References
- Glickman MH, Ciechanover A. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol Rev. 2002;82:373–428. doi:https://doi.org/10.1152/physrev.00027.2001.
- Yang H, Chen X, Li K, Cheaito H, Yang Q, Wu G, Liu J, Dou QP. Repurposing old drugs as new inhibitors of the ubiquitin-proteasome pathway for cancer treatment. Semin Cancer Biol. 2021;68:105–122.
- Sulkshane P, Duek I, Ram J, Thakur A, Reis N, Ziv T, Glickman MH. Inhibition of proteasome reveals basal mitochondrial ubiquitination. J Proteomics. 2020;229:103949. doi:https://doi.org/10.1016/j.jprot.2020.103949.
- Tanaka K. The proteasome: overview of structure and functions. Proc Jpn Acad Ser B Phys Biol Sci. 2009;85:12–36. doi:https://doi.org/10.2183/pjab.85.12.
- Mlynarczuk-Bialy I, Doeppner TR, Golab J, Nowis D, Wilczynski GM, Parobczak K, Wigand ME, Hajdamowicz M, Biały LP, Aniolek O, et al. Biodistribution and Efficacy Studies of the Proteasome Inhibitor BSc2118 in a Mouse Melanoma Model. Transl Oncol. 2014;7:570–579. doi:https://doi.org/10.1016/j.tranon.2014.07.002.
- Nabavi SF, Atanasov AG, Khan H, Barreca D, Trombetta D, Testai L, Sureda A, Tejada S, Vacca RA, Pittalà V, et al. Targeting ubiquitin-proteasome pathway by natural, in particular polyphenols, anticancer agents: lessons learned from clinical trials. Cancer Lett. 2018;434:101–113. doi:https://doi.org/10.1016/j.canlet.2018.07.018.
- Schwartz AL, Ciechanover A. Targeting proteins for destruction by the ubiquitin system: implications for human pathobiology. Annu Rev Pharmacol Toxicol. 2009;49:73–96. doi:https://doi.org/10.1146/annurev.pharmtox.051208.165340.
- Jung T, Catalgol B, Grune T. The proteasomal system. Mol Aspects Med. 2009;30:191–296. doi:https://doi.org/10.1016/j.mam.2009.04.001.
- Park JE, Miller Z, Jun Y, Lee W, Kim KB. Next-generation proteasome inhibitors for cancer therapy. Transl Res. 2018;198:1–16. doi:https://doi.org/10.1016/j.trsl.2018.03.002.
- Sun Y, Zheng X, Yuan H, Chen G, Ouyang J, Liu J, Liu X, Xing X, Zhao B. Proteomic analyses reveal divergent ubiquitylation patterns in hepatocellula carcinoma cell lines with different metastasis potential. J Proteomics. 2020;225:103834. doi:https://doi.org/10.1016/j.jprot.2020.103834.
- Ward WH, Farma JM, editors. Cutaneous Melanoma: etiology and Therapy. Brisbane (AU): Codon Publications, 2017;Available from. http://www.ncbi.nlm.nih.gov/books/NBK481860/
- Priya P, Mohan Raj R, Vasanthakumar V, Raj V. Curcumin-loaded layer-by-layer folic acid and casein coated carboxymethyl cellulose/casein nanogels for treatment of skin cancer. Arab J Chem. 2020;13:694–708. doi:https://doi.org/10.1016/j.arabjc.2017.07.010.
- Hayano SM, Whipple KM, Korn BS, Kikkawa DO. Principles of Periocular Reconstruction following Excision of Cutaneous Malignancy. J Skin Cancer. 2012;2012:438502. doi:https://doi.org/10.1155/2012/438502.
- Jg E, Sp S, Gt B, Ds A. Chemoprevention of human skin cancer. Crit Rev Oncol Hematol. 2002;41:269–285. doi:https://doi.org/10.1016/S1040-8428(01)00185-8.
- Zieba BA, Henry L, Lacroix M, Jemaà M, Lavabre-Bertrand T, Meunier L, Coux O, Stoebner P-E. The proteasome maturation protein POMP increases proteasome assembly and activity in psoriatic lesional skin. J Dermatol Sci. 2017;88:10–19. doi:https://doi.org/10.1016/j.jdermsci.2017.04.009.
- Goldminz AM, Au SC, Kim N, Gottlieb AB, Lizzul PF. NF-κB: an essential transcription factor in psoriasis. J Dermatol Sci. 2013;69:89–94. doi:https://doi.org/10.1016/j.jdermsci.2012.11.002.
- Kim C, Pasparakis M. Epidermal p65/NF-κB signalling is essential for skin carcinogenesis. EMBO Mol Med. 2014;6:970–983. doi:https://doi.org/10.15252/emmm.201303541.
- Oeckinghaus A, The GS. NF-kappaB family of transcription factors and its regulation. Cold Spring Harb Perspect Biol. 2009;1:a000034. doi:https://doi.org/10.1101/cshperspect.a000034.
- El Yaagoubi OM, Lahmadi A, Bouyahya A, Filali H, Samaki H, El Antri S, Aboudkhil S. Antitumor Effect of Inula viscosa Extracts on DMBA-Induced Skin Carcinoma Are Mediated by Proteasome Inhibition. BioMed Res Int. 2021;2021:e6687589. doi:https://doi.org/10.1155/2021/6687589.
