Dynamics of Endocytosis and Degradation of Antibody-Drug Conjugate T-DM1 in HER2 Positive Cancer Cells

References

• VermaS, MilesD, GianniL, et al. Trastuzumab emtansine for HER2-positive advanced breast cancer. N Engl J Med. 2012;367(19):1783–1791. doi:10.1056/NEJMoa120912423020162
   PubMed Web of Science ®Google Scholar
• HurvitzSA, DirixL, KocsisJ, et al. Phase II randomized study of trastuzumab emtansine versus trastuzumab plus docetaxel in patients with human epidermal growth factor receptor 2-positive metastatic breast cancer. J Clin Oncol. 2013;31(9):1157–1163. doi:10.1200/JCO.2012.44.969423382472
   PubMed Web of Science ®Google Scholar
• CeresaBP. Spatial regulation of epidermal growth factor receptor signaling by endocytosis. Int J Mol Sci. 2012;1:72–87.
   Web of Science ®Google Scholar
• CitriA, AlroyI, LaviS, et al. Drug-induced ubiquitylation and degradation of ErbB receptor tyrosine kinases: implications for cancer therapy. EMBO J. 2002;21(10):2407–2417. doi:10.1093/emboj/21.10.240712006493
   PubMed Web of Science ®Google Scholar
• BertelsenV, StangE. The mysterious ways of ErbB2/HER2 trafficking. Membranes. 2014;4(3):424–446. doi:10.3390/membranes403042425102001
   PubMedGoogle Scholar
• HarariD, YardenY. Molecular mechanisms underlying ErbB2/HER2 action in breast cancer. Oncogene. 2000;19(53):6102–6114. doi:10.1038/sj.onc.120397311156523
   PubMed Web of Science ®Google Scholar
• HendriksBS, OpreskoLK, WileyHS, LauffenburgerD. Coregulation of epidermal growth factor receptor/human epidermal growth factor receptor 2 (HER2) levels and locations: quantitative analysis of HER2 overexpression effects. Cancer Res. 2003;5:1130–1137.
   Google Scholar
• AustinCD, De MaziereAM, PisacanePI, et al. Endocytosis and sorting of ErbB2 and the site of action of cancer therapeutics trastuzumab and geldanamycin. Mol Biol Cell. 2004;15(12):5268–5282. doi:10.1091/mbc.e04-07-059115385631
   PubMed Web of Science ®Google Scholar
• HommelgaardAM, LerdrupM, van DeursB. Association with membrane protrusions makes ErbB2 an internalization-resistant receptor. Mol Biol Cell. 2004;15(4):1557–1567. doi:10.1091/mbc.e03-08-059614742716
   PubMed Web of Science ®Google Scholar
• PustS, KlokkTI, MusaN, et al. Flotillins as regulators of ErbB2 levels in breast cancer. Oncogene. 2013;32(29):3443–3451. doi:10.1038/onc.2012.35722869152
   PubMed Web of Science ®Google Scholar
• WilliamsTM, LisantiMP. The caveolin proteins. Genome Biol. 2004;5(3):214. doi:10.1186/gb-2004-5-3-21415003112
   PubMed Web of Science ®Google Scholar
• GuptaR, ToufailyC, AnnabiB. Caveolin and cavin family members: dual roles in cancer. Biochimie. 2014;107 Pt B:188–202. doi:10.1016/j.biochi.2014.09.01025241255
   PubMed Web of Science ®Google Scholar
• LeeSW, ReimerCL, OhP, CampbellDB, SchnitzerJE. Tumor cell growth inhibition by caveolin re-expression in human breast cancer cells. Oncogene. 1998;16(11):1391–1397. doi:10.1038/sj.onc.12016619525738
