Generic placeholder image

Current Signal Transduction Therapy

Editor-in-Chief

ISSN (Print): 1574-3624
ISSN (Online): 2212-389X

Review Article

A Review on Inhibitory Action of Tyrosine Kinase Inhibitors (TKI) by Curbing the ATP-Tyrosine Kinase Interactions

Author(s): Vanktesh Kumar* and Navjot Kaur

Volume 18, Issue 2, 2023

Published on: 15 May, 2023

Article ID: e040423215444 Pages: 8

DOI: 10.2174/1574362418666230404133417

Price: $65

Abstract

According to the latest data, the cancer prevalence fraction has surged to the highest number. This is why cancer has become a prominent disease that must be seen as a serious issue. Inhibitory action and ideas become prominent and necessary because of the rising death incidence daily. The simplifying idea of inhibition of cancer is targeting the complex that forms between the tyrosine kinase and ATP, which ultimately provides a clear way. Tyrosine kinase is a proteinaceous enzyme responsible for various cellular events like cell development, growth, and division. But these functions are performed by the activated tyrosine kinase, and the activation occurs by phosphorylation using ATP. The transfer of the phosphate group from ATP to tyrosine is known as phosphorylation. The basic idea is to enhance the competitive inhibition of the ATP-Tyrosine complex is a promising target for treating cancer. Various molecules have a substantial effect on the above-said target. This review summarizes molecules currently in any drug development or clinical trial with the same effect. This review covers most inhibitory molecules from different categories, which either directly or indirectly inhibit the Tyrosin kinase-ATP complex by incorporating.

Keywords: ATP binding, tyrosine kinase, cancer, oncology, angiogenesis, apoptosis.

