Faculty Opinions recommendation of Comprehensive analysis of the gene encoding filaggrin uncovers prevalent and rare mutations in ichthyosis vulgaris and atopic eczema.

A Turkish boy was referred at the age of 3 6/12 years for the evaluation of a premature moustache. No other signs of virilisation were present. The endocrine evaluation led to the diagnosis of nonclassic congenital adrenal hyperplasia. Genetic analysis revealed 2 rare mutations of theCYP21A2gene, the gene encoding for the 21-hydroxylase enzyme: a recently reported R132C mutation in exon 3 and a R339H mutation in exon 8, both reported in the nonclassic CAH. An early moustache, for which the term premature moustache can be coined, can be the presenting symptom of nonclassic CAH. In all children presenting with a sex or age inappropriate development of a moustache, an endocrine evaluation is indicated.

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FLG mutations in ichthyosis vulgaris and atopic eczema: spectrum of mutations and population genetics

British Journal of Dermatology ◽

10.1111/j.1365-2133.2009.09582.x ◽

2009 ◽

Vol 162 (3) ◽

pp. 472-477 ◽

Cited By ~ 87

Author(s):

M. Akiyama

Keyword(s):

Population Genetics ◽

Atopic Eczema ◽

Ichthyosis Vulgaris

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Stagonospora avenae Secretes Multiple Enzymes that Hydrolyze Oat Leaf Saponins

Molecular Plant-Microbe Interactions ◽

10.1094/mpmi.2000.13.10.1041 ◽

2000 ◽

Vol 13 (10) ◽

pp. 1041-1052 ◽

Cited By ~ 29

Author(s):

John P. Morrissey ◽

Jos P. Wubben ◽

Anne E. Osbourn

Keyword(s):

Antifungal Activity ◽

Leaf Tissue ◽

Phytopathogenic Fungi ◽

Comprehensive Analysis ◽

Gaeumannomyces Graminis ◽

Phytopathogenic Fungus ◽

Gene Encoding ◽

Sugar Chain ◽

Hydrolyzing Enzymes ◽

Hydrolysis Of

The phytopathogenic fungus Stagonospora avenae is able to infect oat leaves despite the presence of avenacoside saponins in the leaf tissue. In response to pathogen attack, avenacosides are converted into 26-desglucoavenacosides (26-DGAs), which possess antifungal activity. These molecules are comprised of a steroidal backbone linked to a branched sugar chain consisting of one α-L-rhamnose and two (avenacoside A) or three (avenacoside B) β-D-glucose residues. Isolates of the fungus that are pathogenic to oats are capable of sequential hydrolysis of the sugar residues from the 26-DGAs. Degradation is initiated by removal of the L-rhamnose, which abolishes antifungal activity. The D-glucose residues are then hydrolyzed by β-glucosidase activity. A comprehensive analysis of saponin-hydrolyzing activities was undertaken, and it was established that S. avenae isolate WAC1293 secretes three enzymes, one α-rhamnosidase and two β-glucosidases, that carry out this hydrolysis. The major β-glucosidase was purified and the gene encoding the enzyme cloned. The protein is similar to saponin-hydrolyzing enzymes produced by three other phytopathogenic fungi, Gaeumannomyces graminis, Septoria lycopersici, and Botrytis cinerea, and is a family 3 β-glucosidase. The gene encoding the β-glucosidase is expressed during infection of oat leaves but is not essential for pathogenicity.

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