|Related Categories||Cell Biology, Cell Signaling and Neuroscience, Cell Stress, DNA Repair Proteins and Reagents, DNA-RNA Transcription Regulators,|
|color||red to orange|
|solubility||DMSO: >20 mg/mL|
E3330 is a specific inhibitor of AP endonuclease 1 redox domain. E3330 inhibits APE-1 regulation of transcription factors, but does not affect Ape1 DNA repair activity. AP endonuclease 1 (APE1; also known as REF-1) is a multifunctional protein with dual functions in DNA repair and redox regulation of transcription factors. It is involved in apurinic/apyrimidinic endonuclease DNA base excision repair activity, in proofreading exonuclease activity, and in modulating DNA binding activity of several transcription factors including NF-κB, Egr-1, p53, AP-1, CREB, HIF-α, and members of the Pax family. APE1 is overexpressed in several human cancers, and disruption of APE1 function has detrimental effects on cancer cell viability. E3330 significantly reduces the growth of human pancreatic cancer cells in vitro and inhibits pancreatic cancer cell migration.
APE1/Ref-1 regulates STAT3 transcriptional activity and APE1/Ref-1-STAT3 dual-targeting effectively inhibits pancreatic cancer cell survival. Cardoso AA, Jiang Y, Luo M, et al. PLoS ONE 7(10), e47462, (2012)
Knock-in reconstitution studies reveal an unexpected role of Cys-65 in regulating APE1/Ref-1 subcellular trafficking and function. Vascotto C, Bisetto E, Li M, et al. Mol. Biol. Cell 22(20), 3887-901, (2011)
Functional analysis of novel analogues of E3330 that block the redox signaling activity of the multifunctional AP endonuclease/redox signaling enzyme APE1/Ref-1. Kelley MR, Luo M, Reed A, et al. Antioxid. Redox Signal. 14(8), 1387-401, (2011)
The Ape-1/Ref-1 redox antagonist E3330 inhibits the growth of tumor endothelium and endothelial progenitor cells: therapeutic implications in tumor angiogenesis. Zou GM, Karikari C, Kabe Y, et al. J. Cell Physiol. 219(1), 209-18, (2009)
Role of the multifunctional DNA repair and redox signaling protein Ape1/Ref-1 in cancer and endothelial cells: small-molecule inhibition of the redox function of Ape1. Luo M, Delaplane S, Jiang A, et al. Antioxid. Redox Signal. 10(11), 1853-67, (2008)
Augmentation of tumor necrosis factor family-induced apoptosis by E3330 in human hepatocellular carcinoma cell lines via inhibition of NF kappa B. Saitou Y, Shiraki K, Yamanaka T, et al. World J. Gastroenterol. 11(40), 6258-61, (2005)
Splenectomy enhances liver regeneration through tumor necrosis factor (TNF)-alpha following dimethylnitrosamine-induced cirrhotic rat model. Murata K, Shiraki K, Sugimoto K, et al. Hepatogastroenterology. 48(40), 1022-7, (2001)
Mad2 haploinsufficiency protects hematopoietic progenitor cells subjected to cell-cycle stress in vivo and to inhibition of redox function of Ape1/Ref-1 in vitro. Rohrabaugh SL, Hangoc G, Kelley MR, et al. Exp. Hematol. 39(4), 415-23, (2011)
Inhibition of the redox function of APE1/Ref-1 in myeloid leukemia cell lines results in a hypersensitive response to retinoic acid-induced differentiation and apoptosis. Fishel ML, Colvin ES, Luo M, et al. Exp. Hematol. 38(12), 1178-88, (2010)
Design and synthesis of novel quinone inhibitors targeted to the redox function of apurinic/apyrimidinic endonuclease 1/redox enhancing factor-1 (Ape1/ref-1). Nyland, R. L.; et al. J. Med. Chem. 53, 1200, (2010)
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