Degradation of membrane-bound ganglioside GM1. Stimulation by bis(monoacylglycero)phosphate and the activator proteins SAP-B and GM2-AP.

According to our hypothesis (Fürst, W., and Sandhoff, K. (1992) Biochim.

Recombinant GM2-activator protein stimulates in vivo degradation of GA2 in GM2 gangliosidosis AB variant fibroblasts but exhibits no detectable binding of GA2 in an in vitro assay.

The interaction between glycosphingolipids and recombinant human GM2-activator was studied in a microwell binding assay. A-series gangliosides like GM3, GM2 and GM1 were strongly bound by the recombinant human GM2 activator. A weak binding was observed to GD1b and sulfatide, while neutral glycolipids were not bound.

How Does Nature Cleave Sulfuric Acid Esters? A Novel Posttranslational Modification of Sulfatases.

A rare inherited disease, multiple sulfatase deficiency, is attributed to a defect in a posttranslational protein modification which is essential for the catalytic activity of all known sulfatases. Structure analysis of arylsulfatase A, the enzyme that cleaves sulfatide 1, shows that the modification of a cysteine residue into a formylglycine residue is essential for catalytic activity.