Immunohistological study of tight junction protein expression in mal de Meleda

References

• Bouadjar B, Benmazouzia S, Prud’homme JF, et al. Clinical and genetic studies of 3 large, consanguineous, Algerian families with mal de Meleda. Arch Dermatol 2000;136(10):1247–52.
   PubMedGoogle Scholar
• Charfeddine C, Mokni M, Ben Mousli R, et al. A novel missense mutation in the gene encoding SLURP-1 in patients with mal de Meleda from northern Tunisia. Br J Dermatol 2003;149(6):1108–15.
   PubMed Web of Science ®Google Scholar
• Charfeddine C, Mokni M, Kassar S, et al. Further evidence of the clinical and genetic heterogeneity of recessive transgressive PPK in the Mediterranean region. J Hum Genet 2006;51:841–5.
   PubMed Web of Science ®Google Scholar
• Bchetnia M, Merdassi A, Charfeddine C, et al. Coexistence of mal de Meleda and congenital cataract in a consanguineous Tunisian family: Two case reports. J Med Case Rep 2010;4:108.
   PubMedGoogle Scholar
• Bchetnia M, Laroussi N, Youssef M, et al. Particular mal de Meleda phenotypes in Tunisia and mutations founder effect in the Mediterranean region. Biomed Res Int 2013;2013:206803.
   PubMed Web of Science ®Google Scholar
• Ward KM, Yerebakan O, Yilmaz E, Celebi JT. Identification of recurrent mutations in the ARS (component B) gene encoding SLURP-1 in two families with mal de Meleda. J Invest Dermatol. 2003;120:96–8.
   PubMed Web of Science ®Google Scholar
• Perez C, Khachemoune A. Mal de Meleda: A focused review. Am J Clin Dermatol. 2016;17(1):63–70.
   Web of Science ®Google Scholar
• Frenk E, Guggisberg D, Mevorah B, et al. Meleda disease: Report of two cases investigated by electron microscopy. Dermatology 1996;193:358–61.
   PubMed Web of Science ®Google Scholar
• Fischer J, Bouadjar B, Heilig R, et al. Mutations in the gene encoding SLURP-1 in mal de Meleda. Hum Mol Genet 2001;10(8):875–80.
   PubMed Web of Science ®Google Scholar
• Chimienti F, Hogg RC, Plantard L, et al. Identification of SLURP-1 as an epidermal neuromodulator explains the clinical phenotype of mal de Meleda. Hum Mol Genet 2003;12:3017–24.
   PubMed Web of Science ®Google Scholar
• Arredondo J, Nguyen VT, Chernyavsky AI, et al. Central role of alpha7 nicotinic receptor in differentiation of the stratified squamous epithelium. J Cell Biol 2002;159:325–36.
   PubMed Web of Science ®Google Scholar
• Kurzen H, Berger H, Jager C, et al. Phenotypical and molecular profiling of the extraneuronal cholinergic system of the skin. J Invest Dermatol 2004;123:937–49.
   PubMed Web of Science ®Google Scholar
• Pummi K, Malminen M, Aho H, et al. Epidermal tight junctions: ZO-1 and occludin are expressed in mature, developing, and affected skin, and in vitro differentiating keratinocytes. J Invest Dermatol 2001;117:1050–8.
   PubMed Web of Science ®Google Scholar
• Brandner JM, Kief S, Grund C, et al. Organization and formation of the tight junction system in human epidermis and cultured keratinocytes. Eur J Cell Biol 2002;81:253–63.
   PubMed Web of Science ®Google Scholar
• Furuse M, Hata M, Furuse K, et al. Claudin-based tight junctions are crucial for the mammalian epidermal barrier: A lesson from claudin-1-deficient mice. J Cell Biol 2002;156:1099–111.
   PubMed Web of Science ®Google Scholar
• Troy TC, Rahbar R, Arabzadeh A, et al. Delayed epidermal permeability barrier formation and hair follicle aberrations in Inv-Cldn6 mice. Mech Dev 2005;122:805–19.
   PubMed Web of Science ®Google Scholar
• Morita K, Miyachi Y. Tight junctions in the skin. J Dermatol Sci 2003;31:81–9.
