A novel substitution in keratin 10 in epidermolytic hyperkeratosis

Détails

ID Serval
serval:BIB_1F047608BC02
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
A novel substitution in keratin 10 in epidermolytic hyperkeratosis
Périodique
Journal of Investigative Dermatology
Auteur⸱e⸱s
Arin  M. J., Longley  M. A., Anton-Lamprecht  I., Kurze  G., Huber  M., Hohl  D., Rothnagel  J. A., Roop  D. R.
ISSN
0022-202X (Print)
Statut éditorial
Publié
Date de publication
04/1999
Volume
112
Numéro
4
Pages
506-8
Notes
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S. --- Old month value: Apr
Résumé
Epidermolytic hyperkeratosis is characterized by tonofilament clumping, cytolysis, and blister formation in suprabasal keratinocytes. It has been shown that the tonofilament aggregates in these areas are composed of keratin 1 (K1) and keratin 10 (K10), and several K1 and K10 point mutations have been identified as the molecular basis of epidermolytic hyperkeratosis. In this report we identify a novel, single base pair substitution resulting in an amino acid exchange from tyrosine to serine at residue 14 within the conserved 1A region of K10 (Y14S). This A to C transversion in codon 160 was only present in the affected individual and was associated with a very severe disease phenotype. Our observations are in agreement with previous reports documenting that this tyrosine residue, located at the beginning of the rod domain of type I keratins, is particularly sensitive to amino acid substitutions, and that alterations in this residue can have deleterious effects on filament assembly and stability.
Mots-clé
Child, Preschool Female Humans Hyperkeratosis, Epidermolytic/*genetics/pathology Keratin-10 Keratins/chemistry/*genetics Male *Point Mutation
Pubmed
Web of science
Open Access
Oui
Création de la notice
25/01/2008 16:36
Dernière modification de la notice
20/08/2019 12:55
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