- Myung J, Kim KB, Crews CM. The Ubiquitin-Proteasome Pathway and Proteasome Inhibitors. Med Res Rev. 2001;21:245–273. doi:https://doi.org/10.1002/med.1009.
- Kimura A, Kurata Y, Nakabayashi J, Kagawa H, Hirano H. N-Myristoylation of the Rpt2 subunit of the yeast 26S proteasome is implicated in the subcellular compartment-specific protein quality control system. J Proteomics. 2016;130:33–41. doi:https://doi.org/10.1016/j.jprot.2015.08.021.
- Coux O, Piechaczyk M. Le système ubiquitine/protéasome : un ensemble (de) complexe(s) pour dégrader les protéines. médecine/sciences. 2000;16:623. doi:https://doi.org/10.4267/10608/1705.
- J L, G P, S J. The ubiquitin-like protein HUB1 forms SDS-resistant complexes with cellular proteins in the absence of ATP. EMBO Rep. 2003;4:1169–1174. doi:https://doi.org/10.1038/sj.embor.7400025.
- Hu Z, Li H, Wang X, Ullah K, Xu G. Proteomic approaches for the profiling of ubiquitylation events and their applications in drug discovery. J Proteomics. 2021;231:103996. doi:https://doi.org/10.1016/j.jprot.2020.103996.
- Hirano H, Kimura Y, Kimura A. Biological significance of co- and post-translational modifications of the yeast 26S proteasome. J Proteomics. 2016;134:37–46. doi:https://doi.org/10.1016/j.jprot.2015.11.016.
- Amm I, Sommer T, Wolf DH. Protein quality control and elimination of protein waste: the role of the ubiquitin-proteasome system. Biochim Biophys Acta. 2014;1843:182–196.
- Nunes AT, Annunziata CM. Proteasome Inhibitors: structure and Function. Semin Oncol. 2017;44:377–380. doi:https://doi.org/10.1053/j.seminoncol.2018.01.004.
- Monte ERC, Rossato C, Llanos RP, Russo LC, De Castro LM, Gozzo FC, de Araujo CB, Peron JPS, Sant’Anna OA, Ferro ES, et al. Interferon-gamma activity is potentiated by an intracellular peptide derived from the human 19S ATPase regulatory subunit 4 of the proteasome. J Proteomics. 2017;151:74–82. doi:https://doi.org/10.1016/j.jprot.2016.08.003.
- Kim HM, Yu Y, Cheng Y. Structure characterization of the 26S proteasome. Biochim Biophys Acta. 2011;1809:67–79. doi:https://doi.org/10.1016/j.bbagrm.2010.08.008.
- Almond JB, Cohen GM. The proteasome: a novel target for cancer chemotherapy. Leukemia. 2002;16:433–443. doi:https://doi.org/10.1038/sj.leu.2402417.
- Lopitz-Otsoa F, Rodriguez-Suarez E, Aillet F, Casado-Vela J, Lang V, Matthiesen R, Elortza F, Rodriguez MS. Integrative analysis of the ubiquitin proteome isolated using Tandem Ubiquitin Binding Entities (TUBEs). J Proteomics. 2012;75:2998–3014. doi:https://doi.org/10.1016/j.jprot.2011.12.001.
- Shahshahan MA, Beckley MN, Jazirehi AR. Potential usage of proteasome inhibitor bortezomib (Velcade, PS-341) in the treatment of metastatic melanoma: basic and clinical aspects. Am J Cancer Res. 2011;1:913–924.
- Chen L, Madura K. Increased Proteasome Activity, Ubiquitin-Conjugating Enzymes, and eEF1A Translation Factor Detected in Breast Cancer Tissue. Cancer Res. 2005;65:5599–5606. doi:https://doi.org/10.1158/0008-5472.CAN-05-0201.
- Arlt A, Bauer I, Schafmayer C, Tepel J, Müerköster SS, Brosch M, Röder C, Kalthoff H, Hampe J, Moyer MP, et al. Increased proteasome subunit protein expression and proteasome activity in colon cancer relate to an enhanced activation of nuclear factor E2-related factor 2 (Nrf2). Oncogene. 2009;28:3983–3996. doi:https://doi.org/10.1038/onc.2009.264.
- Crawford LJ, Walker B, Irvine AE. Proteasome inhibitors in cancer therapy. J Cell Commun Signal. 2011;5:101–110. doi:https://doi.org/10.1007/s12079-011-0121-7.
- Harwood CA, Proby CM, Inman GJ, Leigh IM. The Promise of Genomics and the Development of Targeted Therapies for Cutaneous Squamous Cell Carcinoma. Acta Derm Venereol. 2016;96:3–16. doi:https://doi.org/10.2340/00015555-2181.
- Schmidt M, Finley D. Regulation of proteasome activity in health and disease. Biochim Biophys Acta. 2014;1843:13–25. doi:https://doi.org/10.1016/j.bbamcr.2013.08.012.
- Yadav RK, Chae S-W, Kim H-R, Chae HJ. Endoplasmic Reticulum Stress and Cancer. J Cancer Prev. 2014;19:75–88. doi:https://doi.org/10.15430/JCP.2014.19.2.75.
