Natural Compounds as Protease Inhibitors in Therapeutic Focus on Cancer Therapy

References

1. BeynonR.J. BondJ.S. Proteolytic Enzymes: A Practical Approach.LondonOxford University Press200110.1093/oso/9780199636631.001.0001
   [Google Scholar]
2. López-OtínC. MatrisianL.M. Emerging roles of proteases in tumour suppression.Nat. Rev. Cancer200771080080810.1038/nrc2228 17851543
   [Google Scholar]
3. Proteases: Multifunctional enzymes in life and disease. Lo´ pez-Otín, C.; Judith, S.B., Eds.; The J Biol. Chem.2008283453043330437
   [Google Scholar]
4. ChakrabortiS. ChakrabortiT. DhallaN.S. Eds.; Advances in Biochemistry in health and disease, proteases in human diseases.Springer Nature201310.1007/978‑1‑4614‑9233‑7
   [Google Scholar]
5. García-LorenzoM. SjödinA. JanssonS. FunkC. Protease gene families in Populus and Arabidopsis.BMC Plant Biol.2006613010.1186/1471‑2229‑6‑30 17181860
   [Google Scholar]
6. VoshavarC. Protease inhibitors for the treatment of HIV/AIDS: Recent advances and future challenges.Curr. Top. Med. Chem.201919181571159810.2174/1568026619666190619115243 31237209
   [Google Scholar]
7. AngD. KendallR. AtamianH. Virtual and in vitro screening of natural products identifies indole and benzene derivatives as inhibitors of SARS-CoV-2 Main Protease (Mpro).Biology202312451910.3390/biology12040519 37106720
   [Google Scholar]
8. WadanambiP.M. JayathilakaN. SeneviratneK.N. A computational study of carbazole alkaloids from Murraya koenigii as potential SARS-CoV-2 main protease inhibitors.Appl. Biochem. Biotechnol.2023195157359610.1007/s12010‑022‑04138‑6 36107386
   [Google Scholar]
9. RakashS. RanaF. RafiqS. MasoodA. AminS. Role of proteases in cancer: A review.Biotechnol. Mol. Biol. Rev.2012749010110.5897/BMBR11.027
   [Google Scholar]
10. VeltriC.A. Proteases: Nature’s destroyers and the drugs that stop them.Pharm. Pharmacol. Int. J.20152611110.15406/ppij.2015.02.00044
    [Google Scholar]
11. Quintero-FabiánS. ArreolaR. Becerril-VillanuevaE. Torres-RomeroJ.C. Arana-ArgáezV. Lara-RiegosJ. Ramírez-CamachoM.A. Alvarez-SánchezM.E. Role of matrix metalloproteinases in angiogenesis and cancer.Front. Oncol.20199137010.3389/fonc.2019.01370 31921634
    [Google Scholar]
12. TagirasaR. YooE. Role of serine proteases at the tumor-stroma interface.Front. Immunol.20221383241810.3389/fimmu.2022.832418 35222418
    [Google Scholar]
13. SarkarS. BhattacharjeeP. BhadraK. DNA binding and apoptotic induction ability of harmalol in HepG2: Biophysical and biochemical approaches.Chem. Biol. Interact.201625814215210.1016/j.cbi.2016.08.024 27590872
    [Google Scholar]
14. BhattacharjeeP. SarkarS. GhoshT. BhadraK. Therapeutic potential of harmaline, a novel alkaloid, against cervical cancer cells in vitro: Apoptotic induction and DNA interaction study.J. Appl. Biol. Biotechnol.20186418
    [Google Scholar]
15. SarkarS. TrebediP. BhadraK. Structure-activity insights of harmine targeting DNA, ROS inducing cytotoxicity with PARP mediated apoptosis against cervical cancer, anti-biofilm formation and in vivo therapeutic study.J. Biomol. Struct. Dyn.202240135880590210.1080/07391102.2021.1874533 33480316
    [Google Scholar]
16. LiY.Y. BaoY.L. SongZ.B. SunL.G. WuP. ZhangY. FanC. HuangY.X. WuY. YuC.L. SunY. ZhengL.H. WangG.N. LiY.X. The threonine protease activity of testes-specific protease 50 (TSP50) is essential for its function in cell proliferation.PLoS One201275e3503010.1371/journal.pone.0035030 22574111
    [Google Scholar]
17. UenoT. ElmbergerG. WeaverT.E. ToiM. LinderS. The aspartic protease napsin A suppresses tumor growth independent of its catalytic activity.Lab. Invest.200888325626310.1038/labinvest.3700718 18195689
    [Google Scholar]
18. DudaniJ.S. WarrenA.D. BhatiaS.N. Harnessing protease activity to Improve cancer care.Annu. Rev. Cancer Biol.20182135337610.1146/annurev‑cancerbio‑030617‑050549
    [Google Scholar]
19. OlsonO.C. JoyceJ.A. Cysteine cathepsin proteases: regulators of cancer progression and therapeutic response.Nat. Rev. Cancer2015151271272910.1038/nrc4027 26597527
    [Google Scholar]
20. KessenbrockK. PlaksV. WerbZ. Matrix metalloproteinases: regulators of the tumor microenvironment.Cell20101411526710.1016/j.cell.2010.03.015 20371345
    [Google Scholar]
21. Barreira da SilvaR. LairdM.E. YatimN. FietteL. IngersollM.A. AlbertM.L. Dipeptidylpeptidase 4 inhibition enhances lymphocyte trafficking, improving both naturally occurring tumor immunity and immunotherapy.Nat. Immunol.201516885085810.1038/ni.3201 26075911
    [Google Scholar]
22. TehreemM. MaimoonaQ. AsimurR. MohamadT. NaveedA. AbdelhamidE. Exploiting proteases for cancer theranostic through molecular imaging and drug delivery.Int. J. Pharm.2020587119712
    [Google Scholar]
23. TrezzaA. CicaloniV. PettiniF. SpigaO. Potential roles of protease inhibitors in anticancer therapy.Cancer-Leading Proteases.Elsevier2020134910.1016/B978‑0‑12‑818168‑3.00002‑4
    [Google Scholar]
24. TurkB. Targeting proteases: successes, failures and future prospects.Nat. Rev. Drug Discov.20065978579910.1038/nrd2092 16955069
