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

• Published in: FEBS letters Vol. 590; no. 6; pp. 716 - 725
• Main Authors: Ferraz, Maria J., Marques, André R. A., Appelman, Monique D., Verhoek, Marri, Strijland, Anneke, Mirzaian, Mina, Scheij, Saskia, Ouairy, Cécile M., Lahav, Daniel, Wisse, Patrick, Overkleeft, Herman S., Boot, Rolf G., Aerts, Johannes M.
• Format: Journal Article
• Language: English
• Published: England 01.03.2016
• Subjects: acid ceramidase; Acid Ceramidase - genetics; Acid Ceramidase - metabolism; Acylation; alpha-Galactosidase - genetics; alpha-Galactosidase - metabolism; Animals; Disease Models, Animal; Fabry disease; Fabry Disease - genetics; Fabry Disease - metabolism; Female; Gaucher disease; Gaucher Disease - genetics; Gaucher Disease - metabolism; globotriaosylsphingosine; Glucosylceramidase - genetics; Glucosylceramidase - metabolism; glucosylsphingosine; glycosphingolipids; Glycosphingolipids - chemistry; Glycosphingolipids - metabolism; HEK293 Cells; Humans; Lysosomes - metabolism; Male; Mice; Mice, Knockout; Fabry disease; glucosylsphingosine; Gaucher disease; globotriaosylsphingosine; glycosphingolipids; acid ceramidase

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...