- Baldi A, Pasquali P, Spugnini EP, editors. Skin Cancer: a Practical Approach. New York:Springer New York, 2014; http://link.springer.com/https://doi.org/10.1007/978-1-4614-7357-2
- Frankland-Searby S, Bhaumik SR. The 26S proteasome complex: an attractive target for cancer therapy. Biochim Biophys Acta BBA - Rev Cancer. 2012;1825:64–76. doi:https://doi.org/10.1016/j.bbcan.2011.10.003.
- Adams J, Behnke M, Chen S, Cruickshank AA, Dick LR, Grenier L, Klunder JM, Ma YT, Plamondon L, Stein RL. Potent and selective inhibitors of the proteasome: dipeptidyl boronic acids. Bioorg Med Chem Lett. 1998;8:333–338. doi:https://doi.org/10.1016/S0960-894X(98)00029-8.
- Gardner RC, Assinder SJ, Christie G, Mason GG, Markwell R, Wadsworth H, McLaughlin M, King R, Chabot-Fletcher MC, Breton JJ, et al. Characterization of peptidyl boronic acid inhibitors of mammalian 20 S and 26 S proteasomes and their inhibition of proteasomes in cultured cells. Biochem J. 2000;346:447–454. doi:https://doi.org/10.1042/bj3460447.
- Hirsch T, Dallaporta B, Zamzami N, Susin SA, Ravagnan L, Marzo I, Brenner C, Kroemer G. Proteasome Activation Occurs at an Early, Premitochondrial Step of Thymocyte Apoptosis. J Immunol. 1998;161:35–40.
- Perel G, Bliss J, Thomas CM. Carfilzomib (Kyprolis): a Novel Proteasome Inhibitor for Relapsed And/or Refractory Multiple Myeloma. Pharm Ther. 2016;41:303–307.
- Lee DH, Goldberg AL. Proteasome inhibitors: valuable new tools for cell biologists. Trends Cell Biol. 1998;8:397–403. doi:https://doi.org/10.1016/S0962-8924(98)01346-4.
- Kessler BM, Tortorella D, Altun M, Kisselev AF, Fiebiger E, Hekking BG, Ploegh HL, Overkleeft HS. Extended peptide-based inhibitors efficiently target the proteasome and reveal overlapping specificities of the catalytic β-subunits. Chem Biol. 2001;8:913–929. doi:https://doi.org/10.1016/S1074-5521(01)00069-2.
- Sugiyama N, Adrian G, Schwartz S, Wennerberg J, Ekblad L. 2020. Proteasome Inhibitors Counteract the Effect of Cisplatin in HPV-Positive Squamous Cell Carcinoma in Vitro. Research Square. DOI:https://doi.org/10.21203/rs.3.rs-30654/v1
- Kisselev AF, Akopian TN, Woo KM, Goldberg AL. The sizes of peptides generated from protein by mammalian 26 and 20 S proteasomes Implications for understanding the degradative mechanism and antigen presentation. J Biol Chem. 1999;274:3363–3371. doi:https://doi.org/10.1074/jbc.274.6.3363.
- Adams J. The proteasome: a suitable antineoplastic target. Nat Rev Cancer. 2004;4:349–360. doi:https://doi.org/10.1038/nrc1361.
- Teicher BA, Ara G, Herbst R, Palombella VJ, Adams J. The proteasome inhibitor PS-341 in cancer therapy. Clin Cancer Res Off J Am Assoc Cancer Res. 1999;5:2638–2645.
- Teicher BA, Tomaszewski JE. Proteasome inhibitors. Biochem Pharmacol. 2015;96:1–9. doi:https://doi.org/10.1016/j.bcp.2015.04.008.
- Varga C, Laubach J, Hideshima T, Chauhan D, Anderson KC, Richardson PG. Novel targeted agents in the treatment of multiple myeloma. Hematol Oncol Clin North Am. 2014;28:903–925. doi:https://doi.org/10.1016/j.hoc.2014.07.001.
- Mahmoudian M, Rahimi-Moghaddam P. The anti-cancer activity of noscapine: a review. Recent Patents Anticancer Drug Discov. 2009;4:92–97. doi:https://doi.org/10.2174/157489209787002524.
- Kudo Y, Takata T, Ogawa I, Kaneda T, Sato S, Takekoshi T, Zhao M, Miyauchi M, Nikai H. p27Kip1 accumulation by inhibition of proteasome function induces apoptosis in oral squamous cell carcinoma cells. Clin Cancer Res Off J Am Assoc Cancer Res. 2000;6:916–923.
- Brégégère F, Milner Y, Friguet B. The ubiquitin–proteasome system at the crossroads of stress-response and ageing pathways: a handle for skin care? Ageing Res Rev. 2006;5:60–90. doi:https://doi.org/10.1016/j.arr.2005.09.002.
- Milano A, Iaffaioli RV, Caponigro F. The proteasome: a worthwhile target for the treatment of solid tumours? Eur J Cancer Oxf Engl. 1990;2007(43):1125–1133.
- Sooman L, Gullbo J, Bergqvist M, Bergström S, Lennartsson J, Ekman S. Synergistic effects of combining proteasome inhibitors with chemotherapeutic drugs in lung cancer cells. BMC Res Notes. 2017;10:544. doi:https://doi.org/10.1186/s13104-017-2842-z.
- Chroma K, Mistrik M, Moudry P, Gursky J, Liptay M, Strauss R, Skrott Z, Vrtel R, Bartkova J, Kramara J, et al. Tumors overexpressing RNF168 show altered DNA repair and responses to genotoxic treatments, genomic instability and resistance to proteotoxic stress. Oncogene. 2017;36:2405–2422. doi:https://doi.org/10.1038/onc.2016.392.
