Endoplasmic Reticulum Dysfunction: An Emerging Mechanism of Vitiligo Pathogenesis

References

• Ezzedine K, Eleftheriadou V, Whitton M, et al. Vitiligo. Lancet. 2015;386(9988):74–84. doi:10.1016/S0140-6736(14)60763-7
   PubMed Web of Science ®Google Scholar
• Ezzedine K, Lim HW, Suzuki T, et al. Revised classification/nomenclature of vitiligo and related issues: the Vitiligo Global Issues Consensus Conference. Pigment Cell Melanoma Res. 2012;25(3):E1–E13. doi:10.1111/j.1755-148X.2012.00997.x
   PubMed Web of Science ®Google Scholar
• Smith MP, Ly K, Thibodeaux Q, et al. Home phototherapy for patients with vitiligo: challenges and solutions. Clin Cosmet Investig Dermatol. 2019;12:451–459. doi:10.2147/CCID.S185798
   PubMed Web of Science ®Google Scholar
• Lee AY. Role of keratinocytes in the development of vitiligo. Ann Dermatol. 2012;24(2):115–125. doi:10.5021/ad.2012.24.2.115
   PubMed Web of Science ®Google Scholar
• Le Poole IC, Das PK, van den Wijngaard RM, et al. Review of the etiopathomechanism of vitiligo: a convergence theory. Exp Dermatol. 1993;2(4):145–153. doi:10.1111/j.1600-0625.1993.tb00023.x
   PubMedGoogle Scholar
• Richmond JM, Frisoli ML, Harris JE. Innate immune mechanisms in vitiligo: danger from within. Curr Opin Immunol. 2013;25(6):676–682. doi:10.1016/j.coi.2013.10.010
   PubMed Web of Science ®Google Scholar
• Jian Z, Li K, Song P, et al. Impaired activation of the Nrf2-ARE signaling pathway undermines H2O2-induced oxidative stress response: a possible mechanism for melanocyte degeneration in vitiligo. J Invest Dermatol. 2014;134(8):2221–2230. doi:10.1038/jid.2014.152
   PubMed Web of Science ®Google Scholar
• Jian Z, Li K, Liu L, et al. Heme oxygenase-1 protects human melanocytes from H2O2-induced oxidative stress via the Nrf2-ARE pathway. J Invest Dermatol. 2011;131(7):1420–1427. doi:10.1038/jid.2011.56
   PubMed Web of Science ®Google Scholar
• Yi X, Guo W, Shi Q, et al. SIRT3-dependent mitochondrial dynamics remodeling contributes to oxidative stress-induced melanocyte degeneration in vitiligo. Theranostics. 2019;9(6):1614–1633. doi:10.7150/thno.30398
   PubMed Web of Science ®Google Scholar
• Xie H, Zhou F, Liu L, et al. Vitiligo: how do oxidative stress-induced autoantigens trigger autoimmunity? J Dermatol Sci. 2016;81(1):3–9. doi:10.1016/j.jdermsci.2015.09.003
   PubMed Web of Science ®Google Scholar
• Li S, Zhu G, Yang Y, et al. Oxidative stress drives CD8(+) T-cell skin trafficking in patients with vitiligo through CXCL16 upregulation by activating the unfolded protein response in keratinocytes. J Allergy Clin Immunol. 2017;140(1):177–189.e9. doi:10.1016/j.jaci.2016.10.013
   PubMed Web of Science ®Google Scholar
• Chang WL, Ko CH. The role of oxidative stress in vitiligo: an update on its pathogenesis and therapeutic implications. Cells. 2023;12(6):936. doi:10.3390/cells12060936
   PubMed Web of Science ®Google Scholar
• Yoshida H. ER stress and diseases. Febs j. 2007;274(3):630–658. doi:10.1111/j.1742-4658.2007.05639.x
   PubMed Web of Science ®Google Scholar
• Oakes SA, Papa FR. The role of endoplasmic reticulum stress in human pathology. Annu Rev Pathol. 2015;10(1):173–194. doi:10.1146/annurev-pathol-012513-104649
   PubMed Web of Science ®Google Scholar
• Zeeshan HM, Lee GH, Kim HR, et al. Endoplasmic Reticulum Stress and Associated ROS. Int J Mol Sci. 2016;17(3):327. doi:10.3390/ijms17030327
   PubMed Web of Science ®Google Scholar
• Wang M, Kaufman RJ. Protein misfolding in the endoplasmic reticulum as a conduit to human disease. Nature. 2016;529(7586):326–335. doi:10.1038/nature17041
   PubMed Web of Science ®Google Scholar
• Park K, Lee SE, Shin KO, et al. Insights into the role of endoplasmic reticulum stress in skin function and associated diseases. Febs j. 2019;286(2):413–425. doi:10.1111/febs.14739
   PubMed Web of Science ®Google Scholar
• Boissy RE, Beato KE, Nordlund JJ. Dilated rough endoplasmic reticulum and premature death in melanocytes cultured from the vitiligo mouse. Am J Pathol. 1991;138(6):1511–1525.
