19 research outputs found
The Arabidopsis thaliana lysophospholipid acyltransferase At1g78690p acylates a variety of lysophospholipids including bis(monoacylglycero)phosphate
No full text
Production of Bis(monoacylglycero)phosphate from Phosphatidylglycerol in Isolated Liver Lysosomes of Chloroquine-Pretreated Rats
No full text
Transferase and hydrolase activities of phospholipase D from the roots ofAconitum arcuatum
No full text
A lipid associated with the antiphospholipid syndrome regulates endosome structure and function
No full textLittle is known about the structure and function of membrane domains in the vacuolar apparatus of animal cells. A unique feature of late endosomes, which are part of the pathway that leads to lysosomes, is that they contain a complex system of poorly characterized internal membranes in their lumen. These endosomes are therefore known as multivesicular or multilamellar organelles(1,2). Some proteins distribute preferentially within these internal membranes, whereas others are exclusively localized to the organelle's limiting membrane(3). The composition and function of this membrane system are poorly understood. Here we show that these internal membranes contain large amounts of a unique lipid, and thus form specialized domains within endosomes, These specialized domains are involved in sorting the multifunctional receptor(4) for insulin-like growth factor 2 and ligands bearing mannose-6-phosphate, in particular lysosomal enzymes, We also show that this unique lipid is a specific antigen for human antibodies associated with the antiphospholipid syndrome(5,6). These antibodies may act intracellularly by altering the protein-sorting functions of endosomes
