Bcl-x
Bcl-2
Bcl-xL
Mcl-1
apoptosis
chemotherapy
cholangiocarcinoma
Journal
Liver international : official journal of the International Association for the Study of the Liver
ISSN: 1478-3231
Titre abrégé: Liver Int
Pays: United States
ID NLM: 101160857
Informations de publication
Date de publication:
12 2022
12 2022
Historique:
revised:
26
07
2022
received:
11
01
2022
accepted:
08
08
2022
pubmed:
20
8
2022
medline:
25
11
2022
entrez:
19
8
2022
Statut:
ppublish
Résumé
Intrahepatic, perihilar, and distal cholangiocarcinoma (iCCA, pCCA, dCCA) are highly malignant tumours with increasing mortality rates due to therapy resistances. Among the mechanisms mediating resistance, overexpression of anti-apoptotic Bcl-2 proteins (Bcl-2, Bcl-x
Substances chimiques
bcl-X Protein
0
Myeloid Cell Leukemia Sequence 1 Protein
0
Proto-Oncogene Proteins c-bcl-2
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
2855-2870Informations de copyright
© 2022 The Authors. Liver International published by John Wiley & Sons Ltd.
Références
Florio AA, Ferlay J, Znaor A, et al. Global trends in intrahepatic and extrahepatic cholangiocarcinoma incidence from 1993 to 2012. Cancer. 2020;126(11):2666-2678. doi:10.1002/cncr.32803
Banales JM, Marin JJG, Lamarca A, et al. Cholangiocarcinoma 2020: the next horizon in mechanisms and management. Nat Rev Gastroenterol Hepatol. 2020;17:557-588. doi:10.1038/s41575-020-0310-z
Bertuccio P, Malvezzi M, Carioli G, et al. Global trends in mortality from intrahepatic and extrahepatic cholangiocarcinoma. J Hepatol. 2019;71:104-114. doi:10.1016/j.jhep.2019.03.013
Khan SA, Davidson BR, Goldin RD, et al. Guidelines for the diagnosis and treatment of cholangiocarcinoma: an update. Gut. 2012;61:1657-1669. doi:10.1136/gutjnl-2011-301748
Rizvi S, Khan SA, Hallemeier CL, Kelley RK, Gores GJ. Cholangiocarcinoma - evolving concepts and therapeutic strategies. Nat Rev Clin Oncol. 2018;15:95-111. doi:10.1038/nrclinonc.2017.157
Hanahan D, Weinberg RA. The hallmarks of cancer. Cell. 2000;100:57-70. doi:10.1016/s0092-8674(00)81683-9
Cory S, Adams JM. The Bcl2 family: regulators of the cellular life-or-death switch. Nat Rev Cancer. 2002;2:647-656. doi:10.1038/nrc883
Scherr AL, Gdynia G, Salou M, et al. Bcl-xL is an oncogenic driver in colorectal cancer. Cell Death Dis. 2016;7:e2342. doi:10.1038/cddis.2016.233
Lee EF, Harris TJ, Tran S, et al. BCL-XL and MCL-1 are the key BCL-2 family proteins in melanoma cell survival. Cell Death Dis. 2019;10:342. doi:10.1038/s41419-019-1568-3
Czabotar PE, Lessene G, Strasser A, Adams JM. Control of apoptosis by the BCL-2 protein family: implications for physiology and therapy. Nat Rev Mol Cell Biol. 2014;15:49-63. doi:10.1038/nrm3722
Ashkenazi A, Fairbrother WJ, Leverson JD, Souers AJ. From basic apoptosis discoveries to advanced selective BCL-2 family inhibitors. Nat Rev Drug Discov. 2017;16:273-284. doi:10.1038/nrd.2016.253
Roberts AW, Huang D. Targeting BCL2 with BH3 mimetics: basic science and clinical application of Venetoclax in chronic lymphocytic leukemia and related B cell malignancies. Clin Pharmacol Ther. 2017;101:89-98. doi:10.1002/cpt.553
DiNardo CD, Jonas BA, Pullarkat V, et al. Azacitidine and Venetoclax in previously untreated acute myeloid leukemia. N Engl J Med. 2020;383:617-629. doi:10.1056/NEJMoa2012971
Fischer K, al-Sawaf O, Bahlo J, et al. Venetoclax and Obinutuzumab in patients with CLL and coexisting conditions. N Engl J Med. 2019;380:2225-2236. doi:10.1056/NEJMoa1815281
