Short stature in two siblings heterozygous for a novel bioinactive GH mutant (GH-P59S) suggesting that the mutant also affects secretion of the wild-type GH

Eur J Endocrinol. 2013 Feb 15;168(3):K35-43. doi: 10.1530/EJE-12-0847. Print 2013 Mar.

Abstract

Objective: Short stature caused by biologically inactive GH is clinically characterized by lack of GH action despite normal-high secretion of GH, pathologically low IGF1 concentrations and marked catch-up growth on GH replacement therapy.

Design and methods: Adopted siblings (girl and a boy) of unknown family history were referred for assessment of short stature (-4.5 and -5.6 SDS) at the age of 10 and 8.1 years respectively. They had delayed bone ages (6.8 and 4.5 years), normal GH peaks at stimulation tests, and severely reduced IGF1 concentrations (-3.5 and -4.0 SDS). Genetic analysis of the GH1 gene showed a heterozygous P59S mutation at position involved in binding to GH receptor (GHR).

Results: Isoelectric focusing analysis of secreted GH in patient serum revealed the presence of higher GH-P59S peak compared with that of wt-GH. Furthermore, computational simulation of GH-P59S binding to GHR suggested problems in correct binding of the mutant to the GHR. In vitro GHR binding studies revealed reduced binding affinity of GH-P59S for GHR (IC₅₀, 30 ng/ml) when compared with the wt-GH (IC₅₀, 11.8 ng/ml) while a significantly decreased ability of the mutant to activate the Jak2/Stat5 signaling pathway was observed at physiological concentrations of 25-100 ng/ml.

Conclusions: The clinical and biochemical data of our patients support the diagnosis of partial bioinactive GH syndrome. The higher amount of GH-P59S secreted in their circulation combined with its impact on the wt-GH function on GHR binding and signaling may alter GHR responsiveness to wt-GH and could ultimately explain severe short stature found in our patients.

Publication types

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

MeSH terms

  • Amino Acid Substitution
  • Body Height*
  • Child
  • Female
  • Heterozygote
  • Hormone Replacement Therapy
  • Human Growth Hormone / deficiency*
  • Human Growth Hormone / genetics*
  • Human Growth Hormone / metabolism
  • Humans
  • Insulin-Like Growth Factor I / analysis
  • Male
  • Models, Molecular
  • Mutation*
  • Protein Conformation
  • Protein Interaction Domains and Motifs
  • Receptors, Somatotropin / metabolism
  • Siblings

Substances

  • Receptors, Somatotropin
  • Human Growth Hormone
  • Insulin-Like Growth Factor I