   PubMed Web of Science ®Google Scholar
• SagaraY, MimoriK, YoshinagaK, et al. Clinical significance of Caveolin-1, Caveolin-2 and HER2/neu mRNA expression in human breast cancer. Br J Cancer. 2004;91(5):959–965. doi:10.1038/sj.bjc.660202915305200
   PubMed Web of Science ®Google Scholar
• ParkSS, KimJE, KimYA, KimYC, KimSW. Caveolin-1 is down-regulated and inversely correlated with HER2 and EGFR expression status in invasive ductal carcinoma of the breast. Histopathology. 2005;47(6):625–630. doi:10.1111/j.1365-2559.2005.02303.x16324201
   PubMed Web of Science ®Google Scholar
• PereiraPMR, SharmaSK, CarterLM, et al. Caveolin-1 mediates cellular distribution of HER2 and affects trastuzumab binding and therapeutic efficacy. Nat Commun. 2018;9(1):5137. doi:10.1038/s41467-018-07608-w30510281
   PubMed Web of Science ®Google Scholar
• SekharSC, KasaiT, SatohA, et al. Identification of caveolin-1 as a potential causative factor in the generation of trastuzumab resistance in breast cancer cells. J Cancer. 2013;4(5):391–401. doi:10.7150/jca.647023833684
   PubMed Web of Science ®Google Scholar
• ChungYC, ChangCM, WeiWC, et al. Metformin-induced caveolin-1 expression promotes T-DM1 drug efficacy in breast cancer cells. Sci Rep. 2018;8(1):3930. doi:10.1038/s41598-018-22250-829500444
   PubMed Web of Science ®Google Scholar
• Indira ChandranV, ManssonAS, BarbachowskaM, et al. Hypoxia attenuates trastuzumab uptake and Trastuzumab-Emtansine (T-DM1) cytotoxicity through redistribution of phosphorylated caveolin-1. Mol Cancer Res. 2020;18(4):644–656. doi:10.1158/1541-7786.MCR-19-085631900313
   PubMed Web of Science ®Google Scholar
• ChungYC, KuoJF, WeiWC, ChangKJ, ChaoWT. Caveolin-1 dependent endocytosis enhances the chemosensitivity of HER-2 positive breast cancer cells to Trastuzumab Emtansine (T-DM1). PLoS One. 2015;10(7):e0133072. doi:10.1371/journal.pone.013307226172389
   PubMed Web of Science ®Google Scholar
• KumarGA, SarkarP, JafurullaM, et al. Exploring endocytosis and intracellular trafficking of the human Serotonin(1A) receptor. Biochemistry. 2019;58(22):2628–2641. doi:10.1021/acs.biochem.9b0003330896156
   PubMed Web of Science ®Google Scholar
• Abdollahpour-AlitappehM, LotfiniaM, BagheriN, et al. Trastuzumab-monomethyl auristatin E conjugate exhibits potent cytotoxic activity in vitro against HER2-positive human breast cancer. J Cell Physiol. 2019;234(3):2693–2704. doi:10.1002/jcp.2708530246298
   PubMed Web of Science ®Google Scholar
• FedeleAO, ProudCG. Chloroquine and bafilomycin A mimic lysosomal storage disorders and impair mTORC1 signalling. Biosci Rep. 2020;4:BSR20200905.
   Web of Science ®Google Scholar
• BrowningDJ. Pharmacology of chloroquine and hydroxychloroquine. In: Hydroxychloroquine and Chloroquine Retinopathy. 2014:35–63.