Leverson JD, Phillips DC, Mitten MJ, et al. Exploiting selective BCL-2 family inhibitors to dissect cell survival dependencies and define improved strategies for cancer therapy. Sci Transl Med. 2015;7:279-240. doi:10.1126/scitranslmed.aaa4642
Inoue-Yamauchi A, Jeng PS, Kim K, et al. Targeting the differential addiction to anti-apoptotic BCL-2 family for cancer therapy. Nat Commun. 2017;8:16078. doi:10.1038/ncomms16078
Scherr AL, Mock A, Gdynia G, et al. Identification of BCL-XL as highly active survival factor and promising therapeutic target in colorectal cancer. Cell Death Dis. 2020;11:875. doi:10.1038/s41419-020-03092-7
Horak P, Heining C, Kreutzfeldt S, et al. Comprehensive genomic and transcriptomic analysis for guiding therapeutic decisions in patients with rare cancers. Cancer Discov. 2021;11:2780-2795. doi:10.1158/2159-8290.CD-21-0126
Horak P, Klink B, Heining C, et al. Precision oncology based on omics data: the NCT Heidelberg experience. Int J Cancer. 2017;141:877-886. doi:10.1002/ijc.30828
Ding H, Douglass EF Jr, Sonabend AM, et al. Quantitative assessment of protein activity in orphan tissues and single cells using the metaVIPER algorithm. Nat Commun. 2018;9:1471. doi:10.1038/s41467-018-03843-3
Elssner C, Goeppert B, Longerich T, et al. Nuclear translocation of RELB is increased in diseased human liver and promotes ductular reaction and biliary fibrosis in mice. Gastroenterology. 2019;156:1190-1205 e1114. doi:10.1053/j.gastro.2018.11.018
Beeghly-Fadiel A, Wilson AJ, Keene S, et al. Differential cyclooxygenase expression levels and survival associations in type I and type II ovarian tumors. J Ovarian Res. 2018;11:17. doi:10.1186/s13048-018-0389-9
Banales JM, Sáez E, Úriz M, et al. Up-regulation of microRNA 506 leads to decreased cl-/HCO3- anion exchanger 2 expression in biliary epithelium of patients with primary biliary cirrhosis. Hepatology. 2012;56:687-697. doi:10.1002/hep.25691
Grubman SA, Perrone RD, Lee DW, et al. Regulation of intracellular pH by immortalized human intrahepatic biliary epithelial cell lines. Am J Physiol. 1994;266:G1060-1070. doi:10.1152/ajpgi.1994.266.6.G1060
Riccardi C, Nicoletti I. Analysis of apoptosis by propidium iodide staining and flow cytometry. Nat Protoc. 2006;1:1458-1461. doi:10.1038/nprot.2006.238
Hothorn TLB. On the exact distribution of maximally selected rank statistics. Comput Stat Data Anal. 2003;43:121-137. doi:10.1016/S0167-9473(02)00225-6
Abou-Alfa GK, Sahai V, Hollebecque A, et al. Pemigatinib for previously treated, locally advanced or metastatic cholangiocarcinoma: a multicentre, open-label, phase 2 study. Lancet Oncol. 2020;21:671-684. doi:10.1016/S1470-2045(20)30109-1
Abou-Alfa GK, Macarulla T, Javle MM, et al. Ivosidenib in IDH1-mutant, chemotherapy-refractory cholangiocarcinoma (ClarIDHy): a multicentre, randomised, double-blind, placebo-controlled, phase 3 study. Lancet Oncol. 2020;21:796-807. doi:10.1016/S1470-2045(20)30157-1
Okaro AC, Deery AR, Hutchins RR, Davidson BR. The expression of antiapoptotic proteins Bcl-2, Bcl-X(L), and Mcl-1 in benign, dysplastic, and malignant biliary epithelium. J Clin Pathol. 2001;54:927-932. doi:10.1136/jcp.54.12.927
Charlotte F, L'Herminé A, Martin N, et al. Immunohistochemical detection of bcl-2 protein in normal and pathological human liver. Am J Pathol. 1994;144:460-465.
Skopelitou A, Hadjiyannakis M, Alexopoulou V, Krikoni O, Kamina S, Agnantis N. Topographical immunohistochemical expression of bcl-2 protein in human liver lesions. Anticancer Res. 1996;16:975-978.