    [Google Scholar]
25. AhmadB. BatoolM. AinQ. KimM.S. ChoiS. Exploring the binding mechanism of PF-07321332 SARS-CoV-2 protease inhibitor through molecular dynamics and binding free energy simulations.Int. J. Mol. Sci.20212217912410.3390/ijms22179124 34502033
    [Google Scholar]
26. GillsJ.J. A Lead HIV protease inhibitor, is a broad-spectrum, anticancer agent that induces endoplasmic reticulum stress, autophagy, and apoptosis in vitro and in vivo.Clin. Cancer Res.2007131751835194
    [Google Scholar]
27. RudzińskaM. DagliogluC. SavvateevaL.V. KaciF.N. AntoineR. ZamyatninA.A.Jr ZamyatninA.A.Jr Current status and perspectives of protease inhibitors and their combination with nanosized drug delivery systems for targeted cancer therapy.Drug Des. Devel. Ther.20211592010.2147/DDDT.S285852 33442233
    [Google Scholar]
28. RudzińskaM. ParodiA. SoondS.M. VinarovA.Z. KorolevD.O. MorozovA.O. DagliogluC. TutarY. ZamyatninA.A.Jr The role of cysteine cathepsins in cancer progression and drug resistance.Int. J. Mol. Sci.20192014360210.3390/ijms20143602 31340550
    [Google Scholar]
29. PetushkovaA.I. ZamyatninA.A.Jr Redox-mediated post-translational modifications of proteolytic enzymes and their role in protease functioning.Biomolecules202010465010.3390/biom10040650 32340246
    [Google Scholar]
30. WHO. Guidelines for the assessment of herbal medicines.GenevaWorld Health Organization1991
    [Google Scholar]
31. GahtoriR. TripathiA.H. KumariA. NegiN. PaliwalA. TripathiP. JoshiP. RaiR.C. UpadhyayS.K. Anticancer plant-derivatives: deciphering their oncopreventive and therapeutic potential in molecular terms.Fut. J. Pharmac. Sci.2023911410.1186/s43094‑023‑00465‑5
    [Google Scholar]
32. BhadraK. Handbook of smart materials, technologies, and devices.Applications of Industry 4.0.ChamSpringer202310.1007/978‑3‑030‑58675‑1
    [Google Scholar]
33. CarboneD. De FrancoM. PecoraroC. BassaniD. PavanM. CascioferroS. ParrinoB. CirrincioneG. Dall’AcquaS. SutS. MoroS. GandinV. DianaP. Structural manipulations of marine natural products inspire a new library of 3-amino-1,2,4-triazine PDK inhibitors endowed with antitumor activity in pancreatic ductal adenocarcinoma.Mar. Drugs202321528810.3390/md21050288 37233482
    [Google Scholar]
34. NanY. SuH. ZhouB. LiuS. The function of natural compounds in important anticancer mechanisms.Front. Oncol.202312104988810.3389/fonc.2022.1049888 36686745
    [Google Scholar]
35. LuoY. YinS. LuJ. ZhouS. ShaoY. BaoX. WangT. QiuY. YuH. Tumor microenvironment: A prospective target of natural alkaloids for cancer treatment.Cancer Cell Int.202121138610.1186/s12935‑021‑02085‑6 34284780
    [Google Scholar]
36. NamanC.B. BenatrehinaP.A. KinghornA.D. OhioT. Pharmaceuticals, plant drugs.2nd edNew YorkElsevier201710.1016/B978‑0‑12‑394807‑6.00163‑5
    [Google Scholar]
37. MukeshwarP. MousumiD. ShobitG. SurenderK.C. Phytomedicine: An ancient approach turning into future potential source of therapeutics.J. Pharmacogn. Phytother.2011322737
    [Google Scholar]
38. Chunarkar-PatilP. KaleemM. MishraR. RayS. AhmadA. VermaD. BhayyeS. DubeyR. SinghH. KumarS. Anticancer drug discovery based on natural products: From computational approaches to clinical studies.Biomedicines202412120110.3390/biomedicines12010201 38255306
    [Google Scholar]
39. LiX. YuN. LiJ. BaiJ. DingD. TangQ. XuH. Novel “carrier-free” nanofiber codelivery systems with the synergistic antitumor effect of paclitaxel and tetrandrine through the enhancement of mitochondrial apoptosis.ACS Appl. Mater. Interfaces2020129100961010610.1021/acsami.9b17363 32027119
    [Google Scholar]
40. LaskarP. SomaniS. CampbellS.J. MullinM. KeatingP. TateR.J. IrvingC. LeungH.Y. DufèsC. Camptothecin-based dendrimersomes for gene delivery and redox-responsive drug delivery to cancer cells.Nanoscale20191142200582007110.1039/C9NR07254C 31612185
    [Google Scholar]
41. IshiiN. ArakiK. YokoboriT. HagiwaraK. GantumurD. YamanakaT. HandaT. TsukagoshiM. IgarashiT. WatanabeA. KuboN. HarimotoN. MasamuneA. UmezawaK. KuwanoH. ShirabeK. Conophylline suppresses pancreatic cancer desmoplasia and cancer‐promoting cytokines produced by cancer‐associated fibroblasts.Cancer Sci.2019110133434410.1111/cas.13847 30353606
    [Google Scholar]
42. AntropowA.H. XuK. BuchsbaumR.J. MovassaghiM. Synthesis and evaluation of agelastatin derivatives as potent modulators for cancer invasion and metastasis.J. Org. Chem.201782157720773110.1021/acs.joc.7b01162 28696693
    [Google Scholar]
43. WengT.Y. WuH.F. LiC.Y. HungY.H. ChangY.W. ChenY.L. HsuH.P. ChenY.H. WangC.Y. ChangJ.Y. LaiM.D. Homoharringtonine induced immune alteration for an efcient anti-tumor response in mouse models of non-small cell lung adenocarcinoma expressing Kras mutation.Sci. Rep.201881821610.1038/s41598‑018‑26454‑w 29844447
    [Google Scholar]
44. HockB.D. MacPhersonS.A. McKenzieJ.L. Idelalisib and caffeine reduce suppression of T cell responses mediated by activated chronic lymphocytic leukemia cells.PLoS One2017123e017285810.1371/journal.pone.0172858 28257435