   PubMed Web of Science ®Google Scholar
• Tobin DJ, Swanson NN, Pittelkow MR, et al. Melanocytes are not absent in lesional skin of long duration vitiligo. J Pathol. 2000;191(4):407–416. doi:10.1002/1096-9896(2000)9999:9999<::AID-PATH659>3.0.CO;2-D
   PubMed Web of Science ®Google Scholar
• Porter KR, Claude A, Fullam EF. A Study Of Tissue Culture Cells By Electron Microscopy: Methods And Preliminary Observations. J Exp Med. 1945;81(3):233–246. doi:10.1084/jem.81.3.233
   PubMed Web of Science ®Google Scholar
• Schwarz DS, Blower MD. The endoplasmic reticulum: structure, function and response to cellular signaling. Cell Mol Life Sci. 2016;73(1):79–94. doi:10.1007/s00018-015-2052-6
   PubMed Web of Science ®Google Scholar
• Kang X, Wang J, Yan L. Endoplasmic reticulum in oocytes: spatiotemporal distribution and function. J Assist Reprod Genet. 2023;40(6):1255–1263. doi:10.1007/s10815-023-02782-3
   PubMed Web of Science ®Google Scholar
• Lopez-Crisosto C, Pennanen C, Vasquez-Trincado C, et al. Sarcoplasmic reticulum-mitochondria communication in cardiovascular pathophysiology. Nat Rev Cardiol. 2017;14(6):342–360. doi:10.1038/nrcardio.2017.23
   PubMed Web of Science ®Google Scholar
• Kepp O, Galluzzi L. Preface: endoplasmic reticulum in health and disease. Int Rev Cell Mol Biol. 2020;350:xiii–xvii.
   PubMed Web of Science ®Google Scholar
• Rowland AA, Voeltz GK. Endoplasmic reticulum-mitochondria contacts: function of the junction. Nat Rev Mol Cell Biol. 2012;13(10):607–625. doi:10.1038/nrm3440
   PubMed Web of Science ®Google Scholar
• Friedman JR, Voeltz GK. The ER in 3D: a multifunctional dynamic membrane network. Trends Cell Biol. 2011;21(12):709–717. doi:10.1016/j.tcb.2011.07.004
   PubMed Web of Science ®Google Scholar
• Brandizzi F, Barlowe C. Organization of the ER-Golgi interface for membrane traffic control. Nat Rev Mol Cell Biol. 2013;14(6):382–392. doi:10.1038/nrm3588
   PubMed Web of Science ®Google Scholar
• Navid F, Colbert RA. Causes and consequences of endoplasmic reticulum stress in rheumatic disease. Nat Rev Rheumatol. 2017;13(1):25–40. doi:10.1038/nrrheum.2016.192
   PubMed Web of Science ®Google Scholar
• Scheuner D, Song B, McEwen E, et al. Translational control is required for the unfolded protein response and in vivo glucose homeostasis. Mol Cell. 2001;7(6):1165–1176. doi:10.1016/S1097-2765(01)00265-9
   PubMed Web of Science ®Google Scholar
• Celli A, Crumrine D, Meyer JM, et al. Endoplasmic reticulum calcium regulates epidermal barrier response and desmosomal structure. J Invest Dermatol. 2016;136(9):1840–1847. doi:10.1016/j.jid.2016.05.100
   PubMed Web of Science ®Google Scholar
• Blackstone C. Cellular pathways of hereditary spastic paraplegia. Annu Rev Neurosci. 2012;35(1):25–47. doi:10.1146/annurev-neuro-062111-150400
   PubMedGoogle Scholar
