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http://purl.uniprot.org/citations/7554313http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7554313http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7554313http://www.w3.org/2000/01/rdf-schema#comment"

Unlabelled

The molecular basis for male pseudohermaphroditism produced by the 5 alpha-reductase deficiency is becoming increasingly understood.

Objective

We have performed biochemical and molecular analyses of the 5 alpha-reductase type 2 gene in a Turkish family with a 5 alpha-reductase deficiency.

Patient

A 46,XY prepubertal Turkish patient with female phenotype showing clitoral hypertrophy, high plasma testosterone and dihydrotestosterone, and normally differentiated and developed testosterone-dependent internal genitalia.

Measurements

5 alpha-Reductase activity, measured by the conversion of 3H-T into 5 alpha-reduced compounds, was determined from cultured genital skin fibroblasts by both intact monolayer assay and cell-free extracts at various pH values. The five exons of the 5 alpha-reductase type 2 gene were sequenced after enzymatic amplification (PCR) of the patient's genomic DNA. Labelled PCR of the consanguineous parents' DNA was submitted to electrophoresis on a sequencing gel.

Results

A marked decrease in the transformation of T into 5 alpha-reduced compounds by intact cells and a diminished 5 alpha-reductase activity at acidic pH by sonicated cell extracts strongly suggested a 5 alpha-reductase type 2 deficiency. Molecular analysis of the 5 alpha-reductase type-2 gene showed a trinucleotide deletion straddling codons 156 and 157, responsible for a methionine residue deletion at position 157 of the protein. The parents' DNA contained both normal and deleted alleles.

Conclusions

This is the third deletion described in the 5 alpha-reductase type 2 gene. The deleted methionine 157 is conserved in both types 1 and 2 of human and rat 5 alpha-reductase, which suggests its crucial role in the functioning of the enzyme. This gene rearrangement was thus clearly responsible for the reduced 5 alpha-reductase activity and abnormal genital development in this patient."xsd:string
http://purl.uniprot.org/citations/7554313http://purl.org/dc/terms/identifier"doi:10.1111/j.1365-2265.1995.tb01913.x"xsd:string
http://purl.uniprot.org/citations/7554313http://purl.org/dc/terms/identifier"doi:10.1111/j.1365-2265.1995.tb01913.x"xsd:string
http://purl.uniprot.org/citations/7554313http://purl.uniprot.org/core/author"Belon C."xsd:string
http://purl.uniprot.org/citations/7554313http://purl.uniprot.org/core/author"Belon C."xsd:string
http://purl.uniprot.org/citations/7554313http://purl.uniprot.org/core/author"Boudon C."xsd:string
http://purl.uniprot.org/citations/7554313http://purl.uniprot.org/core/author"Boudon C."xsd:string
http://purl.uniprot.org/citations/7554313http://purl.uniprot.org/core/author"Lobaccaro J.-M."xsd:string
http://purl.uniprot.org/citations/7554313http://purl.uniprot.org/core/author"Lobaccaro J.-M."xsd:string
http://purl.uniprot.org/citations/7554313http://purl.uniprot.org/core/author"Lumbroso S."xsd:string
http://purl.uniprot.org/citations/7554313http://purl.uniprot.org/core/author"Lumbroso S."xsd:string
http://purl.uniprot.org/citations/7554313http://purl.uniprot.org/core/author"Sultan C."xsd:string
http://purl.uniprot.org/citations/7554313http://purl.uniprot.org/core/author"Sultan C."xsd:string
http://purl.uniprot.org/citations/7554313http://purl.uniprot.org/core/author"Ogur G."xsd:string
http://purl.uniprot.org/citations/7554313http://purl.uniprot.org/core/author"Ogur G."xsd:string
http://purl.uniprot.org/citations/7554313http://purl.uniprot.org/core/author"Ocal G."xsd:string
http://purl.uniprot.org/citations/7554313http://purl.uniprot.org/core/author"Ocal G."xsd:string
http://purl.uniprot.org/citations/7554313http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7554313http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7554313http://purl.uniprot.org/core/name"Clin. Endocrinol. (Oxf.)"xsd:string
http://purl.uniprot.org/citations/7554313http://purl.uniprot.org/core/name"Clin. Endocrinol. (Oxf.)"xsd:string
http://purl.uniprot.org/citations/7554313http://purl.uniprot.org/core/pages"183-188"xsd:string
http://purl.uniprot.org/citations/7554313http://purl.uniprot.org/core/pages"183-188"xsd:string
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