A Novel Mutation in ST14 at a Functionally Significant Amino Acid Residue Expands the Spectrum of Ichthyosis-Hypotrichosis Syndrome

December 2017 in “ Orphanet Journal of Rare Diseases ”

Leila Youssefian, Andrew Touati, Amir Hossein Saeidian, Omid Zargari, Sirous Zeinali, Hassan Vahidnezhad, Jouni Uitto

ST14 ichthyosis-hypotrichosis syndrome IHS p.Asp482Asn mutation serine protease matriptase ligand-binding domain histological analysis ultrastructural analysis genotypic characteristics phenotypic characteristics ichthyosis hypotrichosis gene mutation protein activation

A novel homozygous p.Asp482Asn mutation in the ST14 gene, encoding the serine protease matriptase, was identified in a patient with ichthyosis-hypotrichosis syndrome (IHS) from a cohort of 180 ichthyosis patients. This mutation affected a critical ligand-binding domain of matriptase, expanding the known spectrum of IHS pathology. Histological and ultrastructural analyses revealed new features of the disorder, correlating genotypic and phenotypic characteristics and underscoring the clinical significance of the Asp482 residue in matriptase activation.

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A Novel Mutation in ST14 at a Functionally Significant Amino Acid Residue Expands the Spectrum of Ichthyosis-Hypotrichosis Syndrome

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research A Novel Mutation in ST14 at a Functionally Significant Amino Acid Residue Expands the Spectrum of Ichthyosis-Hypotrichosis Syndrome