Top

Published in:

Open Access 01-09-2019 | Ritonavir | Review Article

Cytochrome P450 3A4, 3A5, and 2C8 expression in breast, prostate, lung, endometrial, and ovarian tumors: relevance for resistance to taxanes

Authors: Maarten van Eijk, René J. Boosman, Alfred H. Schinkel, Alwin D. R. Huitema, Jos H. Beijnen

Published in: Cancer Chemotherapy and Pharmacology | Issue 3/2019

Abstract

Enzymes of the cytochrome P450 (CYP) subfamily 3A and 2C play a major role in the metabolism of taxane anticancer agents. While their function in hepatic metabolism of taxanes is well established, expression of these enzymes in solid tumors may play a role in the in situ metabolism of drugs as well, potentially affecting the intrinsic taxane susceptibility of these tumors. This article reviews the available literature on intratumoral expression of docetaxel- and paclitaxel-metabolizing enzymes in mammary, prostate, lung, endometrial, and ovarian tumors. Furthermore, the clinical implications of the intratumoral expression of these enzymes are reviewed and the potential of concomitant treatment with protease inhibitors (PIs) as a method to inhibit CYP3A4-mediated metabolism is discussed.

World Health Organization International Agency for Research on Cancer (IACR) (2018) GLOBOCAN 2018: IARC Global Cancer Observatory. http://gco.iarc.fr/today/home. Accessed 31 May 2019

Montero A, Fossella F, Hortobagyi G, Valero V (2005) Docetaxel for treatment of solid tumours: a systematic review of clinical data. Lancet Oncol 6:229–239. https://doi.org/10.1016/S1470-2045(05)70094-2 CrossRefPubMed

Crown J, O’Leary M (2000) The taxanes: an update. Lancet 355:1176–1178. https://doi.org/10.1016/S0140-6736(00)02074-2 CrossRefPubMed

Akram T, Maseelall P, Fanning J (2005) Carboplatin and paclitaxel for the treatment of advanced or recurrent endometrial cancer. Am J Obstet Gynecol 192:1365–1367. https://doi.org/10.1016/j.ajog.2004.12.032 CrossRefPubMed

Tannock IF, de Wit R, Berry WR et al (2004) Docetaxel plus prednisone or mitoxantrone plus prednisone for advanced prostate cancer. N Engl J Med 351:1502–1512. https://doi.org/10.1056/NEJMoa040720 CrossRefPubMed

Masoud V, Pagès G (2017) Targeted therapies in breast cancer: new challenges to fight against resistance. World J Clin Oncol 8:120. https://doi.org/10.5306/wjco.v8.i2.120 CrossRefPubMedPubMedCentral

Serpa Neto A, Tobias-Machado M, Kaliks R et al (2011) Ten years of docetaxel-based therapies in prostate adenocarcinoma: a systematic review and meta-analysis of 2244 patients in 12 randomized clinical trials. Clin Genitourin Cancer 9:115–123. https://doi.org/10.1016/j.clgc.2011.05.002 CrossRefPubMed

Sweeney CJ, Chen Y-H, Carducci M et al (2015) Chemohormonal therapy in metastatic hormone-sensitive prostate cancer. N Engl J Med 373:737–746. https://doi.org/10.1056/NEJMoa1503747 CrossRefPubMedPubMedCentral

James ND, Sydes MR, Clarke NW et al (2016) Addition of docetaxel, zoledronic acid, or both to first-line long-term hormone therapy in prostate cancer (STAMPEDE): survival results from an adaptive, multiarm, multistage, platform randomised controlled trial. Lancet 387:1163–1177. https://doi.org/10.1016/S0140-6736(15)01037-5 CrossRefPubMedPubMedCentral

10.

Tulsyan S, Chaturvedi P, Singh AK et al (2014) Assessment of clinical outcomes in breast cancer patients treated with taxanes: multi-analytical approach. Gene. https://doi.org/10.1016/j.gene.2014.04.004 CrossRefPubMed

11.

Gligorov J, Lotz JP (2004) Preclinical pharmacology of the taxanes: implications of the differences. Oncologist 9:3–8. https://doi.org/10.1634/theoncologist.9-suppl_2-3 CrossRefPubMed

12.

Lyseng-Williamson KA, Fenton C (2005) Docetaxel: a review of its use in metastatic breast cancer. Drugs 65:2513–2531. https://doi.org/10.2165/00003495-200565170-00007 CrossRefPubMed

13.

Cortes JE, Pazdur R (1995) Docetaxel. J Clin Oncol 13:2643–2655. https://doi.org/10.1200/JCO.1995.13.10.2643 CrossRefPubMed

14.

Gan L, Wang J, Xu H, Yang X (2011) Resistance to docetaxel-induced apoptosis in prostate cancer cells by p38/p53/p21 signaling. Prostate 71:1158–1166. https://doi.org/10.1002/pros.21331 CrossRefPubMed

15.