    [Google Scholar]
45. ChoiD.W. JungS.Y. ShonD.H. ShinH.S. PiperineAmeliorates Trimellitic anhydride-induced atopic dermatitis-like symptoms by suppressing Th2-mediated immune responses via inhibition of STAT6 phosphorylation.Molecules2020259218610.3390/molecules25092186 32392825
    [Google Scholar]
46. LiuH. ZouM. LiP. WangH. LinX. YeJ. Oxymatrine mediated maturation of dendritic cells leads to activation of FOXP3+/CD4+ Treg cells and reversal of cisplatin resistance in lung cancer cells.Mol. Med. Rep.20191954081409010.3892/mmr.2019.10064 30896871
    [Google Scholar]
47. GuoG. ShiF. ZhuJ. ShaoY. GongW. ZhouG. WuH. SheJ. ShiW. Piperine, a functional food alkaloid, exhibits inhibitory potential against TNBS-induced colitis via the inhibition of IκB-α/NF-κB and induces tight junction protein (claudin-1, occludin, and ZO-1) signaling pathway in experimental mice.Hum. Exp. Toxicol.202039447749110.1177/0960327119892042 31835924
    [Google Scholar]
48. YaoM. FanX. YuanB. TakagiN. LiuS. HanX. RenJ. LiuJ. Berberine inhibits NLRP3 inflammasome pathway in human triple-negative breast cancer MDA-MB-231 cell.BMC Complement. Altern. Med.201919121610.1186/s12906‑019‑2615‑4 31412862
    [Google Scholar]
49. ZhuL. HuangS. LiJ. ChenJ. YaoY. LiL. GuoH. XiangX. DengJ. XionJ. Sophoridine inhibits lung cancer cell growth and enhances cisplatin sensitivity through activation of the p53 and Hippo signaling pathways.Gene202074214455610.1016/j.gene.2020.144556
    [Google Scholar]
50. ZhaoL. WangL. DiS.N. XuQ. RenQ.C. ChenS.Z. HuangN. JiaD. ShenX.F. Steroidal alkaloid solanine A from Solanum nigrum Linn. Exhibits anti-inflammatory activity in lipopolysaccharide/interferon gamma activated murine macrophages and animal models of inflammation.Pharmacotherapy2018105606615
    [Google Scholar]
51. PangL. LiuC.Y. GongG.H. QuanZ.S. Synthesis, in vitro and in vivo biological evaluation of novel lappaconitine derivatives as potential anti-inflammatory agents.Acta Pharm. Sin. B202010462864510.1016/j.apsb.2019.09.002
    [Google Scholar]
52. WangX. GaoJ.Q. OuyangX. WangJ. SunX. LvY. Mesenchymal stem cells loaded with paclitaxel–poly(lactic-co-glycolic acid) nanoparticles for glioma-targeting therapy.Int. J. Nanomedicine2018135231524810.2147/IJN.S167142 30237710
    [Google Scholar]
53. LiH. GuoL. JieS. LiuW. ZhuJ. DuW. FanL. WangX. FuB. HuangS. Berberine inhibits SDF-1-induced AML cells and leukemic stem cells migration via regulation of SDF-1 level in bone marrow stromal cells.Biomed. Pharmacother.200862957357810.1016/j.biopha.2008.08.003 18805669
    [Google Scholar]
54. ChakravarthyD. MuñozA.R. SuA. HwangR.F. KepplerB.R. ChanD.E. HalffG. GhoshR. KumarA.P. Palmatine suppresses glutamine-mediated interaction between pancreatic cancer and stellate cells through simultaneous inhibition of survivin and COL1A1.Cancer Lett.201841910311510.1016/j.canlet.2018.01.057 29414301
    [Google Scholar]
55. JieS. LiH. TianY. GuoD. ZhuJ. GaoS. JiangL. Berberine inhibits angiogenic potential of Hep G2 cell line through VEGF down‐regulation in vitro.J. Gastroenterol. Hepatol.201126117918510.1111/j.1440‑1746.2010.06389.x 21175812
    [Google Scholar]
56. WenZ. HuangC. XuY. XiaoY. TangL. DaiJ. SunH. ChenB. ZhouM. α-Solanine inhibits vascular endothelial growth factor expression by down-regulating the ERK1/2-HIF-1α and STAT3 signaling pathways.Eur. J. Pharmacol.2016771939810.1016/j.ejphar.2015.12.020 26688571
    [Google Scholar]
57. ZhangH. RenY. TangX. WangK. LiuY. ZhangL. LiX. LiuP. ZhaoC. HeJ. Vascular normalization induced by sinomenine hydrochloride results in suppressed mammary tumor growth and metastasis.Sci. Rep.201551888810.1038/srep08888 25749075
    [Google Scholar]
58. GuoX.X. LiX.P. ZhouP. LiD.Y. LyuX.T. ChenY. LyuY.W. TianK. YuanD.Z. RanJ.H. ChenD.L. JiangR. LiJ. Evodiamine induces apoptosis in SMMC-7721 and HepG2 cells by suppressing NOD1 signal pathway.Int. J. Mol. Sci.20181911341910.3390/ijms19113419 30384473
    [Google Scholar]
59. BräutigamJ. BischoffI. SchürmannC. BuchmannG. EpahJ. FuchsS. HeissE. BrandesR.P. FürstR. Narciclasine inhibits angiogenic processes by activation of Rho kinase and by downregulation of the VEGF receptor 2.J. Mol. Cell. Cardiol.20191359710810.1016/j.yjmcc.2019.08.001 31381906
    [Google Scholar]
60. YuanZ. LiangZ. YiJ. ChenX. LiR. WuY. WuJ. SunZ. Protective effect of koumine, an alkaloid from gelsemium sempervirens, on injury induced by H2O2 in IPEC-J2 cells.Int. J. Mol. Sci.201920375410.3390/ijms20030754 30754638
    [Google Scholar]
61. YangM.H. JungS.H. SethiG. AhnK.S. Pleiotropic pharmacological actions of capsazepine, a synthetic analogue of capsaicin, against various cancers and infammatory diseases.Molecules201924599510.3390/molecules24050995 30871017
    [Google Scholar]
62. XuZ. ZhangF. BaiC. YaoC. ZhongH. ZouC. ChenX. Sophoridine induces apoptosis and S phase arrest via ROS-dependent JNK and ERK activation in human pancreatic cancer cells.J. Exp. Clin. Cancer Res.201736112410.1186/s13046‑017‑0590‑5 28893319
    [Google Scholar]