• Crapart CC, Scott ZC, Konno T, et al. Luminal transport through intact endoplasmic reticulum limits the magnitude of localized Ca2+ signals. Proc Natl Acad Sci U S A. 2024;121(13):e2312172121. doi:10.1073/pnas.2312172121
   PubMed Web of Science ®Google Scholar
• Bian Y, Yu H, Jin M, Gao X. Repigmentation by combined narrow‑band ultraviolet B/adipose‑derived stem cell transplantation in the mouse model: role of Nrf2/HO‑1‑mediated Ca2+ homeostasis. Mol Med Rep. 2022;25(1):6. doi:10.3892/mmr.2021.12522
   PubMed Web of Science ®Google Scholar
• Araki K, Nagata K. Protein folding and quality control in the ER. Cold Spring Harb Perspect Biol. 2012;4(8):a015438–a015438. doi:10.1101/cshperspect.a015438
   PubMedGoogle Scholar
• Scriven P, Brown NJ, Pockley AG, et al. The unfolded protein response and cancer: a brighter future unfolding? J Mol Med. 2007;85(4):331–341. doi:10.1007/s00109-006-0150-5
   PubMed Web of Science ®Google Scholar
• Gardner BM, Walter P. Unfolded proteins are Ire1-activating ligands that directly induce the unfolded protein response. Science. 2011;333(6051):1891–1894. doi:10.1126/science.1209126
   PubMed Web of Science ®Google Scholar
• Williams B, Verchot J, Dickman MB. When supply does not meet demand-ER stress and plant programmed cell death. Front Plant Sci. 2014;5:211. doi:10.3389/fpls.2014.00211
   PubMed Web of Science ®Google Scholar
• Marciniak SJ, Chambers JE, Ron D. Pharmacological targeting of endoplasmic reticulum stress in disease. Nat Rev Drug Discov. 2022;21(2):115–140. doi:10.1038/s41573-021-00320-3
   PubMed Web of Science ®Google Scholar
• Zhang SX, Wang JJ, Starr CR, et al. The endoplasmic reticulum: homeostasis and crosstalk in retinal health and disease. Prog Retin Eye Res. 2024;98:101231. doi:10.1016/j.preteyeres.2023.101231
   PubMed Web of Science ®Google Scholar
• Walter P, Ron D. The unfolded protein response: from stress pathway to homeostatic regulation. Science. 2011;334(6059):1081–1096. doi:10.1126/science.1209038
   PubMed Web of Science ®Google Scholar
• Krebs J, Agellon LB, Michalak M. Ca(2+) homeostasis and endoplasmic reticulum (ER) stress: an integrated view of calcium signaling. Biochem Biophys Res Commun. 2015;460(1):114–121. doi:10.1016/j.bbrc.2015.02.004
   PubMed Web of Science ®Google Scholar
• Carreras-Sureda A, Pihán P, Hetz C. Calcium signaling at the endoplasmic reticulum: fine-tuning stress responses. Cell Calcium. 2018;70:24–31. doi:10.1016/j.ceca.2017.08.004
   PubMed Web of Science ®Google Scholar
• Mekahli D, Bultynck G, Parys JB, et al. Endoplasmic-reticulum calcium depletion and disease. Cold Spring Harb Perspect Biol. 2011;3(6):a004317–a004317. doi:10.1101/cshperspect.a004317
   PubMed Web of Science ®Google Scholar
• Ando H, Ichihashi M, Hearing VJ. Role of the ubiquitin proteasome system in regulating skin pigmentation. Int J Mol Sci. 2009;10(10):4428–4434. doi:10.3390/ijms10104428
   PubMed Web of Science ®Google Scholar
