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Reduction in keratin aggregates in epidermolysis bullosa simplex keratinocytes after pretreatment with trimethylamine N‐oxide
Author(s) -
Bchetnia Mbarka,
Lacroix Jacynthe,
Farez Tarik,
Larouche Miriam,
Powell Julie,
McCuaig Catherine,
Dupéré Audrey,
Morin Charles,
LegendreGuillemin Valérie,
Laprise Catherine
Publication year - 2016
Publication title -
experimental dermatology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.108
H-Index - 96
eISSN - 1600-0625
pISSN - 0906-6705
DOI - 10.1111/exd.12821
Subject(s) - epidermolysis bullosa simplex , dermatology , keratin , epidermolysis bullosa , chemistry , trimethylamine n oxide , trimethylamine , keratin 14 , medicine , pathology , biochemistry , transgene , gene , genetically modified mouse
Epidermolysis bullosa simplex (EBS) is a dominantly inherited skin disease caused by mutations in the keratin 5 (KRT5) or KRT14 genes (1). Some reports suggested that fever and/or hot weather may exacerbate EBS phenotype (2). Effective EBS therapies are still lacking. Molecular chaperones are proteins whose main function is to promote the correct folding of polypeptides (s1). Molecules such as trimethylamine N-oxide (TMAO) and sodium 4-phenylbutyrate (4-PBA) act as chemical chaperones (s2) with protein folding and stabilization activities (s3, s4, s5)