63. BhattacharjeeP. SarkarP. BhadraK. Evaluation of chemotherapeutic role of harmaline: In vitro cytotoxicity targeting nucleic acids.J. Asian Nat. Prod. Res.202426451953310.1080/10286020.2023.2251116
    [Google Scholar]
64. AwaleS. DibweD.F. BalachandranC. FayezS. FeineisD. LombeB.K. BringmannG. Ancistrolikokine E3, a 5,8′-coupled naphthylisoquinoline alkaloid, eliminates the tolerance of cancer cells to nutrition starvation by inhibition of the Akt/mTOR/autophagy signaling pathway.J. Nat. Prod.201881102282229110.1021/acs.jnatprod.8b00733 30303002
    [Google Scholar]
65. SongL. WangY. ZhenY. LiD. HeX. YangH. ZhangH. LiuQ. Piperine inhibits colorectal cancer migration and invasion by regulating STAT3/Snail-mediated epithelial–mesenchymal transition.Biotechnol. Lett.202042102049205810.1007/s10529‑020‑02923‑z 32500474
    [Google Scholar]
66. SuQ. FanM. WangJ. UllahA. GhauriM.A. DaiB. ZhanY. ZhangD. ZhangY. Sanguinarine inhibits epithelial–mesenchymal transition via targeting HIF-1α/TGF-β feed-forward loop in hepatocellular carcinoma.Cell Death Dis.2019101293910.1038/s41419‑019‑2173‑1 31819036
    [Google Scholar]
67. HuangC. WangX. QiF. PangZ. Berberine inhibits epithelial-mesenchymal transition and promotes apoptosis of tumour-associated fibroblast-induced colonic epithelial cells through regulation of TGF-β signalling.J. Cell Commun. Signal.2020141536610.1007/s12079‑019‑00525‑7 31399854
    [Google Scholar]
68. DengG. ZengS. MaJ. ZhangY. QuY. HanY. YinL. CaiC. GuoC. ShenH. The anti-tumor activities of Neferine on cell invasion and oxaliplatin sensitivity regulated by EMT via Snail signaling in hepatocellular carcinoma.Sci. Rep.2017714161610.1038/srep41616 28134289
    [Google Scholar]
69. JiangY. JiaoY. LiuY. ZhangM. WangZ. LiY. LiT. ZhaoX. WangD. Sinomenine hydrochloride inhibits the metastasis of human glioblastoma cells by suppressing the expression of matrix metalloproteinase-2/-9 and reversing the endogenous and exogenous epithelial mesenchymal transition.Int. J. Mol. Sci.201819384410.3390/ijms19030844 29538296
    [Google Scholar]
70. KimJ.H. ChoE.B. LeeJ. JungO. RyuB.J. KimS.H. ChoJ.Y. RyouC. LeeS.Y. Emetine inhibits migration and invasion of human non-small-cell lung cancer cells via regulation of ERK and p38 signaling pathways.Chem. Biol. Interact.2015242253310.1016/j.cbi.2015.08.014 26332055
    [Google Scholar]
71. RahimN.F.C. HussinY. AzizM.N.M. MohamadN.E. YeapS.K. MasarudinM.J. AbdullahR. AkhtarM.N. AlitheenN.B. Cytotoxicity and apoptosis effects of curcumin analogue (2E, 6E)-2, 6-bis (2,3-dimethoxybenzylidine) cyclohexanone (DMCH) on human colon cancer cells HT29 and SW620 in vitro.Molecules2021265126110.3390/molecules26051261 33652694
    [Google Scholar]
72. FerhiS. SantanielloS. ZerizerS. CrucianiS. FaddaA. SannaD. DoreA. MaioliM. D’hallewinG. Total phenols from grape leaves counteract cell proliferation and modulate apoptosis related gene expression in MCF-7 and HepG2 human cancer cell lines.Molecules201924361210.3390/molecules24030612 30744145
    [Google Scholar]
73. YuY. ZhangC. LiuL. LiX. Hepatic arterial administration of ginsenoside Rg3 and transcatheter arterial embolization for the treatment of VX2 liver carcinomas.Exp. Ther. Med.20135376176610.3892/etm.2012.873 23404440
    [Google Scholar]
74. WuL. WangL. TianX. ZhangJ. FengH. Germacrone exerts anti-cancer effects on gastric cancer through induction of cell cycle arrest and promotion of apoptosis.BMC Complement. Med. Ther.20202012110.1186/s12906‑019‑2810‑3
    [Google Scholar]
75. LauT.S. ChanL.K.Y. ManG.C.W. WongC.H. LeeJ.H.S. YimS.F. CheungT.H. McNeishI.A. KwongJ. Paclitaxel induces immunogenic cell death in ovarian cancer via TLR4/IKK2/SNARE dependent Exocytosis Paclitaxel induces ICD via TLR4 in cancer cells.Cancer Immunol. Res.2020881099111110.1158/2326‑6066.CIR‑19‑0616 32354736
    [Google Scholar]
76. SunY. ZhouQ.M. LuY.Y. ZhangH. ChenQ.L. ZhaoM. SuS.B. Resveratrol inhibits the migration and metastasis of MDA-MB-231 human breast cancer by reversing TGF-b1-induced epithelial-mesenchymal transition.Molecules2019246113110.3390/molecules24061131 30901941
    [Google Scholar]
77. WangY. RenX. DengC. YangL. YanE. GuoT. LiY. XuM.X. Mechanism of the inhibition of the STAT3 signaling pathway by EGCG.Oncol. Rep.20133062691269610.3892/or.2013.2743 24065300
    [Google Scholar]
78. GhasemiF. ShafieeM. BanikazemiZ. PourhanifehM.H. KhanbabaeiH. ShamshirianA. Amiri MoghadamS. ArefNezhad, R.; Sahebkar, A.; Avan, A.; Mirzaei, H. Curcumin inhibits NF-kB and Wnt/β-catenin pathways in cervical cancer cells.Pathol. Res. Pract.20192151015255610.1016/j.prp.2019.152556 31358480
    [Google Scholar]
79. FanH. JiangC. ZhongB. ShengJ. ChenT. ChenQ. LiJ. ZhaoH. Matrine ameliorates colorectal cancer in rats via inhibition of HMGB1 signalling and downregulation of IL-6, TNF-a, and HMGB1.J. Immunol. Res.201820181810.1155/2018/5408324 29546074
    [Google Scholar]
80. ZhaoL. ZhangC. Berberine inhibits MDA-MB-231 cells by attenuating their inflammatory responses.BioMed Res. Int.202020201610.1155/2020/3617514 32258115