Graphical Abstract
[1]
Wishart DS. Is cancer a genetic disease or a metabolic disease? EBioMedicine 2015; 2(6): 478-9.
[http://dx.doi.org/10.1016/j.ebiom.2015.05.022] [PMID: 26288805]
[2]
Lozano R. Genetic aberrations in DNA repair pathways: A cornerstone of precision oncology in prostate cancer. Br J Cancer 2020; •••: 1-12.
[PMID: 33106584]
[3]
Hu T, Yang J, Yan Y, et al. Detection of genes responsible for cetuximab sensitization in colorectal cancer cells using CRISPR-Cas9. Biosci Rep 2020; 40(10): BSR20201125.
[http://dx.doi.org/10.1042/BSR20201125] [PMID: 33048115]
[4]
Huang L, Jiang S, Shi Y, et al. Tyrosine kinase inhibitors for solid tumors in the past 20 years (2001–2020). J Hematol Oncol 2020; 13(1): 143.
[http://dx.doi.org/10.1186/s13045-020-00977-0] [PMID: 33109256]
[5]
Rassy E, Flippot R, Albiges L, et al. Tyrosine kinase inhibitors and immunotherapy combinations in renal cell carcinoma. Ther Adv Med Oncol 2020; •••: 12.
[http://dx.doi.org/10.1177/1758835920907504] [PMID: 32215057]
[6]
Farhan H. Tyrosine kinase signaling in and on the endoplasmic reticulum. Biochem Soc Trans 2020; 48(1): 199-205.
[http://dx.doi.org/10.1042/BST20190543] [PMID: 32065230]
[7]
Trenker R, Jura N. Receptor tyrosine kinase activation: From the ligand perspective. Curr Opin Cell Biol 2020; 63: 174-85.
[http://dx.doi.org/10.1016/j.ceb.2020.01.016] [PMID: 32114309]
[8]
Wintheiser GA, Silberstein PJS. Silberstein, Physiology, tyrosine kinase receptors.StatPearls. Treasure Island, FL: StatPearls Publishing 2022.
[9]
Muhlbauer N, MacDonell-Yilmaz RE, Borsuk R, et al. Mutations within the activation loop domain of FLT3 in two pediatric patients with refractory infant acute myeloid leukemia. Case Rep Oncol 2020; 13(1): 266-70.
[http://dx.doi.org/10.1159/000506194] [PMID: 32308588]
[10]
Sanoyama I, Sakurai Y, Ichinoe M, et al. Increased expression of REV7 in small cell lung carcinomas and its association with tumor cell survival and proliferation. Pathol Int 2021; 71(1): 15-23.
[http://dx.doi.org/10.1111/pin.13040] [PMID: 33112501]
[11]
Lamper AM, Fleming RH, Ladd KM, et al. A phosphorylation-regulated eIF3d translation switch mediates cellular adaptation to metabolic stress. Science 2020; 370(6518): 853-6.
[http://dx.doi.org/10.1126/science.abb0993] [PMID: 33184215]
[12]
Kazi JU, Rönnstrand L. FMS-like tyrosine kinase 3/FLT3: From basic science to clinical implications. Physiol Rev 2019; 99(3): 1433-66.
[http://dx.doi.org/10.1152/physrev.00029.2018] [PMID: 31066629]
[13]
Bose R, Holbert MA, Pickin KA, Cole PA. Protein tyrosine kinase–substrate interactions. Curr Opin Struct Biol 2006; 16(6): 668-75.
[http://dx.doi.org/10.1016/j.sbi.2006.10.012] [PMID: 17085043]
[14]
Harsh G, Keating M, Escobedo J, et al. Platelet Derived Growth Factor (PDGF) autocrine components in human tumor cell lines. J Neurooncol 1990; 8(1): 1-12.
[http://dx.doi.org/10.1007/BF00182081] [PMID: 2156959]
[15]
Attoub S, Rivat C, Rodrigues S, et al. The c-kit tyrosine kinase inhibitor STI571 for colorectal cancer therapy. Cancer Res 2002; 62(17): 4879-83.
[PMID: 12208734]
[16]
Hantschel O, Superti-Furga G. Regulation of the c-Abl and Bcr–Abl tyrosine kinases. Nat Rev Mol Cell Biol 2004; 5(1): 33-44.
[http://dx.doi.org/10.1038/nrm1280] [PMID: 14708008]
[17]
Bogoyevitch M, Fairlie D. A new paradigm for protein kinase inhibition: Blocking phosphorylation without directly targeting ATP binding. Drug Discov Today 2007; 12(15-16): 622-33.
[http://dx.doi.org/10.1016/j.drudis.2007.06.008] [PMID: 17706543]
[18]
Dohse M, Scharenberg C, Shukla S, et al. Comparison of ATP-binding cassette transporter interactions with the tyrosine kinase inhibitors imatinib, nilotinib, and dasatinib. Drug Metab Dispos 2010; 38(8): 1371-80.
[http://dx.doi.org/10.1124/dmd.109.031302] [PMID: 20423956]
[19]
Manley PW, Bold G, Brüggen J, et al. Advances in the structural biology, design and clinical development of VEGF-R kinase inhibitors for the treatment of angiogenesis. Biochim Biophys Acta Proteins Proteomics 2004; 1697(1-2): 17-27.