   Google Scholar
• WeiX, SheG, WuT, XueC, CaoY. PEDV enters cells through clathrin-, caveolae-, and lipid raft-mediated endocytosis and traffics via the endo-/lysosome pathway. Vet Res. 2020;51(1):10. doi:10.1186/s13567-020-0739-732041637
   PubMed Web of Science ®Google Scholar
• RossinR, VersteegenRM, WuJ, et al. Chemically triggered drug release from an antibody-drug conjugate leads to potent antitumour activity in mice. Nat Commun. 2018;10(1):1484. doi:10.1038/s41467-018-03880-y
   Web of Science ®Google Scholar
• KobayashiH, ChoykePL. Near-infrared photoimmunotherapy of cancer. Acc Chem Res. 2019;52(8):2332–2339. doi:10.1021/acs.accounts.9b0027331335117
   PubMed Web of Science ®Google Scholar
• MosessonY, MillsGB, YardenY. Derailed endocytosis: an emerging feature of cancer. Nat Rev Cancer. 2008;8(11):835–850. doi:10.1038/nrc252118948996
   PubMed Web of Science ®Google Scholar
• GerberHP, KoehnFE, AbrahamRT. The antibody-drug conjugate: an enabling modality for natural product-based cancer therapeutics. Nat Prod Rep. 2013;30(5):625–639. doi:10.1039/c3np20113a23525375
   PubMed Web of Science ®Google Scholar
• YardenY, SliwkowskiMX. Untangling the ErbB signalling network. Nat Rev Mol Cell Biol. 2001;2(2):127–137. doi:10.1038/3505207311252954
   PubMed Web of Science ®Google Scholar
• HughesJB, RodlandMS, HasmannM, MadshusIH, StangE. Pertuzumab increases 17-AAG-induced degradation of ErbB2, and this effect is further increased by combining pertuzumab with trastuzumab. Pharmaceuticals. 2012;5(7):674–689. doi:10.3390/ph507067424281706
   PubMedGoogle Scholar
• SzymanskaM, FosdahlAM, NikolaysenF, et al. A combination of two antibodies recognizing non-overlapping epitopes of HER2 induces kinase activity-dependent internalization of HER2. J Cell Mol Med. 2016;20(10):1999–2011. doi:10.1111/jcmm.1289927469139
   PubMed Web of Science ®Google Scholar
• SungM, TanX, LuB, et al. Caveolae-mediated endocytosis as a novel mechanism of resistance to Trastuzumab Emtansine (T-DM1). Mol Cancer Ther. 2018;17(1):243–253. doi:10.1158/1535-7163.MCT-17-040329054985
   PubMed Web of Science ®Google Scholar
• ZhangJ, LiQ, WuY, et al. Cholesterol content in cell membrane maintains surface levels of ErbB2 and confers a therapeutic vulnerability in ErbB2-positive breast cancer. Cell Commun Signal. 2019;20(1):15. doi:10.1186/s12964-019-0328-4
   Web of Science ®Google Scholar
• BistA, FieldingPE, FieldingCJ. Two sterol regulatory element-like sequences mediate up-regulation of caveolin gene transcription in response to low density lipoprotein free cholesterol. Proc Natl Acad Sci USA. 1997;94(20):10693–10698. doi:10.1073/pnas.94.20.106939380697
   PubMed Web of Science ®Google Scholar
• YamaguchiH, TakeoY, YoshidaS, et al. Lipid rafts and caveolin-1 are required for invadopodia formation and extracellular matrix degradation by human breast cancer cells. Cancer Res. 2009;69(22):8594–8602. doi:10.1158/0008-5472.CAN-09-230519887621
   PubMed Web of Science ®Google Scholar
• PereiraPMR, MandleywalaK, RagupathiA, et al. Temporal modulation of HER2 membrane availability increases pertuzumab uptake and pretargeted molecular imaging of gastric tumors. J Nucl Med. 2019;60(11):1569–1578. doi:10.2967/jnumed.119.22581331171598
   PubMed Web of Science ®Google Scholar
• AltwairgiAK. Statins are potential anticancerous agents (review). Oncol Rep. 2015;3(3):1019–1039. doi:10.3892/or.2015.3741
   Web of Science ®Google Scholar
• ShiY, TanSH, NgS, et al. Critical role of CAV1/caveolin-1 in cell stress responses in human breast cancer cells via modulation of lysosomal function and autophagy. Autophagy. 2015;11(5):769–784. doi:10.1080/15548627.2015.103441125945613
   PubMed Web of Science ®Google Scholar
• HaddadD, Al MadhounA, NizamR, Al-MullaF. Role of Caveolin-1 in diabetes and its complications. Oxid Med Cell Longev. 2020;116(5):9761539. doi:10.1021/acs.chemrev.5b00381
   Web of Science ®Google Scholar
• SalisO, BedirA, OzdemirT, OkuyucuA, AlacamH. The relationship between anticancer effect of metformin and the transcriptional regulation of certain genes (CHOP, CAV-1, HO-1, SGK-1 and Par-4) on MCF-7 cell line. Eur Rev Med Pharmacol Sci. 2014;11:1602–1609.
   Google Scholar
• ChungYC, ChiuHH, WeiWC, ChangKJ, ChaoWT. Application of trastuzumab emtansine in HER-2-positive and KRAS/BRAF-mutated colon cancer cells. Eur J Clin Invest. 2020;e13255. doi:10.1111/eci.1325532350854
   PubMed Web of Science ®Google Scholar