Interaction of saposins, acidic lipids, and glucosylceramidase

• Published in: The Journal of biological chemistry Vol. 265; no. 4; pp. 1933 - 1937
• Main Authors: MORIMOTO, S, KISHIMOTO, Y, TOMICH, J, WEILER, S, OHASHI, T, BARRANGER, J. A, KRETZ, K. A, O'BRIEN, J. S
• Format: Journal Article
• Language: English
• Published: Bethesda, MD American Society for Biochemistry and Molecular Biology 05.02.1990
• Subjects: Analytical, structural and metabolic biochemistry; Biological and medical sciences; Female; Fundamental and applied biological sciences. Psychology; Gangliosides - pharmacology; Glucosidases - metabolism; Glucosylceramidase - metabolism; Glycoproteins - metabolism; Glycoproteins - pharmacology; Humans; Kinetics; Lipids; Lysosomes - enzymology; man; Other biological molecules; Phosphatidylserines - metabolism; Phosphatidylserines - pharmacology; placenta; Placenta - enzymology; Pregnancy; Protein Binding; Proteins - metabolism; saposin; Saposins; Sphingolipid Activator Proteins; Sphingolipids; Human; Ligand binding; Binding capacity; Ganglioside; Enzyme; Sphingolipid; Molecular interaction; Glucosylceramidase; Glycoproteins

Activity of lysosomal glucosylceramidase is stimulated by two small glycoproteins, saposin A and C, which are, together with two other similar glycoproteins, derived from a single precursor protein. This enzyme is also stimulated by naturally occurring acidic lipids, such as phosphatidylserine and g...