Patterson SG, Wei S, Chen X et al (2006) Novel role of Stat1 in the development of docetaxel resistance in prostate tumor cells. Oncogene 25:6113–6122. https://doi.org/10.1038/sj.onc.1209632 CrossRefPubMed

16.

Codony-Servat J, Marín-Aguilera M, Visa L et al (2013) Nuclear factor-kappa B and interleukin-6 related docetaxel resistance in castration-resistant prostate cancer. Prostate 73:512–521. https://doi.org/10.1002/pros.22591 CrossRefPubMed

17.

Brown I, Shalli K, McDonald SL et al (2004) Reduced expression of p27 is a novel mechanism of docetaxel resistance in breast cancer cells. Breast Cancer Res 6:R601–R607. https://doi.org/10.1186/bcr918 CrossRefPubMedPubMedCentral

18.

Zhang X, Zhong S, Xu Y et al (2016) MicroRNA-3646 contributes to docetaxel resistance in human breast cancer cells by GSK-3β/β-catenin signaling pathway. PLoS One. https://doi.org/10.1371/journal.pone.0153194 CrossRefPubMedPubMedCentral

19.

Valero V, Jones SE, Von Hoff DD et al (1998) A phase II study of docetaxel in patients with paclitaxel-resistant metastatic breast cancer. J Clin Oncol 16:3362–3368. https://doi.org/10.1200/JCO.1998.16.10.3362 CrossRefPubMed

20.

Verschraegen CF, Sittisomwong T, Kudelka AP et al (2000) Docetaxel for patients with paclitaxel-resistant mullerian carcinoma. J Clin Oncol 18:2733–2739. https://doi.org/10.1200/JCO.2000.18.14.2733 CrossRefPubMed

21.

Kondoh C, Takahari D, Shitara K et al (2012) Efficacy of docetaxel in patients with paclitaxel-resistant advanced gastric cancer. Gan To Kagaku Ryoho 39:1511–1515PubMed

22.

Zunino F, Cassinelli G, Polizzi D, Perego P (1999) Molecular mechanisms of resistance to taxanes and therapeutic implications. Drug Resist Updat 2:351–357. https://doi.org/10.1054/drup.1999.0108 CrossRefPubMed

23.

Germano S, O’Driscoll L (2009) Breast cancer: understanding sensitivity and resistance to chemotherapy and targeted therapies to aid in personalised medicine. Curr Cancer Drug Targets 9:398–418. https://doi.org/10.2174/156800909788166529 CrossRefPubMed

24.

Engels FK, Ten Tije AJ, Baker SD et al (2004) Effect of cytochrome P450 3A4 inhibition on the pharmacokinetics of docetaxel. Clin Pharmacol Ther 75:448–454. https://doi.org/10.1016/j.clpt.2004.01.001 CrossRefPubMed

25.

Cresteil T, Monsarrat B, Dubois J et al (2002) Regioselective metabolism of taxoids by human CYP3A4 and 2C8: structure–activity relationship. Drug Metab Dispos 30:438–445. https://doi.org/10.1124/dmd.30.4.438 CrossRefPubMed

26.

Shou M, Martinet M, Korzekwa KR et al (1998) Role of human cytochrome P450 3A4 and 3A5 in the metabolism of Taxotere and its derivatives: enzyme specificity, interindividual distribution and metabolic contribution in human liver. Pharmacogenetics 8:391–401. https://doi.org/10.1097/00008571-199810000-00004 CrossRefPubMed

27.

Thelen K, Dressman JB (2009) Cytochrome P450-mediated metabolism in the human gut wall. J Pharm Pharmacol 61:541–558. https://doi.org/10.1211/jpp/61.05.0002 CrossRefPubMed

28.

Oyama T, Kagawa N, Naoki Kunugita N et al (2004) Expression of cytochrome P450 in tumor tissues and its association with cancer development. Front Biosci 9:1967–1976. https://doi.org/10.2741/1378 CrossRefPubMed

29.

Kapucuoglu N, Coban T, Raunio H et al (2003) Expression of CYP3A4 in human breast tumour and non-tumour tissues. Cancer Lett 202:17–23. https://doi.org/10.1016/j.canlet.2003.08.015 CrossRefPubMed

30.

Martínez C, García-Martín E, Pizarro RM et al (2002) Expression of paclitaxel-inactivating CYP3A activity in human colorectal cancer: implications for drug therapy. Br J Cancer 87:681–686. https://doi.org/10.1038/sj.bjc.6600494 CrossRefPubMedPubMedCentral

31.

Murray GI, Shaw D, Weaver RJ et al (1994) Cytochrome P450 expression in oesophageal cancer. Gut 35:599–603. https://doi.org/10.1136/gut.35.5.599 CrossRefPubMedPubMedCentral

32.

Murray GI, Patimalla S, Stewart KN et al (2010) Profiling the expression of cytochrome P450 in breast cancer. Histopathology 57:202–211. https://doi.org/10.1111/j.1365-2559.2010.03606.x CrossRefPubMed

33.