    [Google Scholar]
81. PrabhuK.S. BhatA.A. SiveenK.S. KuttikrishnanS. RazaS.S. RaheedT. JochebethA. KhanA.Q. ChawdheryM.Z. HarisM. KulinskiM. DermimeS. SteinhoffM. UddinS. Sanguinarine mediated apoptosis in non-small cell lung cancer via generation of reactive oxygen species and suppression of JAK/STAT pathway.Biomed. Pharmacother.202114411235810.1016/j.biopha.2021.112358 34794241
    [Google Scholar]
82. ZhangW. GouP. DupretJ.M. ChomienneC. Rodrigues-LimaF. Etoposide, an anticancer drug involved in therapy-related secondary leukemia: Enzymes at play.Transl. Oncol.2021141010116910.1016/j.tranon.2021.101169 34243013
    [Google Scholar]
83. SyedR. RaniR. Sabeena; Masoodi, T.A.; Shafi, G.; Alharbi, K. Functional analysis and structure determination of alkaline protease from Aspergillus flavus.Bioinformation20128417518010.6026/97320630008175 22419836
    [Google Scholar]
84. KentS. MarshallG.R. WlodawerA. Determining the 3D structure of HIV-1 protease.Science20002885471159010.1126/science.288.5471.1590a 10858137
    [Google Scholar]
85. OverallC.M. López-OtínC. Strategies for MMP inhibition in cancer: innovations for the post-trial era.Nat. Rev. Cancer20022965767210.1038/nrc884 12209155
    [Google Scholar]
86. YanC. BoydD.D. Regulation of matrix metalloproteinase gene expression.J. Cell. Physiol.20072111192610.1002/jcp.20948 17167774
    [Google Scholar]
87. RiedlS.J. SalvesenG.S. The apoptosome: signalling platform of cell death.Nat. Rev. Mol. Cell Biol.20078540541310.1038/nrm2153 17377525
    [Google Scholar]
88. VersteegH.H. RufW. Emerging insights in tissue factor-dependent signaling events.Semin. Thromb. Hemost.200632102403210.1055/s‑2006‑933337 16479459
    [Google Scholar]
89. FuX. ParksW.C. HeineckeJ.W. RETRACTED: Activation and silencing of matrix metalloproteinases.Semin. Cell Dev. Biol.200819121310.1016/j.semcdb.2007.06.005 17689277
    [Google Scholar]
90. BodeW. HuberR. Structural basis of the endoproteinase–protein inhibitor interaction.Biochim. Biophys. Acta Protein Struct. Mol. Enzymol.200014771-224125210.1016/S0167‑4838(99)00276‑9 10708861
    [Google Scholar]
91. HashemS. AliT.A. AkhtarS. NisarS. SageenaG. AliS. Al-MannaiS. TherachiyilL. MirR. ElfakiI. MirM.M. JamalF. MasoodiT. UddinS. SinghM. HarisM. MachaM. BhatA.A. Targeting cancer signaling pathways by natural products: Exploring promising anti-cancer agents.Biomed. Pharmacother.202215011305410.1016/j.biopha.2022.113054 35658225
    [Google Scholar]
92. HedstromL. Serine protease mechanism and specificity.Chem. Rev.2002102124501452410.1021/cr000033x 12475199
    [Google Scholar]
93. JedinakA. MaliarT. Inhibitors of proteases as anticancer drugs.Neoplasma2005523185192 15875078
    [Google Scholar]
94. Al-AwadhiF. SalvadorL. LawB. PaulV. LueschH. Kempopeptin C, a novel marine-derived serine protease inhibitor targeting invasive breast cancer.Mar. Drugs201715929030710.3390/md15090290 28926939
    [Google Scholar]
95. Al-AwadhiF.H. LueschH. Targeting eukaryotic proteases for natural products-based drug development.Nat. Prod. Rep.202037682786010.1039/C9NP00060G 32519686
    [Google Scholar]
96. KuoC.L. ChiC.W. LiuT.Y. Modulation of apoptosis by berberine through inhibition of cyclooxygenase-2 and Mcl-1 expression in oral cancer cells. in vivo 2005191247252 15796182
    [Google Scholar]
97. KimJ.S. OhD. YimM.J. ParkJ.J. KangK.R. ChoI.A. MoonS.M. OhJ.S. YouJ.S. KimC.S. KimD.K. LeeS.Y. LeeG.J. Im, H.J.; Kim, S.G. Berberine induces FasL-related apoptosis through p38 activation in KB human oral cancer cells.Oncol. Rep.20153341775178210.3892/or.2015.3768 25634589
    [Google Scholar]
98. JagetiaG.C. Anticancer potential of natural isoquinoline alkaloid berberine.J. Explorat. Res. Pharmacol.20216310513310.14218/JERP.2021.00005
    [Google Scholar]
99. LeeS.L. DicksonR.B. LinC.Y. Activation of hepatocyte growth factor and urokinase/plasminogen activator by matriptase, an epithelial membrane serine protease.J. Biol. Chem.200027547367203672510.1074/jbc.M007802200 10962009
    [Google Scholar]
100. BhattA.S. Erdjument-BromageH. TempstP. CraikC.S. MoasserM.M. Adhesion signaling by a novel mitotic substrate of src kinases.Oncogene200524345333534310.1038/sj.onc.1208582 16007225
     [Google Scholar]
101. UhlandK. Matriptase and its putative role in cancer.Cell. Mol. Life Sci.200663242968297810.1007/s00018‑006‑6298‑x 17131055
     [Google Scholar]
102. ListK. Matriptase: A culprit in cancer?Future Oncol.2009519710410.2217/14796694.5.1.97 19243302
     [Google Scholar]
103. LiP. JiangS. LeeS.L. LinC.Y. JohnsonM.D. DicksonR.B. MichejdaC.J. RollerP.P. Design and synthesis of novel and potent inhibitors of the type II transmembrane serine protease, matriptase, based upon the sunflower trypsin inhibitor-1.J. Med. Chem.200750245976598310.1021/jm0704898 17985858
     [Google Scholar]
104. LawM.E. CorsinoP.E. JahnS.C. DavisB.J. ChenS. PatelB. PhamK. LuJ. SheppardB. NørgaardP. HongJ. HigginsP. KimJ-S. LueschH. LawB.K. Glucocorticoids and histone deacetylase inhibitors cooperate to block the invasiveness of basal-like breast cancer cells through novel mechanisms.Oncogene201332101316132910.1038/onc.2012.138 22543582
