Carnitine is a pharmacological allosteric chaperone of the human lysosomal α-glucosidase

J Enzyme Inhib Med Chem. 2021 Dec;36(1):2068-2079. doi: 10.1080/14756366.2021.1975694.

Abstract

Pompe disease is an inherited metabolic disorder due to the deficiency of the lysosomal acid α-glucosidase (GAA). The only approved treatment is enzyme replacement therapy with the recombinant enzyme (rhGAA). Further approaches like pharmacological chaperone therapy, based on the stabilising effect induced by small molecules on the target enzyme, could be a promising strategy. However, most known chaperones could be limited by their potential inhibitory effects on patient's enzymes. Here we report on the discovery of novel chaperones for rhGAA, L- and D-carnitine, and the related compound acetyl-D-carnitine. These drugs stabilise the enzyme at pH and temperature without inhibiting the activity and acted synergistically with active-site directed pharmacological chaperones. Remarkably, they enhanced by 4-fold the acid α-glucosidase activity in fibroblasts from three Pompe patients with added rhGAA. This synergistic effect of L-carnitine and rhGAA has the potential to be translated into improved therapeutic efficacy of ERT in Pompe disease.

Keywords: carbohydrate active enzymes; glycogen storage disease type 2; lysosomal disease; orphan drugs; α-Glucosidase.

MeSH terms

  • Allosteric Regulation / drug effects
  • Carnitine / chemistry
  • Carnitine / pharmacology*
  • Dose-Response Relationship, Drug
  • Glycoside Hydrolase Inhibitors / chemistry
  • Glycoside Hydrolase Inhibitors / pharmacology*
  • Humans
  • Lysosomes / drug effects*
  • Lysosomes / enzymology
  • Molecular Chaperones / chemistry
  • Molecular Chaperones / pharmacology*
  • Molecular Structure
  • Structure-Activity Relationship
  • alpha-Glucosidases / metabolism*

Substances

  • Glycoside Hydrolase Inhibitors
  • Molecular Chaperones
  • alpha-Glucosidases
  • Carnitine

Grants and funding

Nadia Minopoli is supported by PON Dottorati Innovativi con Caratterizzazione Industriale, Ministero Università e Ricerca (MIUR).