Point mutation of Arg440 to His in cytochrome P450c17 causes severe 17 alpha-hydroxylase deficiency

J Clin Endocrinol Metab. 1994 Jul;79(1):160-4. doi: 10.1210/jcem.79.1.8027220.

Abstract

Genetic disorders in the gene encoding P450c17 cause 17 alpha-hydroxylase deficiency. The consequent defects in the synthesis of cortisol and sex steroids cause sexual infantilism and a female phenotype in both genetic sexes as well as mineralocorticoid excess and hypertension. A 15-yr-old patient from Germany was seen for absent pubertal development and mild hypertension with hypokalemia, high concentrations of 17-deoxysteroids, and hypergonadotropic hypogonadism. Analysis of her P450c17 gene by polymerase chain reaction amplification and direct sequencing showed mutation of codon 440 from CGC (Arg) to CAC (His). Expression of a vector encoding this mutated form of P450c17 in transfected nonsteroidogenic COS-1 cells showed that the mutant P450c17 protein was produced, but it lacked both 17 alpha-hydroxylase and 17,20-lyase activities. To date, 15 different P450c17 mutations have been described in 23 patients with 17 alpha-hydroxylase deficiency, indicating that mutations in this gene are due to random events.

Publication types

  • Case Reports
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adolescent
  • Adrenal Hyperplasia, Congenital*
  • Arginine / genetics*
  • Base Sequence
  • Cell Line
  • Female
  • Germany
  • Histidine / genetics*
  • Humans
  • Hypertension / etiology
  • Hypokalemia / etiology
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Point Mutation*
  • Polymerase Chain Reaction
  • Steroid 17-alpha-Hydroxylase / genetics*
  • Steroid 17-alpha-Hydroxylase / metabolism
  • Transfection

Substances

  • Histidine
  • Arginine
  • Steroid 17-alpha-Hydroxylase