     [Google Scholar]
105. NguyenH.H. AronchikI. BrarG.A. NguyenD.H.H. BjeldanesL.F. FirestoneG.L. The dietary phytochemical indole-3-carbinol is a natural elastase enzymatic inhibitor that disrupts cyclin E protein processing.Proc. Natl. Acad. Sci.200810550197501975510.1073/pnas.0806581105 19064917
     [Google Scholar]
106. AronchikI. BjeldanesL.F. FirestoneG.L. Direct inhibition of elastase activity by indole-3-carbinol triggers a CD40-TRAF regulatory cascade that disrupts NF-kappaB transcriptional activity in human breast cancer cells.Cancer Res.201070124961497110.1158/0008‑5472.CAN‑09‑3349 20530686
     [Google Scholar]
107. CrocettiL. QuinnM.T. SchepetkinI.A. GiovannoniM.P. A patenting perspective on human neutrophil elastase (HNE) inhibitors (2014-2018) and their therapeutic applications.Expert Opin. Ther. Pat.201929755557810.1080/13543776.2019.1630379 31204543
     [Google Scholar]
108. AkizukiM. FukutomiT. TakasugiM. TakahashiS. SatoT. HaraoM. MizumotoT. YamashitaJ. Prognostic significance of immunoreactive neutrophil elastase in human breast cancer: long-term follow-up results in 313 patients.Neoplasia20079326026410.1593/neo.06808 17401466
     [Google Scholar]
109. SatoT. TakahashiS. MizumotoT. HaraoM. AkizukiM. TakasugiM. FukutomiT. YamashitaJ. Neutrophil elastase and cancer.Surg. Oncol.200615421722210.1016/j.suronc.2007.01.003 17320378
     [Google Scholar]
110. MittendorfE.A. AlatrashG. QiaoN. WuY. SukhumalchandraP. St JohnL.S. PhilipsA.V. XiaoH. ZhangM. RuisaardK. Clise-DwyerK. LuS. MolldremJ.J. Breast cancer cell uptake of the inflammatory mediator neutrophil elastase triggers an anticancer adaptive immune response.Cancer Res.201272133153316210.1158/0008‑5472.CAN‑11‑4135 22564522
     [Google Scholar]
111. NawaM. OsadaS. MorimitsuK. NonakaK. FutamuraM. KawaguchiY. YoshidaK. Growth effect of neutrophil elastase on breast cancer: favorable action of sivelestat and application to anti-HER2 therapy.Anticancer Res.20123211319 22213283
     [Google Scholar]
112. PorterD.C. ZhangN. DanesC. McGahrenM.J. HarwellR.M. FarukiS. KeyomarsiK. Tumor-specific proteolytic processing of cyclin E generates hyperactive lower-molecular-weight forms.Mol. Cell. Biol.200121186254626910.1128/MCB.21.18.6254‑6269.2001 11509668
     [Google Scholar]
113. AkliS. KeyomarsiK. Cyclin E and its low molecular weight forms in human cancer and as targets for cancer therapy. Cancer Biol. Ther.20032sup1)(1374610.4161/cbt.201 14508079
     [Google Scholar]
114. HuntK.K. KeyomarsiK. Cyclin E as a prognostic and predictive marker in breast cancer.Semin. Cancer Biol.200515431932610.1016/j.semcancer.2005.04.007 16043362
     [Google Scholar]
115. LoebK.R. ChenX. Too much cleavage of cyclin E promotes breast tumorigenesis.PLoS Genet.201283e100262310.1371/journal.pgen.1002623 22479209
     [Google Scholar]
116. HessS. EngelmannH. A novel function of CD40: Induction of cell death in transformed cells.J. Exp. Med.1996183115916710.1084/jem.183.1.159 8551219
     [Google Scholar]
117. WingettD.G. VestalR.E. ForcierK. HadjokasN. NielsonC.P. CD40 is functionally expressed on human breast carcinomas: Variable inducibility by cytokines and enhancement of Fas-mediated apoptosis.Breast Cancer Res. Treat.1998501273610.1023/A:1006012607452 9802617
     [Google Scholar]
118. HiranoA. LongoD.L. TaubD.D. FerrisD.K. YoungL.S. EliopoulosA.G. AgathanggelouA. CullenN. MacartneyJ. FanslowW.C. MurphyW.J. Inhibition of human breast carcinoma growth by a soluble recombinant human CD40 ligand.Blood19999392999300710.1182/blood.V93.9.2999 10216096
     [Google Scholar]
119. Al-AwadhiF.H. PaulV.J. LueschH. Structural diversity and anticancer activity of marine‐derived elastase inhibitors: Key features and mechanisms mediating the antimetastatic effects in invasive breast cancer.ChemBioChem201819881582510.1002/cbic.201700627 29405541
     [Google Scholar]
120. DiD. ChenL. WangL. SunP. LiuY. XuZ. JuJ. Downregulation of human intercellular adhesion molecule-1 attenuates the metastatic ability in human breast cancer cell lines.Oncol. Rep.20163531541154810.3892/or.2016.4543 26751847
     [Google Scholar]
121. Gitlin-DomagalskaA. MaciejewskaA. DębowskiD. Bowman-birk inhibitors: Insights into family of multifunctional proteins and peptides with potential therapeutical applications.Pharmaceuticals2020131242110.3390/ph13120421 33255583
     [Google Scholar]
122. SrikanthS. ChenZ. Plant protease inhibitors in therapeutics-focus on cancer therapy.Front. Pharmacol.2016747048910.3389/fphar.2016.00470 28008315
     [Google Scholar]
123. ArmstrongW.B. KennedyA.R. WanX.S. AtibaJ. McLarenC.E. MeyskensF.L. Jr Single-dose administration of Bowman-Birk inhibitor concentrate in patients with oral leukoplakia.Cancer Epidemiol. Biomarkers Prev.2000914347 10667462
     [Google Scholar]
124. ManasanchE.E. OrlowskiR.Z. Proteasome inhibitors in cancer therapy.Nat. Rev. Clin. Oncol.201714741743310.1038/nrclinonc.2016.206 28117417