• Athanasiou D, Aguila M, Bellingham J, et al. The molecular and cellular basis of rhodopsin retinitis pigmentosa reveals potential strategies for therapy. Prog Retin Eye Res. 2018;62:1–23. doi:10.1016/j.preteyeres.2017.10.002
   PubMed Web of Science ®Google Scholar
• Athanasiou D, Bevilacqua D, Aguila M, et al. The co-chaperone and reductase ERdj5 facilitates rod opsin biogenesis and quality control. Hum Mol Genet. 2014;23(24):6594–6606. doi:10.1093/hmg/ddu385
   PubMed Web of Science ®Google Scholar
• Athanasiou D, Kosmaoglou M, Kanuga N, et al. BiP prevents rod opsin aggregation. Mol Biol Cell. 2012;23(18):3522–3531. doi:10.1091/mbc.e12-02-0168
   PubMed Web of Science ®Google Scholar
• Ruppert M, Pyun J, Chalam KV, et al. Multimodal Imaging Characteristics of ADRP in a Family with p.Thr58Arg Substituted RHO Mutation. Case Rep Genet. 2020;2020:8860863. doi:10.1155/2020/8860863
   PubMedGoogle Scholar
• Bilbao-Malavé V, González-Zamora J, de la Puente M, et al. Mitochondrial dysfunction and endoplasmic reticulum stress in age related macular degeneration, role in pathophysiology, and possible new therapeutic strategies. Antioxidants. 2021;10(8):1170. doi:10.3390/antiox10081170
   Web of Science ®Google Scholar
• Yang F, Yang L, Wataya-Kaneda M, et al. Uncoupling of ER/mitochondrial oxidative stress in mTORC1 hyperactivation-associated skin hypopigmentation. J Invest Dermatol. 2018;138(3):669–678. doi:10.1016/j.jid.2017.10.007
   PubMed Web of Science ®Google Scholar
• Hattori M, Ishikawa O, Oikawa D, et al. In-frame Val(216)-Ser(217) deletion of KIT in mild piebaldism causes aberrant secretion and SCF response. J Dermatol Sci. 2018;91(1):35–42. doi:10.1016/j.jdermsci.2018.03.012
   PubMed Web of Science ®Google Scholar
• Zhang Q, Cui T, Chang Y, et al. HO-1 regulates the function of Treg: association with the immune intolerance in vitiligo. J Cell Mol Med. 2018;22(9):4335–4343. doi:10.1111/jcmm.13723
   PubMed Web of Science ®Google Scholar
• Boissy RE, Liu YY, Medrano EE, et al. Structural aberration of the rough endoplasmic reticulum and melanosome compartmentalization in long-term cultures of melanocytes from vitiligo patients. J Invest Dermatol. 1991;97(3):395–404. doi:10.1111/1523-1747.ep12480976
   PubMed Web of Science ®Google Scholar
• Im S, Hann SK, Kim HI, et al. Biologic characteristics of cultured human vitiligo melanocytes. Int J Dermatol. 1994;33(8):556–562. doi:10.1111/j.1365-4362.1994.tb02895.x
   PubMed Web of Science ®Google Scholar
• Le Poole IC, Boissy RE, Sarangarajan R, et al. PIG3V, an immortalized human vitiligo melanocyte cell line, expresses dilated endoplasmic reticulum. Vitro Cell Dev Biol Anim. 2000;36(5):309–319. doi:10.1290/1071-2690(2000)036<0309:PAIHVM>2.0.CO;2
   PubMed Web of Science ®Google Scholar
• Jadeja SD, Vaishnav J, Bharti AH, et al. Elevated X-Box binding protein1 splicing and interleukin-17A expression are associated with active generalized vitiligo in Gujarat population. Front Immunol. 2021;12:801724. doi:10.3389/fimmu.2021.801724