- Coux O, Goldberg AL. Enzymes catalyzing ubiquitination and proteolytic processing of the p105 precursor of nuclear factor kappaB1. J Biol Chem. 1998;273:8820–8828. doi:https://doi.org/10.1074/jbc.273.15.8820.
- Bonizzi G, Bebien M, Otero DC, Johnson-Vroom KE, Cao Y, Vu D, Jegga AG, Aronow BJ, Ghosh G, Rickert RC, et al. Activation of IKKα target genes depends on recognition of specific κB binding sites by RelB: p52dimers. EMBO J. 2004;23:4202–4210. doi:https://doi.org/10.1038/sj.emboj.7600391.
- Maru GB, Gandhi K, Ramchandani A, Kumar G. The role of inflammation in skin cancer. Basel: Springer; 2014. p. 437–469. doi:https://doi.org/10.1007/978-3-0348-0837-8_17.
- Ueda Y, Richmond A. NF-κB activation in melanoma. Pigment Cell Res Spons Eur Soc Pigment Cell Res Int Pigment Cell Soc. 2006;19:112–124. doi:https://doi.org/10.1111/j.1600-0749.2006.00304.x.
- Roy P, Sarkar UA, The BS. NF-κB Activating Pathways in Multiple Myeloma. Biomedicines. 2018;6:E59. doi:https://doi.org/10.3390/biomedicines6020059.
- Mansouri L, Papakonstantinou N, Ntoufa S, Stamatopoulos K, Rosenquist R. NF-κB activation in chronic lymphocytic leukemia: a point of convergence of external triggers and intrinsic lesions. Semin Cancer Biol. 2016;39:40–48. doi:https://doi.org/10.1016/j.semcancer.2016.07.005.
- Madonna G, Ullman CD, Gentilcore G, Palmieri G, Ascierto PA. NF-κB as potential target in the treatment of melanoma. J Transl Med. 2012;10:53. doi:https://doi.org/10.1186/1479-5876-10-53.
- Sunwoo JB, Chen Z, Dong G, Yeh N, Crowl Bancroft C, Sausville E, Adams J, Elliott P, Van Waes C. Novel proteasome inhibitor PS-341 inhibits activation of nuclear factor-kappa B, cell survival, tumor growth, and angiogenesis in squamous cell carcinoma. Clin Cancer Res Off J Am Assoc Cancer Res. 2001;7:1419–1428.
- Adams J. The development of proteasome inhibitors as anticancer drugs. Cancer Cell. 2004;5:417–421. doi:https://doi.org/10.1016/S1535-6108(04)00120-5.
- Lun M, Zhang PL, Pellitteri PK, Law A, Kennedy TL, Brown RE. Nuclear factor-kappaB pathway as a therapeutic target in head and neck squamous cell carcinoma: pharmaceutical and molecular validation in human cell lines using Velcade and siRNA/NF-kappaB. Ann Clin Lab Sci. 2005;35:251–258.
- Baud V, Is KM. NF-κB a good target for cancer therapy? Hopes and pitfalls. Nat Rev Drug Discov. 2009;8:33–40. doi:https://doi.org/10.1038/nrd2781.
- Ahmed F, Haass NK. Microenvironment-Driven Dynamic Heterogeneity and Phenotypic Plasticity as a Mechanism of Melanoma Therapy Resistance. Front Oncol. 2018;8:173. doi:https://doi.org/10.3389/fonc.2018.00173.
- Karin M, Greten FR. NF-kappaB: linking inflammation and immunity to cancer development and progression. Nat Rev Immunol. 2005;5:749–759. doi:https://doi.org/10.1038/nri1703.
- Gilmore TD. NF-κB and Human Cancer: what Have We Learned over the Past 35 Years? Biomedicines. 2021;9:889. doi:https://doi.org/10.3390/biomedicines9080889.
- Dajee M, Lazarov M, Zhang JY, Cai T, Green CL, Russell AJ, Marinkovich MP, Tao S, Lin Q, Kubo Y, et al. NF-kappaB blockade and oncogenic Ras trigger invasive human epidermal neoplasia. Nature. 2003;421:639–643. doi:https://doi.org/10.1038/nature01283.
- Pham CG, Bubici C, Zazzeroni F, Papa S, Jones J, Alvarez K, Jayawardena S, De Smaele E, Cong R, Beaumont C, et al. Ferritin heavy chain upregulation by NF-kappaB inhibits TNFalpha-induced apoptosis by suppressing reactive oxygen species. Cell. 2004;119:529–542. doi:https://doi.org/10.1016/j.cell.2004.10.017.
- Kamata H, Honda S-I, Maeda S, Chang L, Hirata H, Karin M. Reactive oxygen species promote TNFalpha-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases. Cell. 2005;120:649–661. doi:https://doi.org/10.1016/j.cell.2004.12.041.
- Davies H, Bignell GR, Cox C, Stephens P, Edkins S, Clegg S, Teague J, Woffendin H, Garnett MJ, Bottomley W, et al. Mutations of the BRAF gene in human cancer. Nature. 2002;417:949–954. doi:https://doi.org/10.1038/nature00766.