     [Google Scholar]
125. Bibo-VerdugoB. JiangZ. CaffreyC.R. O’DonoghueA.J. Targeting proteasomes in infectious organisms to combat disease.FEBS J.2017284101503151710.1111/febs.14029 28122162
     [Google Scholar]
126. Della SalaG. AgriestiF. MazzoccoliC. TataranniT. CostantinoV. PiccoliC. Clogging the ubiquitin-proteasome machinery with marine natural products: last decade update.Mar. Drugs2018161246710.3390/md16120467 30486251
     [Google Scholar]
127. HanadaM. SugawaraK. KanetaK. TodaS. NishiyamaY. TomitaK. YamamotoH. KonishiM. OkiT. Epoxomicin, a new antitumor agent of microbial origin.J. Antibiot.199245111746175210.7164/antibiotics.45.1746 1468981
     [Google Scholar]
128. MengL. MohanR. KwokB.H.B. ElofssonM. SinN. CrewsC.M. Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity.Proc. Natl. Acad. Sci.19999618104031040810.1073/pnas.96.18.10403 10468620
     [Google Scholar]
129. GrollM. HuberR. PottsB.C.M. Crystal structures of Salinosporamide A (NPI-0052) and B (NPI-0047) in complex with the 20S proteasome reveal important consequences of β-lactone ring opening and a mechanism for irreversible binding.J. Am. Chem. Soc.2006128155136514110.1021/ja058320b 16608349
     [Google Scholar]
130. MacherlaV.R. MitchellS.S. ManamR.R. ReedK.A. ChaoT.H. NicholsonB. Deyanat-YazdiG. MaiB. JensenP.R. FenicalW.F. NeuteboomS.T.C. LamK.S. PalladinoM.A. PottsB.C.M. Structure-activity relationship studies of salinosporamide A (NPI-0052), a novel marine derived proteasome inhibitor.J. Med. Chem.200548113684368710.1021/jm048995+ 15916417
     [Google Scholar]
131. ManamR.R. McArthurK.A. ChaoT.H. WeissJ. AliJ.A. PalombellaV.J. GrollM. LloydG.K. PalladinoM.A. NeuteboomS.T.C. MacherlaV.R. PottsB.C.M. Leaving groups prolong the duration of 20S proteasome inhibition and enhance the potency of salinosporamides.J. Med. Chem.200851216711672410.1021/jm800548b 18939815
     [Google Scholar]
132. PottsB.C. LamK.S. Generating a generation of proteasome inhibitors: from microbial fermentation to total synthesis of salinosporamide a (marizomib) and other salinosporamides.Mar. Drugs20108483588010.3390/md8040835 20479958
     [Google Scholar]
133. MaL. DiaoA. Marizomib, a potent second generation proteasome inhibitor from natural origin.Anticancer. Agents Med. Chem.201515329830610.2174/1871520614666141114202606 25403165
     [Google Scholar]
134. PereiraR.B. EvdokimovN.M. LefrancF. ValentãoP. KornienkoA. PereiraD.M. AndradeP.B. GomesN.G.M. Marine-derived anticancer agents: Clinical benefits, innovative mechanisms, and new targets.Mar. Drugs201917632910.3390/md17060329 31159480
     [Google Scholar]
135. PereiraA.R. KaleA.J. FenleyA.T. ByrumT. DebonsiH.M. GilsonM.K. ValerioteF.A. MooreB.S. GerwickW.H. The carmaphycins: new proteasome inhibitors exhibiting an α,β-epoxyketone warhead from a marine cyanobacterium.ChemBioChem201213681081710.1002/cbic.201200007 22383253
     [Google Scholar]
136. RawatA. RoyM. JyotiA. KaushikS. VermaK. SrivastavaV.K. Cysteine proteases: Battling pathogenic parasitic protozoans with omnipresent enzymes.Microbiol. Res.202124912678410.1016/j.micres.2021.126784 33989978
     [Google Scholar]
137. VermaS. DixitR. PandeyK.C. Cysteine proteases: Modes of activation and future prospects as pharmacological targets.Front. Pharmacol.2016710710.3389/fphar.2016.00107 27199750
     [Google Scholar]
138. TurkV. StokaV. VasiljevaO. RenkoM. SunT. TurkB. TurkD. Cysteine cathepsins: From structure, function and regulation to new frontiers.Biochim. Biophys. Acta. Proteins Proteomics201218241688810.1016/j.bbapap.2011.10.002
     [Google Scholar]
139. SudhanD.R. SiemannD.W. CathepsinL. Cathepsin L targeting in cancer treatment.Pharmacol. Ther.201515510511610.1016/j.pharmthera.2015.08.007 26299995
     [Google Scholar]
140. FujishimaA. ImaiY. NomuraT. FujisawaY. YamamotoY. SugawaraT. The crystal structure of human cathepsin L complexed with E‐64.FEBS Lett.19974071475010.1016/S0014‑5793(97)00216‑0 9141479
     [Google Scholar]
141. OnoY. SaidoT.C. SorimachiH. Calpain research for drug discovery: Challenges and potential nature reviews drug discovery.Nat. Publis. Gr.20161129854876
     [Google Scholar]
142. SaatmanK.E. CreedJ. RaghupathiR. Calpain as a therapeutic target in traumatic brain injury.Neurotherapeutics201071314210.1016/j.nurt.2009.11.002 20129495
     [Google Scholar]
143. LeloupL. WellsA. Calpains as potential anti-cancer targets.Expert Opin. Ther. Targets201115330932310.1517/14728222.2011.553611 21244345
     [Google Scholar]
144. PotzB.A. AbidM.R. SellkeF.W. Role of calpain in pathogenesis of human disease processes.J. Nat. Sci.201629e218 27747292
     [Google Scholar]
145. BarnardD.L. HubbardV.D. BurtonJ. SmeeD.F. MorreyJ.D. OttoM.J. SidwellR.W. Inhibition of severe acute respiratory syndrome-associated coronavirus (SARSCoV) by calpain inhibitors and β-D-N4-hydroxycytidine.Antivir. Chem. Chemother.2004151152210.1177/095632020401500102 15074711
     [Google Scholar]