   PubMed Web of Science ®Google Scholar
• Ren Y, Yang S, Xu S, et al. Genetic variation of promoter sequence modulates XBP1 expression and genetic risk for vitiligo. PLoS Genet. 2009;5(6):e1000523. doi:10.1371/journal.pgen.1000523
   PubMed Web of Science ®Google Scholar
• Sun X, Wang T, Huang B, et al. RIPK1 regulates the survival of human melanocytes upon endoplasmic reticulum stress. Exp Ther Med. 2020;19(5):3239–3246. doi:10.3892/etm.2020.8575
   PubMed Web of Science ®Google Scholar
• Ahn Y, Lee EJ, Luo E, et al. Particulate matter promotes melanin production through endoplasmic reticulum stress‒mediated IRE1α signaling. J Invest Dermatol. 2022;142(5):1425–1434.e6. doi:10.1016/j.jid.2021.08.444
   PubMed Web of Science ®Google Scholar
• Shi Q, Zhang W, Guo S, et al. Oxidative stress-induced overexpression of miR-25: the mechanism underlying the degeneration of melanocytes in vitiligo. Cell Death Differ. 2016;23(3):496–508. doi:10.1038/cdd.2015.117
   PubMed Web of Science ®Google Scholar
• Ortonne JP, Bose SK. Vitiligo: where do we stand? Pigment Cell Res. 1993;6(2):61–72. doi:10.1111/j.1600-0749.1993.tb00584.x
   PubMedGoogle Scholar
• Elbaz Y, Schuldiner M. Staying in touch: the molecular era of organelle contact sites. Trends Biochem Sci. 2011;36(11):616–623. doi:10.1016/j.tibs.2011.08.004
   PubMed Web of Science ®Google Scholar
• Phillips MJ, Voeltz GK. Structure and function of ER membrane contact sites with other organelles. Nat Rev Mol Cell Biol. 2016;17(2):69–82. doi:10.1038/nrm.2015.8
   PubMed Web of Science ®Google Scholar
• Csordás G, Weaver D, Hajnóczky G. Endoplasmic reticulum-mitochondrial contactology: structure and signaling functions. Trends Cell Biol. 2018;28(7):523–540. doi:10.1016/j.tcb.2018.02.009
   PubMed Web of Science ®Google Scholar
• Aboufares El Alaoui A, Buhl E, Galizia S, et al. Increased interaction between endoplasmic reticulum and mitochondria following sleep deprivation. BMC Biol. 2023;21(1):1. doi:10.1186/s12915-022-01498-7
   PubMed Web of Science ®Google Scholar
• Wang Y, Li S, Li C. Perspectives of new advances in the pathogenesis of vitiligo: from oxidative stress to autoimmunity. Med Sci Monit. 2019;25:1017–1023. doi:10.12659/MSM.914898
   PubMed Web of Science ®Google Scholar
• Kaushik H, Kumar V, Parsad D. Mitochondria-Melanocyte cellular interactions: an emerging mechanism of vitiligo pathogenesis. J Eur Acad Dermatol Venereol. 2023;37(11):2196–2207. doi:10.1111/jdv.19019
   PubMed Web of Science ®Google Scholar
• Marks MS, Seabra MC. The melanosome: membrane dynamics in black and white. Nat Rev Mol Cell Biol. 2001;2(10):738–748. doi:10.1038/35096009
   PubMed Web of Science ®Google Scholar
• Daniele T, Schiaffino MV. Organelle biogenesis and interorganellar connections: better in contact than in isolation. Commun Integr Biol. 2014;7:e29587.