- Thu YM, Su Y, Yang J, Splittgerber R, Na S, Boyd A, Mosse C, Simons C, Richmond A. NF-κB inducing kinase (NIK) modulates melanoma tumorigenesis by regulating expression of pro-survival factors through the β-catenin pathway. Oncogene. 2012;31:2580–2592. doi:https://doi.org/10.1038/onc.2011.427.
- Dang F, Nie L, Wei W. Ubiquitin signaling in cell cycle control and tumorigenesis. Cell Death Differ. 2021;28:427–438. doi:https://doi.org/10.1038/s41418-020-00648-0.
- Jia L, Sun Y, E Ubiquitin SCF. Ligases as Anticancer Targets. Curr Cancer Drug Targets. 2011;11:347–356. doi:https://doi.org/10.2174/156800911794519734.
- Soucy TA, Smith PG, Milhollen MA, Berger AJ, Gavin JM, Adhikari S, Brownell JE, Burke KE, Cardin DP, Critchley S, et al. An inhibitor of NEDD8-activating enzyme as a new approach to treat cancer. Nature. 2009;458:732–736. doi:https://doi.org/10.1038/nature07884.
- Xie C-M, Wei W, Sun Y. Role of SKP1-CUL1-F-Box-Protein (SCF) E3 Ubiquitin Ligases in Skin Cancer. J Genet Genomics. 2013;40:97–106. doi:https://doi.org/10.1016/j.jgg.2013.02.001.
- Avalle L, Pensa S, Regis G, Novelli F, Poli V. STAT1 and STAT3 in tumorigenesis. JAK-STAT. 2012;1:65–72. doi:https://doi.org/10.4161/jkst.20045.
- Lee C-J, An H-J, Cho ES, Kang HC, Lee JY, Lee HS, Cho -Y-Y. Stat2 stability regulation: an intersection between immunity and carcinogenesis. Exp Mol Med. 2020;52:1526–1536. doi:https://doi.org/10.1038/s12276-020-00506-6.
- Macias E, Rao D, DiGiovanni J. Role of Stat3 in Skin Carcinogenesis: insights Gained from Relevant Mouse Models. J Skin Cancer. 2013;2013:e684050. doi:https://doi.org/10.1155/2013/684050.
- Hixon K, Rhea L, Standley J, Canady FJ, Canady JW, Dunnwald M. Interferon Regulatory Factor 6 Controls Proliferation of Keratinocytes From Children With Van der Woude Syndrome. Cleft Palate-Craniofacial J Off Publ Am Cleft Palate-Craniofacial Assoc. 2017;54:281–286. doi:https://doi.org/10.1597/15-275.
- Nakanishi C, Toi M. Nuclear factor-kappaB inhibitors as sensitizers to anticancer drugs. Nat Rev Cancer. 2005;5:297–309. doi:https://doi.org/10.1038/nrc1588.
- Sorolla A, Yeramian A, Dolcet X, Santos De AMP, Llobet D, Schoenenberger JA, JM C, Soria X, Egido R, Llombart A, et al. Effect of proteasome inhibitors on proliferation and apoptosis of human cutaneous melanoma-derived cell lines. Br J Dermatol. 2008;158:496–504. doi:https://doi.org/10.1111/j.1365-2133.2007.08390.x.
- Kundu JK, Surh Y-J. Emerging avenues linking inflammation and cancer. Free Radic Biol Med. 2012;52:2013–2037.
- Mantovani A, Allavena P, Sica A, Balkwill F. Cancer-related inflammation. Nature. 2008;454:436–444. doi:https://doi.org/10.1038/nature07205.
- Grivennikov SI, Greten FR, Immunity KM. Inflammation, and Cancer. Cell. 2010;140:883–899. doi:https://doi.org/10.1016/j.cell.2010.01.025.
- Wu Y, Antony S, Meitzler JL, Doroshow JH. Molecular mechanisms underlying chronic inflammation-associated cancers. Cancer Lett. 2014;345:164–173. doi:https://doi.org/10.1016/j.canlet.2013.08.014.
- Neagu M, Constantin C, Caruntu C, Dumitru C, Surcel M, Inflammation: ZS. A key process in skin tumorigenesis. Oncol Lett. 2019;17:4068–4084.
- Wang Q, Pan F, Li S, Huang R, Wang X, Wang S, Liao X, Li D, Zhang L. The prognostic value of the proteasome activator subunit gene family in skin cutaneous melanoma. J Cancer. 2019;10:2205–2219. doi:https://doi.org/10.7150/jca.30612.
- Tsao H, Chin L, Garraway LA, Fisher DE. Melanoma: from mutations to medicine. Genes Dev. 2012;26:1131–1155. doi:https://doi.org/10.1101/gad.191999.112.
- Miller KD, Siegel RL, Lin CC, Mariotto AB, Kramer JL, Rowland JH, Stein KD, Alteri R, Jemal A. Cancer treatment and survivorship statistics. CA Cancer J Clin. 2016;66:271–289. doi:https://doi.org/10.3322/caac.21349.
- Merlino G, Herlyn M, Fisher DE, Bastian BC, Flaherty KT, Davies MA, Wargo JA, Curiel-Lewandrowski C, Weber MJ, Leachman SA, et al. The State of Melanoma: challenges and Opportunities. Pigment Cell Melanoma Res. 2016;29:404–416. doi:https://doi.org/10.1111/pcmr.12475.
