title: Lipase maturation factor 1: a lipase chaperone involved in lipid metabolism.
abstract: Mutations in lipase maturation factor 1 (LMF1) are associated with severe hypertriglyceridemia in mice and human subjects. The underlying cause is impaired lipid clearance due to lipase deficiency. LMF1 is a chaperone of the endoplasmic reticulum (ER) and it is critically required for the post-translational activation of three vascular lipases: lipoprotein lipase (LPL), hepatic lipase (HL) and endothelial lipase (EL). As LMF1 is only required for the maturation of homodimeric, but not monomeric, lipases, it is likely involved in the assembly of inactive lipase subunits into active enzymes and/or the stabilization of active dimers. Herein, we provide an overview of current understanding of LMF1 function and propose that it may play a regulatory role in lipase activation and lipid metabolism. Further studies will be required to test this hypothesis and elucidate the full spectrum of phenotypes in combined lipase deficiency. This article is part of a Special Issue entitled Triglyceride Metabolism and Disease.
authors: Medical Genetics Institute, Cedars-Sinai Medical Center, Los Angeles, CA, United States. mpeterfy@ucla.edu
authors: Miklós
authors: M
authors: Péterfy
mesh_terms: D000818:Animals; D005786:Gene Expression Regulation; D006801:Humans; D008049:Lipase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D050356:Lipid Metabolism / Q000235:genetics*; D008052:Lipid Metabolism, Inborn Errors / Q000235:genetics / Q000378:metabolism; D008071:Lipoprotein Lipase / Q000172:deficiency / Q000235:genetics / Q000378:metabolism; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism; D051379:Mice; D018832:Molecular Chaperones; D009154:Mutation; D055503:Protein Multimerization / Q000235:genetics
chemical_list: C546366:LMF1 protein, human; D008565:Membrane Proteins; D018832:Molecular Chaperones; D008049:Lipase; D008071:Lipoprotein Lipase