Zia H, Murray GI, Vyhlidal CA et al (2015) CYP3A isoforms in Ewing’s sarcoma tumours: an immunohistochemical study with clinical correlation. Int J Exp Pathol 96:81–86. https://doi.org/10.1111/iep.12115 CrossRefPubMedPubMedCentral

34.

Sparreboom A, Huizing MT, Boesen JJB et al (1995) Isolation, purification, and biological activity of mono- and dihydroxylated paclitaxel metabolites from human feces. Cancer Chemother Pharmacol 36:299–304. https://doi.org/10.1007/BF00689047 CrossRefPubMed

35.

Sparreboom A, Van Tellingen O, Scherrenburg EJ et al (1996) Isolation, purification and biological activity of major docetaxel metabolites from human feces. Drug Metab Dispos 24:655–658PubMed

36.

Nelson DR (1998) Cytochrome P450 nomenclature. Methods Mol Biol 107:15–24. https://doi.org/10.1385/0-89603-519-0:15 CrossRefPubMed

37.

De Jonge M, Huitema A, Rodenhuis S, Beijnen JH (2005) Clinical pharmacokinetics of cyclophosphamide. Clin Pharmacokinet 44:1135–1164CrossRefPubMed

38.

Bruno RD, Njar VCO (2007) Targeting cytochrome P450 enzymes: a new approach in anti-cancer drug development. Bioorg Med Chem 15:5047–5060. https://doi.org/10.1016/j.bmc.2007.05.046 CrossRefPubMedPubMedCentral

39.

Rendic S, Guengerich FP (2012) Contributions of human enzymes in carcinogen metabolism. Chem Res Toxicol 25:1316–1383. https://doi.org/10.1021/tx300132k CrossRefPubMedPubMedCentral

40.

Zanger UM, Schwab M (2008) Cytochrome P450 enzymes in drug metabolism: regulation of gene expression, enzyme activities, and impact of genetic variation. Pharmacol Ther 138:103–141. https://doi.org/10.1016/j.pharmthera.2012.12.007 CrossRef

41.

Traunecker HCL, Stevens MCG, Kerr DJ, Ferry DR (1999) The acridone carboxamide GF120918 potently reverses P-glycoprotein-mediated resistance in human sarcoma MES-Dx5 cells. Br J Cancer 81:942–951. https://doi.org/10.1038/sj.bjc.6690791 CrossRefPubMedPubMedCentral

42.

Bertilsson G, Heidrich J, Svensson K et al (1998) Identification of a human nuclear receptor defines a new signaling pathway for CYP3A induction. Proc Natl Acad Sci USA 95:12208–12213. https://doi.org/10.1073/pnas.95.21.12208 CrossRefPubMedPubMedCentral

43.

Blumberg B, Sabbagh W, Juguilon H et al (1998) SXR, a novel steroid and xenobiotic-sensing nuclear receptor. Genes Dev 12:3195–3205. https://doi.org/10.1101/gad.12.20.3195 CrossRefPubMedPubMedCentral

44.

Kliewer SA, Moore JT, Wade L et al (1998) An orphan nuclear receptor activated by pregnanes defines a novel steroid signaling pathway. Cell 92:73–82. https://doi.org/10.1016/S0092-8674(00)80900-9 CrossRefPubMed

45.

Lehmann JM, McKee DD, Watson MA et al (1998) The human orphan nuclear receptor PXR is activated by compounds that regulate CYP3A4 gene expression and cause drug interactions. J Clin Investig 102:1016–1023. https://doi.org/10.1172/JCI3703 CrossRefPubMedPubMedCentral

46.

Banerjee M, Robbins D, Chen T (2013) Modulation of xenobiotic receptors by steroids. Molecules 18:7389–7406. https://doi.org/10.3390/molecules18077389 CrossRefPubMedPubMedCentral

47.

Goodwin B, Hodgson E, Liddle C (1999) The orphan human pregnane X receptor mediates the transcriptional activation of CYP3A4 by rifampicin through a distal enhancer module. Mol Pharmacol 56:1329–1339. https://doi.org/10.1124/mol.56.6.1329 CrossRefPubMed

48.

Huss JM, Wang SI, Astrom A et al (1996) Dexamethasone responsiveness of a major glucocorticoid-inducible CYP3A gene is mediated by elements unrelated to a glucocorticoid receptor binding motif. Proc Natl Acad Sci USA 93:4666–4670. https://doi.org/10.1073/pnas.93.10.4666 CrossRefPubMedPubMedCentral

49.

Synold T, Dussault I, Forman B (2001) The orphan nuclear receptor SXR coordinately regulates drug metabolism and efflux. Nat Med 7:1–7. https://doi.org/10.1038/87912 CrossRef

50.