- Olsen CM, Whiteman DC. Clinical Epidemiology of Melanoma. In: Balch CM, Atkins MB, Garbe C, Gershenwald JE, Halpern AC, Kirkwood JM, McArthur GA, Thompson JF, Sober AJ, editors. Cutaneous Melanoma. Cham: Springer International Publishing; 2020. p. 425–449. doi:https://doi.org/10.1007/978-3-030-05070-2_47.
- Prasad RR, Paudel S, Raina K, Agarwal R. Silibinin and non-melanoma skin cancers. J Tradit Complement Med. 2020;10:236–244. doi:https://doi.org/10.1016/j.jtcme.2020.02.003.
- Khan AQ, Travers JB, Kemp MG. Roles of UVA radiation and DNA damage responses in melanoma pathogenesis. Environ Mol Mutagen. 2018;59:438–460.
- Carrera C, Puig-Butillè JA, Aguilera P, Ogbah Z, Palou J, Lecha M, Malvehy J, Puig S. Impact of sunscreens on preventing UVR-induced effects in nevi: in vivo study comparing protection using a physical barrier vs sunscreen. JAMA Dermatol. 2013;149:803–813. doi:https://doi.org/10.1001/jamadermatol.2013.398.
- Simone DE, Valiante M, Silipo V. Familial melanoma and multiple primary melanoma. G Ital Dermatol Venereol. 2017;152:262–265.
- Trufant J, Jones E. Cham: Springer International Publishing; 2019. p. 171–208. doi:https://doi.org/10.1007/978-3-030-18065-2_17.
- Grazia G, Penna I, Perotti V, Anichini A, Tassi E. Towards combinatorial targeted therapy in melanoma: from pre-clinical evidence to clinical application (review). Int J Oncol. 2014;45:929–949. doi:https://doi.org/10.3892/ijo.2014.2491.
- Obrist F, Manic G, Kroemer G, Vitale I, Trial Watch: GL. Proteasomal inhibitors for anticancer therapy. Mol Cell Oncol. 2015;2:e974463. doi:https://doi.org/10.4161/23723556.2014.974463.
- Sidor-Kaczmarek J, Cichorek M, Spodnik JH, Wójcik S, Moryś J. Proteasome inhibitors against amelanotic melanoma. Cell Biol Toxicol. 2017;33:557–573. doi:https://doi.org/10.1007/s10565-017-9390-0.
- Reuland SN, Goldstein NB, Partyka KA, Smith S, Luo Y, Fujita M, Gonzalez R, Lewis K, Norris DA, Shellman YG. ABT-737 synergizes with Bortezomib to kill melanoma cells. Biol Open. 2012;1:92–100. doi:https://doi.org/10.1242/bio.2011035.
- Selimovic D, Porzig BBOW, El-Khattouti A, Badura HE, Ahmad M, Ghanjati F, Santourlidis S, Haikel Y, Hassan M. Bortezomib/proteasome inhibitor triggers both apoptosis and autophagy-dependent pathways in melanoma cells. Cell Signal. 2013;25:308–318. doi:https://doi.org/10.1016/j.cellsig.2012.10.004.
- Amiri KI, Richmond A. Role of nuclear factor-kappa B in melanoma. Cancer Metastasis Rev. 2005;24:301–313. doi:https://doi.org/10.1007/s10555-005-1579-7.
- Amiri KI, Horton LW, LaFleur BJ, Sosman JA, Richmond A. Augmenting chemosensitivity of malignant melanoma tumors via proteasome inhibition: implication for bortezomib (VELCADE, PS-341) as a therapeutic agent for malignant melanoma. Cancer Res. 2004;64:4912–4918. doi:https://doi.org/10.1158/0008-5472.CAN-04-0673.
- Triozzi PL, Eng C, Singh AD. Targeted therapy for uveal melanoma. Cancer Treat Rev. 2008;34:247–258. doi:https://doi.org/10.1016/j.ctrv.2007.12.002.
- Wolter KG, Verhaegen M, Fernández Y, Nikolovska-Coleska Z, Riblett M, Martin De La Vega C, Wang S, Soengas MS. Therapeutic window for melanoma treatment provided by selective effects of the proteasome on Bcl-2 proteins. Cell Death Differ. 2007;14:1605–1616. doi:https://doi.org/10.1038/sj.cdd.4402163.
- Lesinski GB, Raig ET, Guenterberg K, Brown L, Go MR, Shah NN, Lewis A, Quimper M, Hade E, Young G, et al. IFN-alpha and bortezomib overcome Bcl-2 and Mcl-1 overexpression in melanoma cells by stimulating the extrinsic pathway of apoptosis. Cancer Res. 2008;68:8351–8360. doi:https://doi.org/10.1158/0008-5472.CAN-08-0426.
- Wang C, Li S, Wang M. Evodiamine-induced human melanoma A375-S2 cell death was mediated by PI3K/Akt/caspase and Fas-L/NF-κB signaling pathways and augmented by ubiquitin–proteasome inhibition. Toxicol In Vitro. 2010;24:898–904. doi:https://doi.org/10.1016/j.tiv.2009.11.019.
- Ma J, Guo W, Li C. Ubiquitination in melanoma pathogenesis and treatment. Cancer Med. 2017;6:1362–1377. doi:https://doi.org/10.1002/cam4.1069.
- Levy C, Khaled M, Fisher DE. MITF: master regulator of melanocyte development and melanoma oncogene. Trends Mol Med. 2006;12:406–414. doi:https://doi.org/10.1016/j.molmed.2006.07.008.