   PubMedGoogle Scholar
• Sitaram A, Marks MS. Mechanisms of protein delivery to melanosomes in pigment cells. Physiology. 2012;27(2):85–99. doi:10.1152/physiol.00043.2011
   PubMed Web of Science ®Google Scholar
• Park HY, Kosmadaki M, Yaar M, et al. Cellular mechanisms regulating human melanogenesis. Cell Mol Life Sci. 2009;66(9):1493–1506. doi:10.1007/s00018-009-8703-8
   PubMed Web of Science ®Google Scholar
• Slominski A, Tobin DJ, Shibahara S, et al. Melanin pigmentation in mammalian skin and its hormonal regulation. Physiol Rev. 2004;84(4):1155–1228. doi:10.1152/physrev.00044.2003
   PubMed Web of Science ®Google Scholar
• Watt B, van Niel G, Raposo G, et al. PMEL: a pigment cell-specific model for functional amyloid formation. Pigment Cell Melanoma Res. 2013;26(3):300–315. doi:10.1111/pcmr.12067
   PubMed Web of Science ®Google Scholar
• Simon JD, Peles D, Wakamatsu K, et al. Current challenges in understanding melanogenesis: bridging chemistry, biological control, morphology, and function. Pigment Cell Melanoma Res. 2009;22(5):563–579. doi:10.1111/j.1755-148X.2009.00610.x
   PubMed Web of Science ®Google Scholar
• Hoogduijn MJ, Smit NP, van der Laarse A, et al. Melanin has a role in Ca2+ homeostasis in human melanocytes. Pigment Cell Res. 2003;16(2):127–132. doi:10.1034/j.1600-0749.2003.00018.x
   PubMedGoogle Scholar
• Patel S, Docampo R. Acidic calcium stores open for business: expanding the potential for intracellular Ca2+ signaling. Trends Cell Biol. 2010;20(5):277–286. doi:10.1016/j.tcb.2010.02.003
   PubMed Web of Science ®Google Scholar
• Burgoyne T, Patel S, Eden ER. Calcium signaling at ER membrane contact sites. Biochim Biophys Acta. 2015;1853(9):2012–2017. doi:10.1016/j.bbamcr.2015.01.022
   PubMed Web of Science ®Google Scholar
• Guan C, Lin F, Zhou M, et al. The role of VIT1/FBXO11 in the regulation of apoptosis and tyrosinase export from endoplasmic reticulum in cultured melanocytes. Int J Mol Med. 2010;26(1):57–65. doi:10.3892/ijmm_00000435
   PubMed Web of Science ®Google Scholar
• Francis E, Wang N, Parag H, et al. Tyrosinase maturation and oligomerization in the endoplasmic reticulum require a melanocyte-specific factor. J Biol Chem. 2003;278(28):25607–25617. doi:10.1074/jbc.M303411200
   PubMed Web of Science ®Google Scholar
• Garg AD, Kaczmarek A, Krysko O, et al. ER stress-induced inflammation: does it aid or impede disease progression? Trends Mol Med. 2012;18(10):589–598. doi:10.1016/j.molmed.2012.06.010
   PubMed Web of Science ®Google Scholar
• Verfaillie T, Garg AD, Agostinis P. Targeting ER stress induced apoptosis and inflammation in cancer. Cancer Lett. 2013;332(2):249–264. doi:10.1016/j.canlet.2010.07.016
   PubMed Web of Science ®Google Scholar
• Tanaka T, Narazaki M, Kishimoto T. IL-6 in inflammation, immunity, and disease. Cold Spring Harb Perspect Biol. 2014;6(10):a016295–a016295. doi:10.1101/cshperspect.a016295
   PubMed Web of Science ®Google Scholar
• Singh M, Kotnis A, Jadeja SD, et al. Cytokines: the yin and yang of vitiligo pathogenesis. Expert Rev Clin Immunol. 2019;15(2):177–188. doi:10.1080/1744666X.2019.1550358
   PubMed Web of Science ®Google Scholar
• Yu HS, Chang KL, Yu CL, et al. Alterations in IL-6, IL-8, GM-CSF, TNF-alpha, and IFN-gamma release by peripheral mononuclear cells in patients with active vitiligo. J Invest Dermatol. 1997;108(4):527–529. doi:10.1111/1523-1747.ep12289743
   PubMed Web of Science ®Google Scholar
• Toosi S, Orlow SJ, Manga P. Vitiligo-inducing phenols activate the unfolded protein response in melanocytes resulting in upregulation of IL6 and IL8. J Invest Dermatol. 2012;132(11):2601–2609. doi:10.1038/jid.2012.181
   PubMed Web of Science ®Google Scholar
