Prosaposin deficiency: further characterization of the sphingolipid activator protein-deficient sibs. Multiple glycolipid elevations (including lactosylceramidosis), partial enzyme deficiencies and ultrastructure of the skin in this generalized sphingolipid storage disease

Hum Genet. 1993 Sep;92(2):143-52. doi: 10.1007/BF00219682.

Abstract

Sphingolipid activator protein (SAP) deficiency, previously described in two sibs and shown to be caused by the absence of the common saposin precursor (prosaposin), was further characterized by biochemical lipid and enzyme studies and by ultrastructural analysis. The 20-week-old fetal sib had increased concentrations of neutral glycolipids, including mono-, di-, tri- and tetrahexosylceramide, in liver, kidney and cultured skin fibroblasts compared with the controls. Glucosylceramide and lactosylceramide were particularly elevated. The kidney of the affected fetus showed additional increases in the concentration of sulphatide, galactosylceramide and digalactosylceramide. Free ceramide was stored in the liver and kidney, and GM3 and GM2 gangliosides were elevated in the liver, but not the brain, of the fetus. Phospholipids, however, were normal in the affected fetus. In the liver biopsy of the propositus, who later died at 16 weeks of age, only a few lipids could be studied. Glucosylceramide, dihexosylceramide and ceramide were elevated in agreement with our previous study. Enzyme studies were undertaken using detergent-free liposomal substrate preparations and fibroblast extracts. The sibs' beta-glucocerebrosidase and beta-galactocerebrosidase activities were clearly reduced, but their sphingomyelinase activities were normal. The normal activity of the latter enzyme and the almost normal tissue concentration of sphingomyelin in prosaposin deficiency suggest that the prosaposin-derived SAPs are not required for sphingomyelinase activity in vivo. In keeping with the biochemical findings, skin biopsies from the sibs showed massive lysosomal storage with a vesicular and membranous ultrastructure. The function of SAPs in sphingolipid degradation and the role of SAPs for enzyme activity in vitro are discussed. In addition, the similarity in neutral glycolipid accumulations in Niemann-Pick disease type C and in prosaposin deficiency are noted. The phenotype of the prosaposin deficient sibs resembled acute neuronopathic (type 2) Gaucher disease more than Farber disease in several aspects, but their genotype was unique.

Publication types

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

MeSH terms

  • Brain Chemistry
  • Ceramides / metabolism
  • Chromatography, Thin Layer
  • Enzyme Activation
  • Fetal Diseases / metabolism
  • Fetal Diseases / pathology
  • Fibroblasts / metabolism
  • Gangliosides / metabolism
  • Glycolipids / metabolism
  • Glycoproteins / deficiency*
  • Glycosphingolipids / metabolism
  • Humans
  • Infant, Newborn
  • Kidney / metabolism
  • Liposomes / metabolism
  • Liver / metabolism
  • Lysosomes / ultrastructure
  • Male
  • Protein Precursors / deficiency*
  • Saposins
  • Skin / metabolism
  • Skin / ultrastructure
  • Sphingolipidoses / metabolism*
  • Sphingolipidoses / pathology*
  • Sulfoglycosphingolipids / metabolism

Substances

  • Ceramides
  • Gangliosides
  • Glycolipids
  • Glycoproteins
  • Glycosphingolipids
  • Liposomes
  • PSAP protein, human
  • Protein Precursors
  • Saposins
  • Sulfoglycosphingolipids