[http://dx.doi.org/10.1016/j.bbapap.2003.11.010] [PMID: 15023347]
[20]
Manley PW, Furet P, Bold G, et al. Anthranilic acid amides: A novel class of antiangiogenic VEGF receptor kinase inhibitors. J Med Chem 2002; 45(26): 5687-93.
[http://dx.doi.org/10.1021/jm020899q] [PMID: 12477352]
[21]
Pargellis C, Tong L, Churchill L, et al. Inhibition of p38 MAP kinase by utilizing a novel allosteric binding site. Nat Struct Biol 2002; 9(4): 268-72.
[http://dx.doi.org/10.1038/nsb770] [PMID: 11896401]
[22]
Regan J, Breitfelder S, Cirillo P, et al. Pyrazole urea-based inhibitors of p38 MAP kinase: from lead compound to clinical candidate. J Med Chem 2002; 45(14): 2994-3008.
[http://dx.doi.org/10.1021/jm020057r] [PMID: 12086485]
[23]
Regan J, Capolino A, Cirillo PF, et al. Structure-activity relationships of the p38α MAP kinase inhibitor 1-(5- tert -Butyl-2- p -tolyl-2 H -pyrazol-3-yl)-3-[4-(2-morpholin-4-yl-ethoxy)naph- thalen-1-yl]urea (BIRB 796). J Med Chem 2003; 46(22): 4676-86.
[http://dx.doi.org/10.1021/jm030121k] [PMID: 14561087]
[24]
Wan PTC, Garnett MJ, Roe SM, et al. Mechanism of activation of the RAF-ERK signaling pathway by oncogenic mutations of B-RAF. Cell 2004; 116(6): 855-67.
[http://dx.doi.org/10.1016/S0092-8674(04)00215-6] [PMID: 15035987]
[25]
Wilhelm SM, Carter C, Tang L, et al. BAY 43-9006 exhibits broad spectrum oral antitumor activity and targets the RAF/MEK/ERK pathway and receptor tyrosine kinases involved in tumor progression and angiogenesis. Cancer Res 2004; 64(19): 7099-109.
[http://dx.doi.org/10.1158/0008-5472.CAN-04-1443] [PMID: 15466206]
[26]
Adnane L, Trail PA, Taylor I, et al. Sorafenib (BAY 43-9006, Nexavar), a dual-action inhibitor that targets RAF/MEK/ERK pathway in tumor cells and tyrosine kinases VEGFR/PDGFR in tumor vasculature. Methods Enzymol 2006; 407: 597-612.
[http://dx.doi.org/10.1016/S0076-6879(05)07047-3] [PMID: 16757355]
[27]
Iacob RE, Zhang J, Gray NS, et al. Allosteric interactions between the myristate- and ATP-site of the Abl kinase. PLoS One 2011; 6(1): e15929.
[http://dx.doi.org/10.1371/journal.pone.0015929] [PMID: 21264348]
[28]
Burke JR, Pattoli MA, Gregor KR, et al. BMS-345541 is a highly selective inhibitor of I kappa B kinase that binds at an allosteric site of the enzyme and blocks NF-kappa B-dependent transcription in mice. J Biol Chem 2003; 278(3): 1450-6.
[http://dx.doi.org/10.1074/jbc.M209677200] [PMID: 12403772]
[29]
McIntyre KW, Shuster DJ, Gillooly KM, et al. A highly selective inhibitor of I?B kinase, BMS-345541, blocks both joint inflammation and destruction in collagen-induced arthritis in mice. Arthritis Rheum 2003; 48(9): 2652-9.
[http://dx.doi.org/10.1002/art.11131] [PMID: 13130486]
[30]
Herrmann O, Baumann B, de Lorenzi R, et al. IKK mediates ischemia-induced neuronal death. Nat Med 2005; 11(12): 1322-9.
[http://dx.doi.org/10.1038/nm1323] [PMID: 16286924]
[31]
Carnero A, Blanco-Aparicio C, Renner O, et al. The PTEN/PI3K/AKT signalling pathway in cancer, therapeutic implications. Curr Cancer Drug Targets 2008; 8(3): 187-98.
[http://dx.doi.org/10.2174/156800908784293659] [PMID: 18473732]
[32]
Akhtar N, Jabeen I. Pharmacoinformatic approaches to design novel inhibitors of protein kinase B pathways in cancer. Curr Cancer Drug Targets 2018; 18(9): 830-46.
[http://dx.doi.org/10.2174/1568009617666170623104540] [PMID: 28669343]
[33]
Balasuriya N, McKenna M, Liu X, et al. Phosphorylation-dependent inhibition of Akt1. Genes 2018; 9(9): 450.
[http://dx.doi.org/10.3390/genes9090450] [PMID: 30205513]
[34]
Bastian C, Quinn J, Tripathi A, et al. CK2 inhibition confers functional protection to young and aging axons against ischemia by differentially regulating the CDK5 and AKT signaling pathways. Neurobiol Dis 2019; 126: 47-61.
[http://dx.doi.org/10.1016/j.nbd.2018.05.011] [PMID: 29944965]
[35]
Budi EH, Mamai O, Hoffman S, et al. Enhanced TGF-β signaling contributes to the insulin-induced angiogenic responses of endothelial cells. iScience 2019; 11: 474-91.
[http://dx.doi.org/10.1016/j.isci.2018.12.038] [PMID: 30684493]