Masuyama H, Hiramatsu Y, Kodama JI, Kudo T (2003) Expression and potential roles of pregnane X receptor in endometrial cancer. J Clin Endocrinol Metab 88:4446–4454. https://doi.org/10.1210/jc.2003-030203 CrossRefPubMed

51.

Miki Y, Suzuki T, Kitada K et al (2006) Expression of the steroid and xenobiotic receptor and its possible target gene, organic anion transporting polypeptide-A, in human breast carcinoma. Cancer Res 66:535–542. https://doi.org/10.1158/0008-5472.CAN-05-1070 CrossRefPubMed

52.

Nallani SC, Goodwin B, Buckley AR et al (2004) Differences in the induction of cytochrome P450 3A4 by taxane anticancer drugs, docetaxel and paclitaxel, assessed employing primary human hepatocytes. Cancer Chemother Pharmacol 54:219–229. https://doi.org/10.1007/s00280-004-0799-9 CrossRefPubMed

53.

Harmsen S, Meijerman I, Beijnen JH, Schellens JHM (2009) Nuclear receptor-mediated induction of cytochrome P450 3A4 by anticancer drugs: a key role for the pregnane X receptor. Cancer Chemother Pharmacol 64:35–43. https://doi.org/10.1007/s00280-008-0842-3 CrossRefPubMed

54.

Bièche I, Narjoz C, Asselah T et al (2007) Reverse transcriptase-PCR quantification of mRNA levels from cytochrome (CYP)1, CYP2 and CYP3 families in 22 different human tissues. Pharmacogenet Genomics 17:731–742. https://doi.org/10.1097/FPC.0b013e32810f2e58 CrossRefPubMed

55.

Patterson LH, Murray GI (2002) Tumour cytochrome P450 and drug activation. CurrPharmDes 8:1335–1347. https://doi.org/10.2174/1381612023394502 CrossRef

56.

El-Rayes BF, Ali S, Heilbrun LK et al (2003) Cytochrome p450 and glutathione transferase expression in human breast cancer. Clin Cancer Res 9:1705–1709PubMed

57.

Murray GI, Taylor MC, McFadyen MCE et al (1997) Tumor-specific expression of cytochrome P450 CYP1B1. Cancer Res 57:3026–3031. https://doi.org/10.1016/j.neuint.2010.10.017 CrossRefPubMed

58.

Finnström N, Bjelfman C, Söderström TG et al (2001) Detection of cytochrome P450 mRNA transcripts in prostate samples by RT-PCR. Eur J Clin Investig 31:880–886. https://doi.org/10.1046/j.1365-2362.2001.00893.x CrossRef

59.

Mclemore TL, Adelberg S, Liu MC et al (1990) Expression of CYP1A1 gene in patients with lung cancer: evidence for cigarette smoke-induced gene expression in normal lung tissue and for altered gene regulation in primary pulmonary carcinomas. J Natl Cancer Inst 82:1333–1339. https://doi.org/10.1093/jnci/82.16.1333 CrossRefPubMed

60.

Yager JD, Davidson NE (2006) Estrogen carcinogenesis in breast cancer. N Engl J Med 354:270–282. https://doi.org/10.1056/NEJMra050776 CrossRefPubMed

61.

Tsuchiya Y, Nakajima M, Yokoi T (2005) Cytochrome P450-mediated metabolism of estrogens and its regulation in human. Cancer Lett 227:115–124. https://doi.org/10.1016/j.canlet.2004.10.007 CrossRefPubMed

62.

Huang Z, Fasco MJ, Figge HL et al (1996) Expression of cytochromes P450 in human breast tissue and tumors. Drug Metab Dispos 24:899–905PubMed

63.

Hellmold H, Rylander T, Magnusson M et al (1998) Characterization of cytochrome P450 enzymes in human breast tissue from reduction mammaplasties. J Clin Endocrinol Metab 83:886–895. https://doi.org/10.1210/jcem.83.3.4647 CrossRefPubMed

64.

Iscan M, Klaavuniemi T, Coban T et al (2001) The expression of cytochrome P450 enzymes in human breast tumours and normal breast tissue. Breast Cancer Res Treat 70:47–54. https://doi.org/10.1023/A:1012526406741 CrossRefPubMed

65.

Vaclavikova R, Hubackova M, Stribrna-Sarmanova J et al (2007) RNA expression of cytochrome P450 in breast cancer patients. Anticancer Res 27:4443–4450PubMed

66.

Murray GI, Weaver RJ, Paterson PJ et al (1993) Expression of xenobiotic metabolizing enzymes in breast cancer. J Pathol 169:347–353. https://doi.org/10.1002/path.1711690312 CrossRefPubMed

67.

Yokose T, Doy M, Taniguchi T et al (1999) Immunohistochemical study of cytochrome P450 2C and 3A in human non-neoplastic and neoplastic tissues. Virchows Arch 434:401–411. https://doi.org/10.1007/s004280050359 CrossRefPubMed

68.

