A novel asparagine-->aspartic acid mutation in the rod 1A domain in keratin 2e in a Japanese family with ichthyosis bullosa of Siemens.

Abstract

Ichthyosis bullosa of Siemens is a unique type of congenital ichthyosis characterized by mild hyperkeratosis over the flexural areas and blister formation after mechanical trauma and superficial denuded areas in the hyperkeratotic skin. Recently, mutations in the helix initiation or termination motifs of keratin 2e (KRT2E) have been described in ichthyosis bullosa of Siemens patients. The majority of the mutations reported to date lie in the 2B region. We report a novel amino acid substitution mutation (asparagine-->aspartic acid) in codon 192 at the conserved 1A helix initiation site of the rod domain of KRT2E in a Japanese family with ichthyosis bullosa of Siemens. Our data indicate aspartic acid substitution in codon 192 in the 1A helix initiation site is deleterious to keratin filament network integrity and leads to ichthyosis bullosa of Siemens phenotype.

• Authors: Y Takizawa, M Akiyama, M Nagashima, H Shimizu
• Journal: The Journal of investigative dermatology (J Invest Dermatol) Vol. 114 Issue 1 Pg. 193-5 (Jan 2000) ISSN: 0022-202X [Print] United States
• PMID: 10620137 (Publication Type: Case Reports, Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• KRT2 protein, human
• Keratin-2
• Keratins

Topics

• Amino Acid Sequence (genetics)
• Amino Acid Substitution (genetics)
• Asian People (genetics)
• Base Sequence (genetics)
• Female
• Humans
• Ichthyosis (genetics, pathology)
• Japan
• Keratin-2
• Keratins (genetics)
• Middle Aged
• Molecular Sequence Data
• Mutation (genetics)
• Pedigree
• Skin Diseases, Vesiculobullous (genetics, pathology)