[36]
LoPiccolo J, Granville CA, Gills JJ, et al. Targeting Akt in cancer therapy. Anticancer Drugs 2007; 18(8): 861-74.
[http://dx.doi.org/10.1097/CAD.0b013e3280cc2c6f] [PMID: 17667591]
[37]
Li L, Zhao GD, Shi Z, et al. The Ras/Raf/MEK/ERK signaling pathway and its role in the occurrence and development of HCC. Oncol Lett 2016; 12(5): 3045-50.
[http://dx.doi.org/10.3892/ol.2016.5110] [PMID: 27899961]
[38]
Cheng Y, Tian H. Current development status of MEK inhibitors. Molecules 2017; 22(10): 1551.
[http://dx.doi.org/10.3390/molecules22101551] [PMID: 28954413]
[39]
Kumar V, Nayak SK. Homoisoflavonoids: Isolation, chemical synthesis strategies and biological activities. JPSCR Journal of Pharmaceutical Science and Clinical Research 2020; 12(8): 1046-55.
[40]
Kumar M, Singla R, Dandriyal J, et al. Coumarin derivatives as anticancer agents for lung cancer therapy: A review. Anticancer Agents Med Chem 2018; 18(7): 964-84.
[http://dx.doi.org/10.2174/1871520618666171229185926] [PMID: 29298657]
[41]
Pereira TM, Franco DP, Vitorio F, et al. Coumarin compounds in medicinal chemistry: some important examples from the last years. Curr Top Med Chem 2018; 18(2): 124-48.
[http://dx.doi.org/10.2174/1568026618666180329115523] [PMID: 29595110]
[42]
Lee CS, Lee LC, Yuan TL, et al. MAP kinase and autophagy pathways cooperate to maintain RAS mutant cancer cell survival. Proc Natl Acad Sci USA 2019; 116(10): 4508-17.
[http://dx.doi.org/10.1073/pnas.1817494116] [PMID: 30709910]
[43]
Marchetti P, Trinh A, Khamari R, et al. Melanoma metabolism contributes to the cellular responses to MAPK/ERK pathway inhibitors. Biochim Biophys Acta, Gen Subj 2018; 1862(4): 999-1005.
[http://dx.doi.org/10.1016/j.bbagen.2018.01.018] [PMID: 29413908]
[44]
Li Y, Zhang D, Yu K, et al. CMPD1 inhibited human gastric cancer cell proliferation by inducing apoptosis and G2/M cell cycle arrest. Biol Res 2018; 51(1): 11.
[http://dx.doi.org/10.1186/s40659-018-0159-6] [PMID: 29661232]
[45]
Zhang H-J. Progress of dynamin 3 in tumors. Int J Clin Exp Med 2017; 10(11): 15060-3.
[46]
Chapman MS, Miner JN. Novel mitogen-activated protein kinase kinase inhibitors. Expert Opin Investig Drugs 2011; 20(2): 209-20.
[47]
Wang C, Zhang H, Xu F, et al. Substituted 3-benzylcoumarins as allosteric MEK1 inhibitors: Design, synthesis and biological evaluation as antiviral agents. Molecules 2013; 18(5): 6057-91.
[http://dx.doi.org/10.3390/molecules18056057] [PMID: 23698055]
[48]
Uko NE, Güner OF, Barnett LMA, et al. Discovery and biological activity of computer-assisted drug designed Akt pathway inhibitors. Bioorg Med Chem Lett 2018; 28(19): 3247-50.
[http://dx.doi.org/10.1016/j.bmcl.2018.08.006] [PMID: 30143420]
[49]
Clark MJ, Miduturu C, Schmidt AG, et al. GNF-2 inhibits dengue virus by targeting Abl kinases and the viral E protein. Cell Chem Biol 2016; 23(4): 443-52.
[http://dx.doi.org/10.1016/j.chembiol.2016.03.010] [PMID: 27105280]
[50]
Rossari F, Minutolo F, Orciuolo E. Past, present, and future of Bcr-Abl inhibitors: From chemical development to clinical efficacy. J Hematol Oncol 2018; 11(1): 84.
[http://dx.doi.org/10.1186/s13045-018-0624-2] [PMID: 29925402]
[51]
Wojcik J, Lamontanara AJ, Grabe G, et al. Allosteric inhibition of Bcr-Abl kinase by high affinity monobody inhibitors directed to the Src homology 2 (SH2)-kinase interface. J Biol Chem 2016; 291(16): 8836-47.
[http://dx.doi.org/10.1074/jbc.M115.707901] [PMID: 26912659]
[52]
Wu J, Meng F, Ying Y, et al. ON012380, a putative BCR-ABL kinase inhibitor with a unique mechanism of action in imatinib-resistant cells. Leukemia 2010; 24(4): 869-72.
[http://dx.doi.org/10.1038/leu.2009.300] [PMID: 20111070]
[53]
Kirkland LO, McInnes C. Non-ATP competitive protein kinase inhibitors as anti-tumor therapeutics. Biochem Pharmacol 2009; 77(10): 1561-71.
[http://dx.doi.org/10.1016/j.bcp.2008.12.022] [PMID: 19167366]
[54]
Ďugová M. Inhibitory proteazomu. 2020.
[55]