Albin N, Mathieu MC, Massaad L et al (1993) Main drug-metabolizing enzyme systems in human breast tumors and peritumoral tissues. Cancer Res 53:3541–3546PubMed

69.

Floriano-Sanchez E, Rodriguez NC, Bandala C, Coballase-Urrutia E (2014) CYP3A4 expression in breast cancer and its association with risk factors in Mexican women. Asian Pac J Cancer Prev 15:3805–3809. https://doi.org/10.7314/APJCP.2014.15.8.3805 CrossRefPubMed

70.

Haas S, Pierl C, Harth V et al (2006) Expression of xenobiotic and steroid hormone metabolizing enzymes in human breast carcinomas. Int J Cancer 119:1785–1791. https://doi.org/10.1002/ijc.21915 CrossRefPubMed

71.

Schmidt R, Baumann F, Knüpfer H et al (2004) CYP3A4, CYP2C9 and CYP2B6 expression and ifosfamide turnover in breast cancer tissue microsomes. Br J Cancer 90:911–916. https://doi.org/10.1038/sj.bjc.6601492 CrossRefPubMedPubMedCentral

72.

Knüpfer H, Schmidt R, Stanitz D et al (2004) CYP2C and IL-6 expression in breast cancer. Breast 13:28–34. https://doi.org/10.1016/j.breast.2003.07.002 CrossRefPubMed

73.

Schmidt R, Baumann F, Hanschmann H et al (2001) Gender difference in ifosfamide metabolism by human liver microsomes. Eur J Drug Metab Pharmacokinet 26:193–200. https://doi.org/10.1007/BF03190396 CrossRefPubMed

74.

Koch I, Weil R, Wolbold R et al (2002) Interindividual variability and tissue-specificity in the expression of cytochrome P450 3a mRNA. Drug Metab Dispos 30:1108–1114. https://doi.org/10.1124/dmd.30.10.1108 CrossRefPubMed

75.

Mitsiades N, Sung CC, Schultz N et al (2012) Distinct patterns of dysregulated expression of enzymes involved in androgen synthesis and metabolism in metastatic prostate cancer tumors. Cancer Res 72:6142–6152. https://doi.org/10.1158/0008-5472.CAN-12-1335 CrossRefPubMedPubMedCentral

76.

Leskelä S, Honrado E, Montero-Conde C et al (2007) Cytochrome P450 3A5 is highly expressed in normal prostate cells but absent in prostate cancer. Endocr Relat Cancer 14:645–654. https://doi.org/10.1677/ERC-07-0078 CrossRefPubMed

77.

Moilanen AM, Hakkola J, Vaarala MH et al (2007) Characterization of androgen-regulated expression of CYP3A5 in human prostate. Carcinogenesis 28:916–921. https://doi.org/10.1093/carcin/bgl222 CrossRefPubMed

78.

Blanco JG, Edick MJ, Hancock ML et al (2002) Genetic polymorphisms in CYP3A5, CYP3A4 and NQO1 in children who developed therapy-related myeloid malignancies. Pharmacogenetics 12:605–611. https://doi.org/10.1097/00008571-200211000-00004 CrossRefPubMed

79.

Murray GI, Taylor VE, McKay JA et al (1995) The immunohistochemical localization of drug-metabolizing enzymes in prostate cancer. J Pathol 177:147–152. https://doi.org/10.1002/path.1711770208 CrossRefPubMed

80.

Di Paolo OA, Teitel CH, Nowell S et al (2005) Expression of cytochromes P450 and glutathione S-transferases in human prostate, and the potential for activation of heterocyclic amine carcinogens via acetyl-CoA-, PAPS- and ATP-dependent pathways. Int J Cancer 117:8–13. https://doi.org/10.1002/ijc.21152 CrossRefPubMed

81.

Fujimura T, Takahashi S, Urano T et al (2009) Expression of cytochrome P450 3A4 and its clinical significance in human prostate cancer. Urology 74:391–397. https://doi.org/10.1016/j.urology.2009.02.033 CrossRefPubMed

82.

Loukola A, Chadha M, Penn SG et al (2004) Comprehensive evaluation of the association between prostate cancer and genotypes/haplotypes in CYP17A1, CYP3A4 and SRD5A2. Eur J Hum Genet 12:321–332. https://doi.org/10.1038/sj.ejhg.5201101 CrossRefPubMed

83.

Plummer SJ, Conti DV, Paris PL et al (2003) CYP3A4 and CYP3A5 genotypes, haplotypes, and risk of prostate cancer. Cancer Epidemiol Biomarkers Prev 12:928–932PubMed

84.

Macé K, Bowman ED, Vautravers P et al (1998) Characterisation of xenobiotic-metabolising enzyme expression in human bronchial mucosa and peripheral lung tissues. Eur J Cancer 34:914–920. https://doi.org/10.1016/S0959-8049(98)00034-3 CrossRefPubMed

85.