146. SchneiderM. AckermannK. StuartM. WexC. ProtzerU. SchätzlH.M. GilchS. Severe acute respiratory syndrome coronavirus replication is severely impaired by MG132 due to proteasome-independent inhibition of M-calpain.J. Virol.20128618101121012210.1128/JVI.01001‑12 22787216
     [Google Scholar]
147. TaoriK. LiuY. PaulV.J. LueschH. Combinatorial strategies by marine cyanobacteria: symplostatin 4, an antimitotic natural dolastatin 10/15 hybrid that synergizes with the coproduced HDAC inhibitor largazole.ChemBioChem200910101634163910.1002/cbic.200900192 19514039
     [Google Scholar]
148. LiuS. GaoX. ZhangL. QinS. WeiM. LiuN. ZhaoR. LiB. MengY. LinG. LuC. LiuX. XieM. LiuT. ZhouH. QiM. YangG. YangC. A novel Anti-Cancer Stem Cells compound optimized from the natural symplostatin 4 scaffold inhibits Wnt/β-catenin signaling pathway.Eur. J. Med. Chem.2018156214210.1016/j.ejmech.2018.06.046 30006166
     [Google Scholar]
149. WhiteJ.B. BeckfordJ. YadegaryniaS. NgoN. LialiutskaT. d’AlarcaoM. Some natural flavonoids are competitive inhibitors of caspase-1, -3, and -7 despite their cellular toxicity.Food Chem.201213141453145910.1016/j.foodchem.2011.10.026 22140296
     [Google Scholar]
150. YadavP. YadavR. JainS. VaidyaA. Caspase‐3: A primary target for natural and synthetic compounds for cancer therapy.Chem. Biol. Drug Des.202198114416510.1111/cbdd.13860 33963665
     [Google Scholar]
151. Al-AwadhiF.H. LawB.K. PaulV.J. LueschH. Grassystatins D–F, potent aspartic protease inhibitors from marine cyanobacteria as potential antimetastatic agents targeting invasive breast cancer.J. Nat. Prod.201780112969298610.1021/acs.jnatprod.7b00551 29087712
     [Google Scholar]
152. Cerdà-CostaN. Xavier Gomis-RüthF. Architecture and function of metallopeptidase catalytic domains.Protein Sci.201423212314410.1002/pro.2400 24596965
     [Google Scholar]
153. KumarG.B. NairB.G. PerryJ.J.P. MartinD.B.C. Recent insights into natural product inhibitors of matrix metalloproteinases.MedChemComm201910122024203710.1039/C9MD00165D 32904148
     [Google Scholar]
154. GuptaP. Natural products as inhibitors of matrix metalloproteinases.Nat. Prod. Chem. Res.201641110.4172/2329‑6836.1000e114
     [Google Scholar]
155. CathcartJ. Pulkoski-GrossA. CaoJ. Targeting matrix metalloproteinases in cancer: Bringing new life to old ideas genes and diseases.Chongq. Med. Univ.2015312634
     [Google Scholar]
156. MannelloF. TontiG. PapaS. Matrix metalloproteinase inhibitors as anticancer therapeutics.Curr. Cancer Drug Targets20055428529810.2174/1568009054064615 15975049
     [Google Scholar]
157. PengP.L. HsiehY.S. WangC.J. HsuJ.L. ChouF.P. Inhibitory effect of berberine on the invasion of human lung cancer cells via decreased productions of urokinase-plasminogen activator and matrix metalloproteinase-2.Toxicol. Appl. Pharmacol.2006214181510.1016/j.taap.2005.11.010 16387334
     [Google Scholar]
158. JamesM.A. FuH. LiuY. ChenD.R. YouM. Dietary administration of berberine or Phellodendron amurense extract inhibits cell cycle progression and lung tumorigenesis.Mol. Carcinog.20115011710.1002/mc.20690 21061266
     [Google Scholar]
159. LingX.H. WangS.K. HuangY.H. HuangM.J. DuhC.Y. A high-content screening assay for the discovery of novel proteasome inhibitors from formosan soft corals.Mar. Drugs2018161039510.3390/md16100395 30347865
     [Google Scholar]
160. MajumdarD.D. Recent updates on pharmaceutical potential of plant protease inhibitors.Int. J. Med. Pharm. Sci.20133101120
     [Google Scholar]
161. ClementeA. ArquesM.C. Bowman-Birk inhibitors from legumes as colorectal chemopreventive agents.World J. Gastroenterol.20142030103051031510.3748/wjg.v20.i30.10305 25132747
     [Google Scholar]
162. MorrisonK.C. HergenrotherP.J. Natural products as starting points for the synthesis of complex and diverse compounds.Nat. Prod. Rep.201431161410.1039/C3NP70063A 24219884
     [Google Scholar]
163. HashmiM.A. AndreassendS.K. KeyzersR.A. LeinM. Accurate prediction of the optical rotation and NMR properties for highly flexible chiral natural products.Phys. Chem. Chem. Phys.20161835245062451010.1039/C6CP04828E 27539138
     [Google Scholar]
164. AdelusiT.I. OyedeleA.Q.K. BoyenleI.D. OgunlanaA.T. AdeyemiR.O. UkachiC.D. IdrisM.O. OlaobaO.T. AdedotunI.O. KolawoleO.E. XiaoxingY. Abdul-HammedM. Molecular modeling in drug discovery.Informatics in Medicine Unlocked20222910088010.1016/j.imu.2022.100880
     [Google Scholar]
165. BaxiS.M. BeallR. YangJ. MackeyT.K. A multidisciplinary review of the policy, intellectual property rights, and international trade environment for access and affordability to essential cancer medications.Global. Health20191515710.1186/s12992‑019‑0497‑3 31533850
     [Google Scholar]
166. LiuG.H. ChenT. ZhangX. MaX.L. ShiH.S. Small molecule inhibitors targeting the cancers.MedComm202234e18110.1002/mco2.181 36254250
     [Google Scholar]
167. BedardP.L. HymanD.M. DavidsM.S. SiuL.L. Small molecules, big impact: 20 years of targeted therapy in oncology.Lancet2020395102291078108810.1016/S0140‑6736(20)30164‑1 32222192
     [Google Scholar]