Tokyo) 48:194–200

Min BS, Lee HK, Lee SM, Kim YH, Bae KH, Otake T, Nakamura N, Hattori M (2002) Anti-human immunodeficiency virus-type 1 activity of constituents from Juglans mandshurica. Arch Pharm Res 25:441–445

Li G, Xu ML, Choi HG, Lee SH, Jahng YD, Lee CS, Moon DC, Woo MH, Son JK (2003) Four new diarylheptanoids from the roots of Juglans mandshurica. Chem Pharm Bull (Tokyo) 51:262–264

Han L, Li W, Narimatsu S, Liu L, Fu H, Okuda H, Koike K (2007) Inhibitory effects of compounds isolated from fruit of Juglans mandshurica on pancreatic lipase. J Nat Med 61:184–186

Lin H, Zhang YW, Zheng LH, Meng XY, Bao YL, Wu Y, Yu CL, Huang YX, Li YX (2011) Anthracene and anthraquinone derivatives from the stem bark of Juglans mandshurica Maxim. Helv Chim Acta 94:1488–1495

Zhang Y, Zhou L, Bao YL, Wu Y, Yu CL, Huang YX, Sun Y, Zheng LH, Li YX (2010) Butyrate induces cell apoptosis through activation of JNK MAP kinase pathway in human colon cancer RKO cells. Chem Biol Interact 185:174–181

Tounekti O, Belehradek J, Mir LM (1995) Relationships between DNA fragmentation, chromatin condensation, and changes in flow cytometry profiles detected during apoptosis. Exp Cell Res 217:506–516

Chen TF, Wong YS (2008) Selenocysteine induces S-phase arrest and apoptosis in human breast adenocarcinoma MCF-7 cells by modulating ERK and Akt phosphorylation. J Agric Food Chem 56:10574–10581

Seim J, Graff P, Amellem O, Landsverk KS, Stokke T, Pettersen EO (2003) Hypoxia-induced irreversible S-phase arrest involves down-regulation of cyclin A. Cell Prolif 36:321–332

Zhu H, Zhang L, Wu S, Teraishi F, Davis JJ, Jacob D, Fang B (2004) Induction of S-phase arrest and p21 overexpression by a small molecule 2-[[3-(2,3-dichlorophenoxy)propyl]amino]ethanol in correlation with activation of ERK. Oncogene 23:4984–4992

Debatin KM (2004) Apoptosis pathways in cancer and cancer therapy. Cancer Immunol Immunother 53:153–159

Aouida M, Mekid H, Belhadj O, Mir LM, Tounekti O (2007) Mitochondria-independent morphological and biochemical apoptotic alterations promoted by the anti-tumor agent bleomycin in Saccharomyces cerevisiae. Biochem Cell Biol 85:49–55

Broker LE, Kruyt FA, Giaccone G (2005) Cell death independent of caspases: a review. Clin Cancer Res 11:3155–3162

Siegel RM (2006) Caspases at the crossroads of immune-cell life and death. Nat Rev Immunol 6:308–317

Thornberry NA, Lazebnik Y (1998) Caspases: enemies within. Science 281:1312–1316

Los M, Wesselborg S, Schulze-Osthoff K (1999) The role of caspases in development, immunity, and apoptotic signal transduction: lessons from knockout mice. Immunity 10:629–639

Degen WG, Pruijn GJ, Raats JM, van Venrooij WJ (2000) Caspase-dependent cleavage of nucleic acids. Cell Death Differ 7:616–627

Earnshaw WC, Martins LM, Kaufmann SH (1999) Mammalian caspases: structure, activation, substrates, and functions during apoptosis. Annu Rev Biochem 68:383–424

Slee EA, Adrain C, Martin SJ (1999) Serial killers: ordering caspase activation events in apoptosis. Cell Death Differ 6:1067–1074

Utz PJ, Anderson P (2000) Life and death decisions: regulation of apoptosis by proteolysis of signaling molecules. Cell Death Differ 7:589–602

Vermeulen K, Van Bockstaele DR, Berneman ZN (2003) The cell cycle: a review of regulation, deregulation and therapeutic targets in cancer. Cell Prolif 36:131–149

Schafer KA (1998) The cell cycle: a review. Vet Pathol 35:461–478

Hengartner MO (2000) The biochemistry of apoptosis. Nature 407:770–776

Kaufmann SH, Hengartner MO (2001) Programmed cell death: alive and well in the new millennium. Trends Cell Biol 11:526–534

Johnstone RW, Ruefli AA, Lowe SW (2002) Apoptosis: a link between cancer genetics and chemotherapy. Cell 108:153–164

Green DR, Reed JC (1998) Mitochondria and Apoptosis. Science 281:1309–1312

Antonsson B (2001) Bax and other pro-apoptotic Bcl-2 family “killer-proteins” and their victim the mitochondrion. Cell Tissue Res 306:347–361

Murray A (1995) Cyclin ubiquitination: the destructive end of mitosis. Cell 81:149–152

Antonsson B, Martinou JC (2000) The Bcl-2 protein family. Exp Cell Res 256:50–57

Reed JC (1997) Double identity for proteins of the Bcl-2 family. Nature 387:773–776

Vander Heiden MG, Thompson CB (1999) Bcl-2 proteins: regulators of apoptosis or of mitochondrial homeostasis? Nat Cell Biol 1:E209–E216

Mayer B, Oberbauer R (2003) Mitochondrial regulation of apoptosis. News Physiol Sci 18:89–94