Nakajima T, Elovaara E, Gonzalez F et al (2005) Styrene metabolism by cDNA-expressed human hepatic and pulmonary cytochromes P450. Chem Res Toxicol 7:891–896. https://doi.org/10.1021/tx00042a026 CrossRef

86.

Kivistö KT, Fritz P, Linder A et al (1995) Immunohistochemical localization of cytochrome P450 3A in human pulmonary carcinomas and normal bronchial tissue. Histochem Cell Biol 103:25–29CrossRefPubMed

87.

Kivistö KT, Griese EU, Fritz P et al (1996) Expression of cytochrome P 450 3A enzymes in human lung: a combined RT-PCR and immunohistochemical analysis of normal tissue and lung tumours. Naunyn Schmiedebergs Arch Pharmacol 353:207–212. https://doi.org/10.1007/BF00168759 CrossRefPubMed

88.

Anttila S, Hukkanen J, Hakkola J et al (1997) Expression and localization of CYP3A4 and CYP3A5 in human lung. Am J Respir Cell Mol Biol 16:242–249. https://doi.org/10.1165/ajrcmb.16.3.9070608 CrossRefPubMed

89.

Qixing M, Juqing X, Yajing W et al (2017) The expression levels of CYP3A4 and CYP3A5 serve as potential prognostic biomarkers in lung adenocarcinoma. Tumor Biol. https://doi.org/10.1177/1010428317698340 CrossRef

90.

Fujitaka K, Oguri T, Isobe T et al (2001) Induction of cytochrome P450 3A4 by docetaxel in peripheral mononuclear cells and its expression in lung cancer. Cancer Chemother Pharmacol 48:42–46. https://doi.org/10.1007/s002800100291 CrossRefPubMed

91.

Klose TS, Blaisdell JA, Goldstein JA (1999) Gene structure of CYP2C8 and extrahepatic distribution of the human CYP2Cs. J Biochem Mol Toxicol 13:289–295. https://doi.org/10.1002/(SICI)1099-0461(1999)13:6%3c289:AID-JBT1%3e3.0.CO;2-N CrossRefPubMed

92.

Rodriguez AC, Blanchard Z, Maurer KA, Gertz J (2019) Estrogen signaling in endometrial cancer: a key oncogenic pathway with several open questions. Horm Cancer 10:51–63. https://doi.org/10.1007/s12672-019-0358-9 CrossRefPubMedPubMedCentral

93.

Schuetz JD, Kauma S, Guzelian PS (1993) Identification of the fetal liver cytochrome CYP3A7 in human endometrium and placenta. J Clin Investig 92:1018–1024. https://doi.org/10.1172/JCI116607 CrossRefPubMedPubMedCentral

94.

Hukkanen J, Mäntylä M, Kangas L et al (1998) Expression of cytochrome P450 genes encoding enzymes active in the metabolism of tamoxifen in human uterine endometrium. Pharmacol Toxicol 82:93–97. https://doi.org/10.1111/j.1600-0773.1998.tb01404.x CrossRefPubMed

95.

Sarkar MA, Vadlamuri V, Ghosh S, Glover DD (2003) Expression and cyclic variability of CYP3A4 and CYP3A7 isoforms in human endometrium and cervix during the menstrual cycle. Drug Metab Dispos 31:1–6. https://doi.org/10.1124/dmd.31.1.1 CrossRefPubMed

96.

Ho SM (2003) Estrogen, progesterone and epithelial ovarian cancer. Reprod Biol Endocrinol. https://doi.org/10.1186/1477-7827-1-73 CrossRefPubMedPubMedCentral

97.

DeLoia JA, Zamboni WC, Jones JM et al (2008) Expression and activity of taxane-metabolizing enzymes in ovarian tumors. Gynecol Oncol 108:355–360. https://doi.org/10.1016/j.ygyno.2007.10.029 CrossRefPubMed

98.

Downie D, McFadyen MCE, Rooney PH et al (2005) Profiling cytochrome P450 expression in ovarian cancer: identification of prognostic markers. Clin Cancer Res 11:7369–7375. https://doi.org/10.1158/1078-0432.CCR-05-0466 CrossRefPubMed

99.

Ikezoe T, Hisatake Y, Takeuchi T et al (2004) HIV-1 protease inhibitor, ritonavir: a potent inhibitor of CYP3A4, enhanced the anticancer effects of docetaxel in androgen-independent prostate cancer cells in vitro and in vivo. Cancer Res 64:7426–7431. https://doi.org/10.1158/0008-5472.CAN-03-2677 CrossRefPubMed

100.

Li W-J, Zhong S-L, Wu Y-J et al (2013) Systematic expression analysis of genes related to multidrug-resistance in isogenic docetaxel- and adriamycin-resistant breast cancer cell lines. Mol Biol Rep 40:6143–6150. https://doi.org/10.1007/s11033-013-2725-x CrossRefPubMed

101.