Berus T, Markiewicz A, Kobylinska K, et al. Downregulation of Polo-like kinase-1 (PLK-1) expression is associated with poor clinical outcome in uveal melanoma patients. Folia Histochem Cytobiol 2020; 58(2): 108-16.
[http://dx.doi.org/10.5603/FHC.a2020.0017] [PMID: 32602935]
[56]
Yin Y, Yuan X, Gao H, Yang Q. Nanoformulations of small molecule protein tyrosine kinases inhibitors potentiate targeted cancer therapy. Int J Pharm 2020; 573: 118785.
[http://dx.doi.org/10.1016/j.ijpharm.2019.118785] [PMID: 31678384]
[57]
Shali H, Ahmadi M, Kafil HS, Dorosti A, Yousefi M. IGF1R and c-met as therapeutic targets for colorectal cancer. Biomed Pharmacother 2016; 82: 528-36.
[http://dx.doi.org/10.1016/j.biopha.2016.05.034] [PMID: 27470393]
[58]
Xu B, Washington AM, Domeniconi RF, et al. Protein tyrosine kinase 7 is essential for tubular morphogenesis of the Wolffian duct. Dev Biol 2016; 412(2): 219-33.
[http://dx.doi.org/10.1016/j.ydbio.2016.02.029] [PMID: 26944093]
[59]
Kim JW, Botvinnik OB, Abudayyeh O, et al. Characterizing genomic alterations in cancer by complementary functional associations. Nat Biotechnol 2016; 34(5): 539-46.
[http://dx.doi.org/10.1038/nbt.3527] [PMID: 27088724]
[60]
Moffat D, Davis P, Hutchings M, et al. 4-Pyridin-5-yl-2-(3,4,5-trimethoxyphenylamino)pyrimidines: Potent and selective inhibitors of ZAP 70. Bioorg Med Chem Lett 1999; 9(23): 3351-6.
[http://dx.doi.org/10.1016/S0960-894X(99)00615-0] [PMID: 10612598]
[61]
Hennequin LF, Thomas AP, Johnstone C, et al. Design and structure-activity relationship of a new class of potent VEGF receptor tyrosine kinase inhibitors. J Med Chem 1999; 42(26): 5369-89.
[http://dx.doi.org/10.1021/jm990345w] [PMID: 10639280]
[62]
Chikhale R, Thorat S, Choudhary RK, Gadewal N, Khedekar P. Design, synthesis and anticancer studies of novel aminobenzazolyl pyrimidines as tyrosine kinase inhibitors. Bioorg Chem 2018; 77: 84-100.
[http://dx.doi.org/10.1016/j.bioorg.2018.01.008] [PMID: 29342447]
[63]
Alexander KL, Serrano CA, Chakraborty A, et al. Modulation of glycosyltransferase ST6Gal-I in gastric cancer-derived organoids disrupts homeostatic epithelial cell turnover. J Biol Chem 2020; 295(41): 14153-63.
[http://dx.doi.org/10.1074/jbc.RA120.014887] [PMID: 32763973]
[64]
de Jong FA, Verweij J. Role of imatinib mesylate (Gleevec®/Glivec®) in gastrointestinal stromal tumors. Expert Rev Anticancer Ther 2003; 3(6): 757-66.
[http://dx.doi.org/10.1586/14737140.3.6.757] [PMID: 14686698]
[65]
Ali I, Lone M, Al-Othman Z, Al-Warthan A, Sanagi M. Heterocyclic scaffolds: Centrality in anticancer drug development. Curr Drug Targets 2015; 16(7): 711-34.
[http://dx.doi.org/10.2174/1389450116666150309115922] [PMID: 25751009]
[66]
Lang DK, Kaur R, Arora R, Saini B, Arora S. Nitrogen-containing heterocycles as anticancer agents: An overview. Anticancer Agents Med Chem 2020; 20(18): 2150-68.
[http://dx.doi.org/10.2174/1871520620666200705214917] [PMID: 32628593]
[67]
Fatima S, Agarwal SM. Structure-activity relationship study on therapeutically relevant EGFR double mutant inhibitors. Med Chem 2020; 16(1): 52-62.
[http://dx.doi.org/10.2174/1573406415666190206204853] [PMID: 30727906]
[68]
Saber AF. A facile method for preparation and evaluation of the antimicrobial efficiency of various heterocycles containing thieno[2,3-d]pyrimidine. Synth Commun 2020; 51(3): 398-409.
[69]
Singh AP, Umbarkar P, Tousif S, Lal H. Cardiotoxicity of the BCR-ABL1 tyrosine kinase inhibitors: Emphasis on ponatinib. Int J Cardiol 2020; 316: 214-21.
[http://dx.doi.org/10.1016/j.ijcard.2020.05.077] [PMID: 32470534]
[70]
Cao L. High throughput image analysis for cardiotoxicity study using human pluripotent stem cell-derived cardiomyocytes. J Cell Immunol 2020; 2(6)
[http://dx.doi.org/10.33696/immunology.2.062]
[71]
Faivre S, Delbaldo C, Vera K, et al. Safety, pharmacokinetic, and antitumor activity of SU11248, a novel oral multitarget tyrosine kinase inhibitor, in patients with cancer. J Clin Oncol 2006; 24(1): 25-35.
[http://dx.doi.org/10.1200/JCO.2005.02.2194] [PMID: 16314617]

Rights & Permissions Print Cite
© 2024 Bentham Science Publishers | Privacy Policy