• Mansuri MS, Singh M, Begum R. miRNA signatures and transcriptional regulation of their target genes in vitiligo. J Dermatol Sci. 2016;84(1):50–58. doi:10.1016/j.jdermsci.2016.07.003
   PubMed Web of Science ®Google Scholar
• Xue X, Piao JH, Nakajima A, et al. Tumor necrosis factor alpha (TNFalpha) induces the unfolded protein response (UPR) in a reactive oxygen species (ROS)-dependent fashion, and the UPR counteracts ROS accumulation by TNFalpha. J Biol Chem. 2005;280(40):33917–33925. doi:10.1074/jbc.M505818200
   PubMed Web of Science ®Google Scholar
• Seneschal J, Speeckaert R, Taïeb A, et al. Worldwide expert recommendations for the diagnosis and management of vitiligo: position statement from the international Vitiligo Task Force-Part 2: specific treatment recommendations. J Eur Acad Dermatol Venereol. 2023;37(11):2185–2195. doi:10.1111/jdv.19450
   PubMed Web of Science ®Google Scholar
• Pao HP, Liao WI, Tang SE, et al. Suppression of endoplasmic reticulum stress by 4-PBA protects against hyperoxia-induced acute lung injury via up-regulating claudin-4 expression. Front Immunol. 2021;12:674316. doi:10.3389/fimmu.2021.674316
   PubMed Web of Science ®Google Scholar
• Bhardwaj R, Bhardwaj A, Dhawan DK, et al. 4-PBA rescues hyperoxaluria induced nephrolithiasis by modulating urinary glycoproteins: cross talk between endoplasmic reticulum, calcium homeostasis and mitochondria. Life Sci. 2022;305:120786. doi:10.1016/j.lfs.2022.120786
   PubMed Web of Science ®Google Scholar
• Xing D, Zhou Q, Wang Y, et al. Effects of tauroursodeoxycholic acid and 4-phenylbutyric acid on selenium distribution in mice model with type 1 diabetes. Biol Trace Elem Res. 2023;201(3):1205–1213. doi:10.1007/s12011-022-03193-8
   PubMed Web of Science ®Google Scholar
• Shu S, Zhu J, Liu Z, et al. Endoplasmic reticulum stress is activated in post-ischemic kidneys to promote chronic kidney disease. EBioMedicine. 2018;37:269–280. doi:10.1016/j.ebiom.2018.10.006
   PubMed Web of Science ®Google Scholar
• Ni Q, Ye Z, Wang Y, et al. Gut microbial dysbiosis and plasma metabolic profile in individuals with vitiligo. Front Microbiol. 2020;11:592248. doi:10.3389/fmicb.2020.592248
   PubMed Web of Science ®Google Scholar
• Zalpoor H, Nabi-Afjadi M, Forghaniesfidvajani R, et al. Quercetin as a JAK-STAT inhibitor: a potential role in solid tumors and neurodegenerative diseases. Cell Mol Biol Lett. 2022;27(1):60. doi:10.1186/s11658-022-00355-3
   PubMed Web of Science ®Google Scholar
• Guan C, Xu W, Hong W, et al. Quercetin attenuates the effects of H2O2 on endoplasmic reticulum morphology and tyrosinase export from the endoplasmic reticulum in melanocytes. Mol Med Rep. 2015;11(6):4285–4290. doi:10.3892/mmr.2015.3242
   PubMed Web of Science ®Google Scholar
• Lu L, Wang S, Fu L, et al. Bilobalide protection of normal human melanocytes from hydrogen peroxide-induced oxidative damage via promotion of antioxidase expression and inhibition of endoplasmic reticulum stress. Clin Exp Dermatol. 2016;41(1):64–73. doi:10.1111/ced.12664
   PubMed Web of Science ®Google Scholar
• Ni YH, Deng HF, Zhou L, et al. Ginsenoside Rb1 ameliorated bavachin-induced renal fibrosis via suppressing Bip/eIF2α/CHOP signaling-mediated EMT. Front Pharmacol. 2022;13:872474. doi:10.3389/fphar.2022.872474
   PubMed Web of Science ®Google Scholar
• Nguyen S, Chuah SY, Fontas E, et al. Atorvastatin in combination with narrowband UV-B in adult patients with active vitiligo: a randomized clinical trial. JAMA Dermatol. 2018;154(6):725–726. doi:10.1001/jamadermatol.2017.6401
   PubMed Web of Science ®Google Scholar
• Bian Y, Yu H, Jin M, et al. Repigmentation by combined narrow‑band ultraviolet B/adipose‑derived stem cell transplantation in the mouse model: role of Nrf2/HO‑1‑mediated Ca(2+) homeostasis. Mol Med Rep. 2022;25:1.
   PubMed Web of Science ®Google Scholar