Miyoshi Y, Ando A, Takamura Y et al (2002) Prediction of response to docetaxel by CYP3A4 mRNA expression in breast cancer tissues. Int J Cancer 97:129–132. https://doi.org/10.1002/ijc.1568 CrossRefPubMed

102.

Miyoshi Y, Taguchi T, Kim SJ et al (2005) Prediction of response to docetaxel by immunohistochemical analysis of CYP3A4 expression in human breast cancers. Breast Cancer 12:11–15. https://doi.org/10.2325/jbcs.12.11 CrossRefPubMed

103.

Sakurai K, Enomoto K, Matsuo S et al (2011) CYP3A4 expression to predict treatment response to docetaxel for metastasis and recurrence of primary breast cancer. Surg Today 41:674–679. https://doi.org/10.1007/s00595-009-4328-7 CrossRefPubMed

104.

Eagling VA, Back DJ, Barry MG (1997) Differential inhibition of cytochrome P450 isoforms by the protease inhibitors, ritonavir, saquinavir and indinavir. Br J Pharmacol 44:190–194. https://doi.org/10.1046/j.1365-2125.1997.00644 CrossRef

105.

Sevrioukova IF, Poulos TL (2010) Structure and mechanism of the complex between cytochrome P4503A4 and ritonavir. Proc Natl Acad Sci 107:18422–18427. https://doi.org/10.1073/pnas.1010693107 CrossRefPubMedPubMedCentral

106.

Hull MW, Montaner JSG (2011) Ritonavir-boosted protease inhibitors in HIV therapy. 2:375–388. https://doi.org/10.3109/07853890.2011.572905 CrossRef

107.

Ramsden D, Zhou J, Tweedie DJ (2015) Determination of a degradation constant for CYP3A4 by direct suppression of mRNA in a novel human hepatocyte model, HepatoPac. Drug Metab Dispos 43:1307–1315. https://doi.org/10.1124/dmd.115.065326 CrossRefPubMed

108.

Rock BM, Hengel SM, Rock DA et al (2014) Characterization of ritonavir-mediated inactivation of cytochrome P450 3A4. Mol Pharmacol 86:665–674. https://doi.org/10.1124/mol.114.094862 CrossRefPubMed

109.

Yu H, Hendrikx JJMA, Rottenberg S et al (2016) Development of a tumour growth inhibition model to elucidate the effects of ritonavir on intratumoural metabolism and anti-tumour effect of docetaxel in a mouse model for hereditary breast cancer. AAPS J 18:362–371. https://doi.org/10.1208/s12248-015-9838-1 CrossRefPubMed

110.

Rudek MA, Chang CY, Steadman K et al (2014) Combination antiretroviral therapy (cART) component ritonavir significantly alters docetaxel exposure. Cancer Chemother Pharmacol 73:729–736. https://doi.org/10.1007/s00280-014-2399-7 CrossRefPubMedPubMedCentral

111.

Hendrikx JJMA, Lagas JS, Wagenaar E et al (2014) Oral co-administration of elacridar and ritonavir enhances plasma levels of oral paclitaxel and docetaxel without affecting relative brain accumulation. Br J Cancer 110:2669–2676. https://doi.org/10.1038/bjc.2014.222 CrossRefPubMedPubMedCentral

112.

Hendrikx JJMA, Lagas JS, Song JY et al (2016) Ritonavir inhibits intratumoral docetaxel metabolism and enhances docetaxel antitumor activity in an immunocompetent mouse breast cancer model. Int J Cancer 138:758–769. https://doi.org/10.1002/ijc.29812 CrossRefPubMed

113.

Suh J, Payvandi F, Edelstein L (2002) Mechanisms of constitutive NF-κB activation in human prostate cancer cells. Prostate 52:183–200. https://doi.org/10.1002/pros.10082 CrossRefPubMed

114.

Yang Y, Ikezoe T, Nishioka C et al (2006) NFV, an HIV-1 protease inhibitor, induces growth arrest, reduced Akt signalling, apoptosis and docetaxel sensitisation in NSCLC cell lines. Br J Cancer 95:1653–1662. https://doi.org/10.1038/sj.bjc.6603435 CrossRefPubMedPubMedCentral

115.

Wendel HG, Stanchina D, Fridman JS et al (2004) Survival signalling by Akt and eIF4E in oncogenesis and cancer therapy. Nature 428:332–337. https://doi.org/10.1038/nature02369 CrossRefPubMed

116.

Dey G, Bharti R, Das AK et al (2017) Resensitization of Akt induced docetaxel resistance in breast cancer by ‘Iturin A’ a lipopeptide molecule from marine bacteria Bacillus megaterium. Sci Rep. https://doi.org/10.1038/s41598-017-17652-z CrossRefPubMedPubMedCentral

117.

Vinod BS, Nair HH, Vijayakurup V et al (2015) Resveratrol chemosensitizes HER-2-overexpressing breast cancer cells to docetaxel chemoresistance by inhibiting docetaxel-mediated activation of HER-2–Akt axis. Cell Death Discov 1:15061. https://doi.org/10.1038/cddiscovery.2015.61 CrossRefPubMedPubMedCentral

118.