   PubMed Web of Science ®Google Scholar
• Peltonen S, Riehokainen J, Pummi K, et al. Tight junction components occludin, ZO-1, and claudin-1, -4 and -5 in active and healing psoriasis. Br J Dermatol 2007;156:466–72.
   PubMed Web of Science ®Google Scholar
• Yuki T, Haratake A, Koishikawa H, et al. Tight junction proteins in keratinocytes: Localization and contribution to barrier function. Exp Dermatol 2007;16:324–30.
   PubMed Web of Science ®Google Scholar
• Kirschner N, Brandne, JM. Barriers and more: Functions of tight junction proteins in the skin. Ann NY Acad Sci 2012;1257:158–66.
   PubMed Web of Science ®Google Scholar
• Brandner JM, Zorn-Kruppa M, Yoshida T, et al. Epidermal tight junctions in health and disease. Tissue Barriers 2015;3:1–2.
   Google Scholar
• Yoshida Y, Kazumasa M, Akira M, Chizuka I, Yoshiki M. Altered expression of occludin and tight junction formation in psoriasis. Arch Dermatol Res 2001;293:239–44.
   PubMed Web of Science ®Google Scholar
• Raiko L, Pekka Leinonen, Päivi M. Hägg, Juha Peltonen, Aarne Oikarinen, Sirkku Peltonen. Tight junctions in Hailey-Hailey and Darier’s diseases. Dermatol Rep 2009;1:1.
   Google Scholar
• Kassar S, Charfeddine C, Zribi H, et al. Immunohistological study of involucrin expression in Darier’s disease skin. J Cutan Path 2008;35(7):635–40.
   PubMed Web of Science ®Google Scholar
• Sakakibara A, Furuse M, Saitou M, et al. Possible involvement of phosphorylation of occludin in tight junction formation. J Cell Biol 1997;137:393–1401.
   Web of Science ®Google Scholar
• Hartsock A, James Nelson W. Adherens and tight junctions: Structure, function and connections to the actin cytoskeleton. Biochim Biophys Acta 2008;1778:660–9.
   PubMed Web of Science ®Google Scholar
• Gonzalez-Mariscal L, Tapia R, Chamorro D. Crosstalk of tight junction components with signaling pathways. Biochim Biophys Acta 2008;1778:729–56.
   PubMed Web of Science ®Google Scholar
• Youssef G, Gerner L, Naeem AS, et al. Rab3Gap1 mediates exocytosis of Claudin-1 and tight junction formation during epidermal barrier acquisition. Dev Biol 2013;380(2):274–85.
   PubMed Web of Science ®Google Scholar
• Findley MK, Koval M. Regulation and roles for claudin family tight junction proteins. IUBMB Life 2009;61:431–7.
   PubMed Web of Science ®Google Scholar
• Kirschner N, Claudia Bohner, Susanne Rachow, et al. Tight junctions: Is there a role in dermatology. Arch Dermatol Res 2010;302:483–93.
   PubMed Web of Science ®Google Scholar
• Mertens AEE, Rygiel TP, Olivo C, et al. The Rac activator Tiam1 controls tight junction biogenesis in keratinocytes through binding to and activation of the Par polarity complex. J Cell Biol 2005;170:1029–37.
   PubMed Web of Science ®Google Scholar
• Helfrich I, Schmitz A, Zigrino P, et al. Role of aPKC isoforms and their binding partners Par3 and Par6 in epidermal barrier formation. J Invest Dermatol 2006;127:782–91.
   PubMed Web of Science ®Google Scholar
• Mastrangeli R, Donini S, Kelton CA, et al. ARS Component B: Structural characterization, tissue expression and regulation of the gene and protein (SLURP-1) associated with mal de Meleda. Eur J Dermatol 2003;13(6):560–70.
   PubMed Web of Science ®Google Scholar
• Chernyavsky AI, Arredondo J, Galitovskiy V, et al. Upregulation of nuclear factor-kappaB expression by SLURP-1 is mediated by alpha7-nicotinic acetylcholine receptor and involves both ionic events and activation of protein kinases. Am J Physiol Cell Physiol 2010;299(5):C903–11.
   PubMed Web of Science ®Google Scholar