Lysosomal glycosphingolipid catabolism by acid ceramidase: formation of glycosphingoid bases during deficiency of glycosidases

FEBS Lett. 2016 Mar;590(6):716-25. doi: 10.1002/1873-3468.12104. Epub 2016 Mar 3.

Abstract

Glycosphingoid bases are elevated in inherited lysosomal storage disorders with deficient activity of glycosphingolipid catabolizing glycosidases. We investigated the molecular basis of the formation of glucosylsphingosine and globotriaosylsphingosine during deficiency of glucocerebrosidase (Gaucher disease) and α-galactosidase A (Fabry disease). Independent genetic and pharmacological evidence is presented pointing to an active role of acid ceramidase in both processes through deacylation of lysosomal glycosphingolipids. The potential pathophysiological relevance of elevated glycosphingoid bases generated through this alternative metabolism in patients suffering from lysosomal glycosidase defects is discussed.

Keywords: Fabry disease; Gaucher disease; acid ceramidase; globotriaosylsphingosine; glucosylsphingosine; glycosphingolipids.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acid Ceramidase / genetics
  • Acid Ceramidase / metabolism*
  • Acylation
  • Animals
  • Disease Models, Animal
  • Fabry Disease / genetics
  • Fabry Disease / metabolism*
  • Female
  • Gaucher Disease / genetics
  • Gaucher Disease / metabolism*
  • Glucosylceramidase / genetics
  • Glucosylceramidase / metabolism
  • Glycosphingolipids / chemistry
  • Glycosphingolipids / metabolism*
  • HEK293 Cells
  • Humans
  • Lysosomes / metabolism
  • Male
  • Mice
  • Mice, Knockout
  • alpha-Galactosidase / genetics
  • alpha-Galactosidase / metabolism

Substances

  • Glycosphingolipids
  • GLA protein, human
  • alpha-Galactosidase
  • Glucosylceramidase
  • ASAH1 protein, human
  • Acid Ceramidase