Harnois DM, Que FG, Celli A, LaRusso NF, Gores GJ. Bcl-2 is overexpressed and alters the threshold for apoptosis in a cholangiocarcinoma cell line. Hepatology. 1997;26:884-890. doi:10.1002/hep.510260413
Ross JS, Wang K, Gay L, et al. New routes to targeted therapy of intrahepatic cholangiocarcinomas revealed by next-generation sequencing. Oncologist. 2014;19:235-242. doi:10.1634/theoncologist.2013-0352
Li S, Guo W, Wu H. The role of post-translational modifications in the regulation of MCL1. Cell Signal. 2021;81:109933. doi:10.1016/j.cellsig.2021.109933
Onyeagucha B, Subbarayalu P, Abdelfattah N, et al. Novel post-transcriptional and post-translational regulation of pro-apoptotic protein BOK and anti-apoptotic protein Mcl-1 determine the fate of breast cancer cells to survive or die. Oncotarget. 2017;8:85984-85996. doi:10.18632/oncotarget.20841
Bobo C, Céré C, Dufossée M, et al. Improved electrophoretic separation to assist the monitoring of Bcl-xL post-translational modifications. Int J Mol Sci. 2019;20:5571. doi:10.3390/ijms20225571
Follis AV, Llambi F, Kalkavan H, et al. Regulation of apoptosis by an intrinsically disordered region of Bcl-xL. Nat Chem Biol. 2018;14:458-465. doi:10.1038/s41589-018-0011-x
Zucchini N, de Sousa G, Bailly-Maitre B, et al. Regulation of Bcl-2 and Bcl-xL anti-apoptotic protein expression by nuclear receptor PXR in primary cultures of human and rat hepatocytes. Biochim Biophys Acta. 2005;1745:48-58. doi:10.1016/j.bbamcr.2005.02.005
Konig SM, Rissler V, Terkelsen T, Lambrughi M, Papaleo E. Alterations of the interactome of Bcl-2 proteins in breast cancer at the transcriptional, mutational and structural level. PLoS Comput Biol. 2019;15:e1007485. doi:10.1371/journal.pcbi.1007485
Weeden CE, Ah-Cann C, Holik AZ, et al. Dual inhibition of BCL-XL and MCL-1 is required to induce tumour regression in lung squamous cell carcinomas sensitive to FGFR inhibition. Oncogene. 2018;37:4475-4488. doi:10.1038/s41388-018-0268-2
Williams MM, Elion DL, Rahman B, Hicks DJ, Sanchez V, Cook RS. Therapeutic inhibition of Mcl-1 blocks cell survival in estrogen receptor-positive breast cancers. Oncotarget. 2019;10:5389-5402. doi:10.18632/oncotarget.27070
Yasuda Y, Ozasa H, Kim YH, et al. MCL1 inhibition is effective against a subset of small-cell lung cancer with high MCL1 and low BCL-XL expression. Cell Death Dis. 2020;11:177. doi:10.1038/s41419-020-2379-2
Wang W, Zhan M, Li Q, et al. FXR agonists enhance the sensitivity of biliary tract cancer cells to cisplatin via SHP dependent inhibition of Bcl-xL expression. Oncotarget. 2016;7:34617-34629. doi:10.18632/oncotarget.8964
Wu X, Luo Q, Liu Z. Ubiquitination and deubiquitination of MCL1 in cancer: deciphering chemoresistance mechanisms and providing potential therapeutic options. Cell Death Dis. 2020;11:556. doi:10.1038/s41419-020-02760-y
Wood KC. Overcoming MCL-1-driven adaptive resistance to targeted therapies. Nat Commun. 2020;11:531. doi:10.1038/s41467-020-14392-z
Bose P, Gandhi V, Konopleva M. Pathways and mechanisms of venetoclax resistance. Leuk Lymphoma. 2017;58:1-17. doi:10.1080/10428194.2017.1283032
Wang Q, Wan J, Zhang W, Hao S. MCL-1 or BCL-xL-dependent resistance to the BCL-2 antagonist (ABT-199) can be overcome by specific inhibitor as single agents and in combination with ABT-199 in acute myeloid leukemia cells. Leuk Lymphoma. 2019;60:2170-2180. doi:10.1080/10428194.2018.1563694
Josefsson EC, Vainchenker W, James C. Regulation of platelet production and life span: role of Bcl-xL and potential implications for human platelet diseases. Int J Mol Sci. 2020;21:7591. doi:10.3390/ijms21207591
Khan S, Zhang X, Lv D, et al. A selective BCL-XL PROTAC degrader achieves safe and potent antitumor activity. Nat Med. 2019;25:1938-1947. doi:10.1038/s41591-019-0668-z
Afreen S, Bohler S, Müller A, et al. BCL-XL expression is essential for human erythropoiesis and engraftment of hematopoietic stem cells. Cell Death Dis. 2020;11:8. doi:10.1038/s41419-019-2203-z
Mukherjee N, Skees J, Todd KJ, et al. MCL1 inhibitors S63845/MIK665 plus navitoclax synergistically kill difficult-to-treat melanoma cells. Cell Death Dis. 2020;11:443. doi:10.1038/s41419-020-2646-2
Sjostrom J, Blomqvist C, von Boguslawski K, et al. The predictive value of bcl-2, bax, bcl-xL, bag-1, fas, and fasL for chemotherapy response in advanced breast cancer. Clin Cancer Res. 2002;8:811-816.