- Wiedemann GM, Aithal C, Kraechan A, Heise C, Cadilha BL, Zhang J, Duewell P, Ballotti R, Endres S, Bertolotto C, et al. Microphthalmia-Associated Transcription Factor (MITF) Regulates Immune Cell Migration into Melanoma. Transl Oncol. 2018;12:350–360. doi:https://doi.org/10.1016/j.tranon.2018.10.014.
- Garraway LA, Widlund HR, Rubin MA, Getz G, Berger AJ, Ramaswamy S, Beroukhim R, Milner DA, Granter SR, Du J, et al. Integrative genomic analyses identify MITF as a lineage survival oncogene amplified in malignant melanoma. Nature. 2005;436:117–122. doi:https://doi.org/10.1038/nature03664.
- Nakayama K. Growth and progression of melanoma and non-melanoma skin cancers regulated by ubiquitination. Pigment Cell Melanoma Res. 2010;23:338–351. doi:https://doi.org/10.1111/j.1755-148X.2010.00692.x.
- Greaves WO, Verma S, Patel KP, Davies MA, Barkoh BA, Galbincea JM, Yao H, Lazar AJ, Aldape KD, Medeiros LJ, et al. Frequency and spectrum of BRAF mutations in a retrospective, single-institution study of 1112 cases of melanoma. J Mol Diagn JMD. 2013;15:220–226. doi:https://doi.org/10.1016/j.jmoldx.2012.10.002.
- Sosman JA, Kim KB, Schuchter L, Gonzalez R, Pavlick AC, Weber JS, McArthur GA, Hutson TE, Moschos SJ, Flaherty KT, et al. Survival in BRAF V600-mutant advanced melanoma treated with vemurafenib. N Engl J Med. 2012;366:707–714. doi:https://doi.org/10.1056/NEJMoa1112302.
- Vasudevan S, Flashner-Abramson E, Alkhatib H, Roy Chowdhury S, Adejumobi IA, Vilenski D, Stefansky S, Rubinstein AM, Kravchenko-Balasha N. Overcoming resistance to BRAFV600E inhibition in melanoma by deciphering and targeting personalized protein network alterations. Npj Precis Oncol. 2021;5:50. doi:https://doi.org/10.1038/s41698-021-00190-3.
- Alqathama A. BRAF in malignant melanoma progression and metastasis: potentials and challenges. Am J Cancer Res. 2020;10:1103–1114.
- Nikolaou VA, Stratigos AJ, Flaherty KT, Tsao H. Melanoma: new insights and new therapies. J Invest Dermatol. 2012;132:854–863. doi:https://doi.org/10.1038/jid.2011.421.
- Kalal BS, Upadhya D, Pai VR. Chemotherapy Resistance Mechanisms in Advanced Skin Cancer. Oncol Rev. 2017;11:326.
- Wu S, Singh RK. Resistance to Chemotherapy and Molecularly Targeted Therapies: rationale for Combination Therapy in Malignant Melanoma. Curr Mol Med. 2011;11:553–563. doi:https://doi.org/10.2174/156652411800615153.
- Chapman PB, Hauschild A, Robert C, Haanen JB, Ascierto P, Larkin J, Dummer R, Garbe C, Testori A, Maio M, et al. Improved survival with vemurafenib in melanoma with BRAF V600E mutation. N Engl J Med. 2011;364:2507–2516. doi:https://doi.org/10.1056/NEJMoa1103782.
- Lacouture M, Sibaud V. Toxic Side Effects of Targeted Therapies and Immunotherapies Affecting the Skin, Oral Mucosa, Hair, and Nails. Am J Clin Dermatol. 2018;19:31–39. doi:https://doi.org/10.1007/s40257-018-0384-3.
- Capalbo C, Belardinilli F, Filetti M, Parisi C, Petroni M, Colicchia V, Tessitore A, Santoni M, Coppa A, Giannini G, et al. Effective treatment of a platinum-resistant cutaneous squamous cell carcinoma case by EGFR pathway inhibition. Mol Clin Oncol. 2018;9:30–34.
- McHugh A, Fernandes K, South AP, Mellerio JE, Salas-Alanís JC, Proby CM, Leigh IM, Saville MK. Preclinical comparison of proteasome and ubiquitin E1 enzyme inhibitors in cutaneous squamous cell carcinoma: the identification of mechanisms of differential sensitivity. Oncotarget. 2018;9:20265–20281. doi:https://doi.org/10.18632/oncotarget.24750.
- Karia PS, Han J, Schmults CD. Cutaneous squamous cell carcinoma: estimated incidence of disease, nodal metastasis, and deaths from disease in the United States, 2012. J Am Acad Dermatol. 2013;68:957–966. doi:https://doi.org/10.1016/j.jaad.2012.11.037.
- Green AC, Olsen CM. Cutaneous squamous cell carcinoma: an epidemiological review. Br J Dermatol. 2017;177:373–381. doi:https://doi.org/10.1111/bjd.15324.
- Fine J-D, Johnson LB, Weiner M, Li K-P SC. Epidermolysis bullosa and the risk of life-threatening cancers: the National EB Registry experience, 1986-2006. J Am Acad Dermatol. 2009;60:203–211. doi:https://doi.org/10.1016/j.jaad.2008.09.035.
