Anomeric Structures of Globoside and Ceramide Trihexoside of Human Erythrocytes and Hamster Fibroblasts

Human erythrocyte P and Pk blood group antigens: identification as glycosphingolipids.

Two patients with Fabry's disease were infused with normal plasma to provide active enzyme (ceramide trihexosidase) for hydrolysis of the plasma substrate, galactosylgalactosylglucosylceramide. Maximum ceramide trihexosidase activity occurred 6 hours after infusion of the plasma, attaining a level approximately 150 percent of that in normal plasma; enzymatic activity was detectable for 7 days. The amount of accumulated substrate in the plasma of these recipients decreased about 50 percent on day 10 after infusion. Thus, periodic replacement of ceramide trihexosidase activity in the plasma of patients with Fabry's disease might lead to consistently lower amounts of substrate in the plasma and a decrease in its rate of accumulation in tissues.

Enzyme replacement in Fabry's disease, an inborn error of metabolism.

A procedure is described for the intrauterine detection, at the 17th week of gestation, of a male fetus afflicted with Fabry's disease. The validity of this determination was substantiated by multiple enzyme and lipid analyses of tissue specimens obtained from the afflicted fetus. Fabry's disease may now be included with other X-linked metabolic deficiency diseases that are amenable to precise genetic counseling, through carrier identification, and the monitoring of ensuing pregnancies.

https://science.sciencemag.org/content/sci/172/3979/174.full.pdf

C.E. Griffin

Papers

Chemistry of glycosphingolipids in Fabry's disease