Dunne PD, Coleman HG, Bankhead P, et al. Bcl-xL as a poor prognostic biomarker and predictor of response to adjuvant chemotherapy specifically in BRAF-mutant stage II and III colon cancer. Oncotarget. 2018;9:13834-13847. doi:10.18632/oncotarget.24481
Ben-Hamo R, Jacob Berger A, Gavert N, et al. Predicting and affecting response to cancer therapy based on pathway-level biomarkers. Nat Commun. 2020;11:3296. doi:10.1038/s41467-020-17090-y
Jin-Song Y, Zhao-Xia W, Cheng-Yu L, et al. Prognostic significance of Bcl-xL gene expression in human colorectal cancer. Acta Histochem. 2011;113:810-814. doi:10.1016/j.acthis.2011.01.002
Groeger AM, Esposito V, de Luca A, et al. Prognostic value of immunohistochemical expression of p53, bax, Bcl-2 and Bcl-xL in resected non-small-cell lung cancers. Histopathology. 2004;44:54-63. doi:10.1111/j.1365-2559.2004.01750.x
Addeo R, Caraglia M, Baldi A, et al. Prognostic role of bcl-xL and p53 in childhood acute lymphoblastic leukemia (ALL). Cancer Biol Ther. 2005;4:32-38. doi:10.4161/cbt.4.1.1371
Friess H, Lu Z, Andrén-Sandberg Å, et al. Moderate activation of the apoptosis inhibitor bcl-xL worsens the prognosis in pancreatic cancer. Ann Surg. 1998;228:780-787. doi:10.1097/00000658-199812000-00009
Jusakul A, Cutcutache I, Yong CH, et al. Whole-genome and epigenomic landscapes of etiologically distinct subtypes of cholangiocarcinoma. Cancer Discov. 2017;7:1116-1135. doi:10.1158/2159-8290.CD-17-0368
Nakamura H, Arai Y, Totoki Y, et al. Genomic spectra of biliary tract cancer. Nat Genet. 2015;47:1003-1010. doi:10.1038/ng.3375
Akita M, Sofue K, Fujikura K, et al. Histological and molecular characterization of intrahepatic bile duct cancers suggests an expanded definition of perihilar cholangiocarcinoma. HPB (Oxford). 2019;21:226-234. doi:10.1016/j.hpb.2018.07.021
Lowery MA, Ptashkin R, Jordan E, et al. Comprehensive molecular profiling of intrahepatic and extrahepatic Cholangiocarcinomas: potential targets for intervention. Clin Cancer Res. 2018;24:4154-4161. doi:10.1158/1078-0432.CCR-18-0078
Kendall T, Verheij J, Gaudio E, et al. Anatomical, histomorphological and molecular classification of cholangiocarcinoma. Liver Int. 2019;39(Suppl 1):7-18. doi:10.1111/liv.14093
Arai Y, Totoki Y, Hosoda F, et al. Fibroblast growth factor receptor 2 tyrosine kinase fusions define a unique molecular subtype of cholangiocarcinoma. Hepatology. 2014;59:1427-1434. doi:10.1002/hep.26890
Kipp BR, Voss JS, Kerr SE, et al. Isocitrate dehydrogenase 1 and 2 mutations in cholangiocarcinoma. Hum Pathol. 2012;43:1552-1558. doi:10.1016/j.humpath.2011.12.007
Rizzo A. Targeted therapies in advanced cholangiocarcinoma: a focus on FGFR inhibitors. Medicina (Kaunas). 2021;57:458. doi:10.3390/medicina57050458
Goyal L, Kongpetch S, Crolley VE, Bridgewater J. Targeting FGFR inhibition in cholangiocarcinoma. Cancer Treat Rev. 2021;95:102170. doi:10.1016/j.ctrv.2021.102170
Hoyos S, Navas MC, Restrepo JC, Botero RC. Current controversies in cholangiocarcinoma. Biochim Biophys Acta Mol Basis Dis. 2018;1864:1461-1467. doi:10.1016/j.bbadis.2017.07.027