NDLI: Acid sphingomyelinase activity is regulated by membrane lipids and facilitates cholesterol transfer by NPC2

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Oninla, Vincent O. Breiden, Bernadette Babalola, Jonathan O. Sandhoff, Konrad
Description	Country affiliation: Nigeria Author Affiliation: Oninla VO ( LIMES Institute, Membrane Biology and Lipid Biochemistry Unit, Kekulé-Institut für Organische Chemie und Biochemie, Universität Bonn, D-53121 Bonn, Germany Department of Chemistry, University of Ibadan, Ibadan, Nigeria.); Breiden B ( LIMES Institute, Membrane Biology and Lipid Biochemistry Unit, Kekulé-Institut für Organische Chemie und Biochemie, Universität Bonn, D-53121 Bonn, Germany.); Babalola JO ( Department of Chemistry, University of Ibadan, Ibadan, Nigeria.); Sandhoff K ( LIMES Institute, Membrane Biology and Lipid Biochemistry Unit, Kekulé-Institut für Organische Chemie und Biochemie, Universität Bonn, D-53121 Bonn, Germany.)
Abstract	During endocytosis, membrane components move to intraluminal vesicles of the endolysosomal compartment for digestion. At the late endosomes, cholesterol is sorted out mainly by two sterol-binding proteins, Niemann-Pick protein type C (NPC)1 and NPC2. To study the NPC2-mediated intervesicular cholesterol transfer, we developed a liposomal assay system. (Abdul-Hammed, M., B. Breiden, M. A. Adebayo, J. O. Babalola, G. Schwarzmann, and K. Sandhoff. 2010. Role of endosomal membrane lipids and NPC2 in cholesterol transfer and membrane fusion. J. Lipid Res. 51: 1747-1760.) Anionic lipids stimulate cholesterol transfer between liposomes while SM inhibits it, even in the presence of anionic bis(monoacylglycero)phosphate (BMP). Preincubation of vesicles containing SM with acid sphingomyelinase (ASM) (SM phosphodiesterase, EC 3.1.4.12) results in hydrolysis of SM to ceramide (Cer), which enhances cholesterol transfer. Besides SM, ASM also cleaves liposomal phosphatidylcholine. Anionic phospholipids derived from the plasma membrane (phosphatidylglycerol and phosphatidic acid) stimulate SM and phosphatidylcholine hydrolysis by ASM more effectively than BMP, which is generated during endocytosis. ASM-mediated hydrolysis of liposomal SM was also stimulated by incorporation of diacylglycerol (DAG), Cer, and free fatty acids into the liposomal membranes. Conversely, phosphatidylcholine hydrolysis was inhibited by incorporation of cholesterol, Cer, DAG, monoacylglycerol, and fatty acids. Our data suggest that SM degradation by ASM is required for physiological secretion of cholesterol from the late endosomal compartment, and is a key regulator of endolysosomal lipid digestion.
File Format	HTM / HTML
ISSN	00222275
e-ISSN	15397262
DOI	10.1194/jlr.M054528
Journal	The Journal of Lipid Research
Issue Number	12
Volume Number	55
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2014-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Biochemistry Cholesterol Metabolism Endosomes Lipid Bilayers Models, Biological Sphingomyelin Phosphodiesterase Sphingomyelins Vesicular Transport Proteins Animals Biological Transport Endocytosis Chemistry Enzymology Hydrolysis Micelles Phosphatidic Acids Phosphatidylcholines Phosphatidylglycerols Recombinant Proteins Genetics Unilamellar Liposomes Up-regulation Comparative Study Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Endocrinology

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