- Zhong L, Yang X, Zhu Y, Peng J, Cao Y. Radix Tetrastigma Hemsleyani Flavone Suppresses Cutaneous Squamous Cell Carcinoma A431 Cells via Proteasome Inhibition. Med Sci Monit Int Med J Exp Clin Res. 2019;25:436–442.
- Wang S, Shen P, Zhou J, Lu Y. Diet phytochemicals and cutaneous carcinoma chemoprevention: a review. Pharmacol Res. 2017;119:327–346. doi:https://doi.org/10.1016/j.phrs.2017.02.021.
- Pandey S, Patil A. Recent advances on self modified patch for (trans) dermal drug delivery. Recent Pat Drug Deliv Formul. 2015;9:88–94. doi:https://doi.org/10.2174/187221130901150303113918.
- Fakhari A, Anand Subramony J. Engineered in-situ depot-forming hydrogels for intratumoral drug delivery. J Control Release Off J Control Release Soc. 2015;220:465–475. doi:https://doi.org/10.1016/j.jconrel.2015.11.014.
- Pasparakis M, Courtois G, Hafner M, Schmidt-Supprian M, Nenci A, Toksoy A, Krampert M, Goebeler M, Gillitzer R, Israel A, et al. TNF-mediated inflammatory skin disease in mice with epidermis-specific deletion of IKK2. Nature. 2002;417:861–866. doi:https://doi.org/10.1038/nature00820.
- Lind MH, Rozell B, Wallin RPA, van Hogerlinden M, Ljunggren H-G, Toftgård R, Sur I. Tumor necrosis factor receptor 1-mediated signaling is required for skin cancer development induced by NF-kappaB inhibition. Proc Natl Acad Sci U S A. 2004;101:4972–4977. doi:https://doi.org/10.1073/pnas.0307106101.
- Sur I, Ulvmar M, The Two-Faced TR. NF-κB in the Skin. Int Rev Immunol. 2008;27:205–223. doi:https://doi.org/10.1080/08830180802130319.
- Anghaei S, Kamyab-Hesari K, Haddadi S, Jolehar M. New diagnostic markers in basal cell carcinoma. J Oral Maxillofac Pathol. 2020;24:99. doi:https://doi.org/10.4103/jomfp.JOMFP_199_19.
- Feller L, Khammissa RAG, Kramer B, Altini M, Lemmer J. Basal cell carcinoma, squamous cell carcinoma and melanoma of the head and face. Head Face Med. 2016;12:11. doi:https://doi.org/10.1186/s13005-016-0106-0.
- Dika E, Veronesi G, Patrizi A, De Salvo S, Misciali C, Baraldi C, Mussi M, Fabbri E, Tartari F, It’s Time LM. For Mohs: micrographic Surgery For The Treatment Of High-Risk Basal Cell Carcinomas Of The Head And Neck Region. Dermatologic Therapy 2020;33:e13474. doi:https://doi.org/10.1111/dth.13474.
- Park K, Lee J-H. Bcl-XL protein is markedly decreased in UVB-irradiated basal cell carcinoma cell lines through proteasome-mediated degradation. Oncol Rep. 2009;21:689–692.
- Mo J-S, Kim M-Y, Han S-O, Kim I-S, Ann E-J, Lee KS, Seo M-S, Kim J-Y, Lee S-C, Park J-W, et al. Integrin-linked kinase controls Notch1 signaling by down-regulation of protein stability through Fbw7 ubiquitin ligase. Mol Cell Biol. 2007;27:5565–5574. doi:https://doi.org/10.1128/MCB.02372-06.
- Nicolas M, Wolfer A, Raj K, Kummer JA, Mill P, van Noort M, Hui C, Clevers H, Dotto GP, Notch RF. functions as a tumor suppressor in mouse skin. Nat Genet. 2003;33:416–421. doi:https://doi.org/10.1038/ng1099.
- Takebe N, Nguyen D, Yang SX. Targeting Notch signaling pathway in cancer: clinical development advances and challenges. Pharmacol Ther. 2014;141:140–149. doi:https://doi.org/10.1016/j.pharmthera.2013.09.005.
- Miele L, Miao H, Nickoloff BJ. NOTCH signaling as a novel cancer therapeutic target. Curr Cancer Drug Targets. 2006;6:313–323. doi:https://doi.org/10.2174/156800906777441771.
- Wei C-L, Wu Q, Vega VB, Chiu KP, Ng P, Zhang T, Shahab A, Yong HC, Fu Y, Weng Z, et al. A global map of p53 transcription-factor binding sites in the human genome. Cell. 2006;124:207–219. doi:https://doi.org/10.1016/j.cell.2005.10.043.
- Lefort K, Mandinova A, Ostano P, Kolev V, Calpini V, Kolfschoten I, Devgan V, Lieb J, Raffoul W, Hohl D, et al. Notch1 is a p53 target gene involved in human keratinocyte tumor suppression through negative regulation of ROCK1/2 and MRCKalpha kinases. Genes Dev. 2007;21:562–577. doi:https://doi.org/10.1101/gad.1484707.
- Mandinova A, Lefort K, Di Vignano AT, Stonely W, Ostano P, Chiorino G, Iwaki H, Nakanishi J, Dotto GP. The FoxO3a gene is a key negative target of canonical Notch signalling in the keratinocyte UVB response. EMBO J. 2008;27:1243–1254. doi:https://doi.org/10.1038/emboj.2008.45.