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| http://dx.doi.org/10.1042/bj3100359b | DOI Listing |
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Mechanism of low density lipoprotein (LDL) release in the endosome: implications of the stability and Ca2+ affinity of the fifth binding module of the LDL receptor.
J Biol Chem
August 2008
Biocomputation and Complex Systems Physics Institute (BIFI), Universidad de Zaragoza, 50009 Zaragoza, Spain.
Uptake of low density lipoproteins (LDL) by their receptor, LDLR, is the primary mechanism by which cells incorporate cholesterol from plasma. Mutations in LDLR lead to familial hypercholesterolemia, a common disease affecting 1 in 500 of the human population. LDLR is a modular protein that uses several small repeats to bind LDL.
View Article and Find Full Text PDFStructure and physiologic function of the low-density lipoprotein receptor.
Annu Rev Biochem
September 2005
Life Sciences Division, Korea Institute of Science and Technology, Seoul 136-791, Korea.
The low-density lipoprotein receptor (LDLR) is responsible for uptake of cholesterol-carrying lipoprotein particles into cells. The receptor binds lipoprotein particles at the cell surface and releases them in the low-pH environment of the endosome. The focus of the current review is on biochemical and structural studies of the LDLR and its ligands, emphasizing how structural features of the receptor dictate the binding of low-density lipoprotein (LDL) and beta-migrating forms of very low-density lipoprotein (beta-VLDL) particles, how the receptor releases bound ligands at low pH, and how the cytoplasmic tail of the LDLR interfaces with the endocytic machinery.
View Article and Find Full Text PDFTransient remnant removal disease in acute fatty liver of pregnancy.
Hypertens Pregnancy
October 2004
Department of Obstetrics and Gynecology, University of Freiburg, Freiburg, Germany.
Objective: To elucidate the potential role of an altered lipid metabolism in the pathophysiology of acute fatty liver of pregnancy (AFLP).
Case Report: We report on two otherwise healthy women in the 34th gestational week who presented with symptoms of AFLP. Besides characteristic symptoms like nausea, abdominal pain, highly elevated serum amino transferase levels, and increased creatinine concentrations, the patients' clotting system showed consumption and/or decreased synthesis of coagulation factors.
A two-module region of the low-density lipoprotein receptor sufficient for formation of complexes with apolipoprotein E ligands.
Biochemistry
February 2004
Department of Pathology, Brigham and Women's Hospital and Harvard Medical School, 77 Avenue Louis Pasteur, Boston, Massachusetts 02115, USA.
The low-density lipoprotein (LDL) receptor transports two different classes of cholesterol-carrying lipoprotein particles into cells: LDL particles, which contain a single copy of apolipoprotein B-100 (apoB-100), and beta-migrating very low-density lipoprotein (beta-VLDL) particles, which contain multiple copies of apolipoprotein E (apoE). The ligand-binding domain of the receptor lies at its amino-terminal end within seven adjacent LDL-A repeats (LA1-LA7). Although prior work clearly establishes that LA5 is required for high-affinity binding of particles containing apolipoprotein E (apoE), the number of ligand-binding repeats sufficient to bind apoE ligands has not yet been determined.
View Article and Find Full Text PDFRemnant lipoprotein particles are taken up into myocardium through VLDL receptor--a possible mechanism for cardiac fatty acid metabolism.
Biochem Biophys Res Commun
May 2002
Tohoku University Gene Research Center, Sendai, Japan
The VLDL (very low-density lipoprotein) receptor is a peripheral lipoprotein receptor expressing in fatty acid active tissues abundantly. In the Balb/c fasting mice, VLDL receptor as well as LPL (lipoprotein lipase), FAT (fatty acid translocase)/CD36, H-FABP (heart-type fatty acid-binding protein), ACS (acyl-CoA synthetase) and LCAD (long-chain acyl-CoA dehydrogenase) expressions increased. An electron microscopic examination indicated the lipid droplets that accumulated in the hearts of fasting Balb/c mice.
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