Srirangam A, Mitra R, Wang M et al (2006) Effects of HIV protease inhibitor ritonavir on Akt-regulated cell proliferation in breast cancer. Clin Cancer Res 12:1883–1896. https://doi.org/10.1158/1078-0432.CCR-05-1167 CrossRefPubMedPubMedCentral

119.

Kumar S, Bryant CS, Chamala S et al (2009) Ritonavir blocks AKT signaling, activates apoptosis and inhibits migration and invasion in ovarian cancer cells. Mol Cancer. https://doi.org/10.1186/1476-4598-8-26 CrossRefPubMedPubMedCentral

120.

de Weger VA, Stuurman FE, Hendrikx JJMA et al (2017) A dose-escalation study of bi-daily once weekly oral docetaxel either as ModraDoc001 or ModraDoc006 combined with ritonavir. Eur J Cancer 86:217–225. https://doi.org/10.1016/j.ejca.2017.09.010 CrossRefPubMed

121.

de Weger VA, Stuurman FE, Mergui-Roelvink M et al (2016) A phase I dose-escalation trial of bi-daily (BID) weekly oral docetaxel as ModraDoc006 in combination with ritonavir. Ann Oncol 27:vi130. https://doi.org/10.1093/annonc/mdw368.42 CrossRef

122.

De Weger VA, Stuurman FE, Koolen SLW, et al (2019) A phase I dose escalation study of once weekly oral administration of docetaxel as ModraDoc001 capsule or ModraDoc006 tablet in combination with ritonavir. Clin Cancer Res. https://doi.org/10.1158/1078-0432.CCR-17-2299 CrossRefPubMed

123.

Gills JJ, Lopiccolo J, Tsurutani J et al (2007) Nelfinavir, a lead HIV protease inhibitor, is a broad-spectrum, anticancer agent that induces endoplasmic reticulum stress, autophagy, and apoptosis in vitro and in vivo anticancer agent that induces endoplasmic reticulum stress, autophagy, and Apo. Clin Cancer Res 13:5183–5195. https://doi.org/10.1158/1078-0432.CCR-07-0161 CrossRefPubMed

124.

AbbVie BV (2019) Norvir, INN-ritonavir-summary of product characteristics. https://www.ema.europa.eu/en/documents/product-information/norvir-epar-product-information_en.pdf. Accessed 20 Apr 2019

125.

Marzolini C, Gibbons S, Khoo S, Back D (2016) Cobicistat versus ritonavir boosting and differences in the drug-drug interaction profiles with co-medications. J Antimicrob Chemother 71:1755–1758. https://doi.org/10.1093/jac/dkw032 CrossRefPubMed

Title: Cytochrome P450 3A4, 3A5, and 2C8 expression in breast, prostate, lung, endometrial, and ovarian tumors: relevance for resistance to taxanes
Authors: Maarten van Eijk
René J. Boosman
Alfred H. Schinkel
Alwin D. R. Huitema
Jos H. Beijnen
Publication date: 01-09-2019
Publisher: Springer Berlin Heidelberg
Keyword: Ritonavir
Published in: Cancer Chemotherapy and Pharmacology / Issue 3/2019
Print ISSN: 0344-5704
Electronic ISSN: 1432-0843
DOI: https://doi.org/10.1007/s00280-019-03905-3

Webinar | 19-02-2024 | 17:30 (CET)

Keynote webinar | Spotlight on antibody–drug conjugates in cancer

Watch now

Antibody–drug conjugates (ADCs) are novel agents that have shown promise across multiple tumor types. Explore the current landscape of ADCs in breast and lung cancer with our experts, and gain insights into the mechanism of action, key clinical trials data, existing challenges, and future directions.

Dr. Véronique Diéras

Prof. Fabrice Barlesi

Developed by: Springer Medicine

Keynote webinar | Spotlight on medication adherence

Springer Medicine

Abstract

Please log in to get access to this content

Other articles of this Issue 3/2019

Genistein combined with FOLFOX or FOLFOX–Bevacizumab for the treatment of metastatic colorectal cancer: phase I/II pilot study

Assessment of the effect of erdafitinib on cardiac safety: analysis of ECGs and exposure–QTc in patients with advanced or refractory solid tumors

Electrophysiologic evaluation of facial nerve functions after oxaliplatin treatment

A high AR:ERα or PDEF:ERα ratio predicts a sub-optimal response to tamoxifen therapy in ERα-positive breast cancer

The efficacy and safety of nab paclitaxel plus gemcitabine in elderly patients over 75 years with unresectable pancreatic cancer compared with younger patients

A phase 1b, multicenter, open-label, dose-finding study of eribulin in combination with carboplatin in advanced solid tumors and non-small cell lung cancer

Keynote webinar | Spotlight on antibody–drug conjugates in cancer