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Detection of Glycosaminoglycans by Polyacrylamide Gel Electrophoresis and Silver Staining
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Detection of Glycosaminoglycans by Polyacrylamide Gel Electrophoresis and Silver Staining

Published on: February 25, 2021

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Molecular characteristics of patients with glycosaminoglycan storage disorders in Russia

Dimitry A Chistiakov1, Kirill V Savost'anov2, Lyudmila M Kuzenkova3

  • 1Department of Medical Nanobiotechnology, Pirogov Russian State Medical University, 117997 Moscow, Russia; Department of Molecular Genetic Diagnostics, Division of Laboratory Medicine, Institute of Pediatrics, Research Center for Children's Health, 119991 Moscow, Russia.

Clinica Chimica Acta; International Journal of Clinical Chemistry
|May 31, 2014
PubMed
Abstract

Insights

This study identified five novel mutations in mucopolysaccharidoses (MPS) patients, enhancing understanding of these rare genetic disorders. The findings detail specific genetic variants and their impact on enzyme function.

Area of Science:

  • Biochemistry
  • Genetics
  • Molecular Biology

Background:

  • Mucopolysaccharidoses (MPS) are rare genetic disorders.
  • Caused by mutations in lysosomal enzymes crucial for glycosaminoglycans (GAGs) degradation.
  • Study analyzed 48 patients across MPS I, II, IIIA, IVA, and VI types.

Purpose of the Study:

  • To identify and characterize novel mutations in MPS patients.
  • To functionally assess the impact of identified mutations on enzyme activity.
  • To expand the knowledge of the genetic basis of various MPS types.

Main Methods:

  • Colorimetric and fluorimetric assays for urinary GAGs and enzyme activity.
  • Sequencing of exons and intronic flanks for IDUA, IDS, SGSH, GALNS, and ARSB genes.
  • Functional assessment using site-directed mutagenesis, cell expression (CHO cells), enzymatic assays, and Western blot analysis.

Main Results:

  • Identified five novel mutations: p.Asn348Lys (IDUA), p.Tyr240Cys (GALNS), and three ARSB mutations (p.Gln110*, p.Asn262Lysfs*14, pArg315*).
  • Mutations p.Asn348Lys, p.Asn262Lysfs*14, and p.Gln110* resulted in undetectable mutant protein and <1% enzyme activity.
  • p.Tyr240Cys showed trace protein with 3.6% activity; pArg315* yielded a truncated protein with 7.9% activity.

Conclusions:

  • The identified mutations contribute to the genetic diversity of MPS disorders.
  • Functional analyses confirm the pathogenic nature of the novel variants.
  • Findings enrich the understanding of genotype-phenotype correlations in MPS.
Keywords:
Enzyme activityGlycosaminoglycansMucopolysaccharidosesMutation

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