Cholesterol Binding And Cholesterol Transport Proteins
Cholesterol Binding and CholesterolTransport Proteins
SUBCELLULAR BIOCHEMISTRYSERIES EDITORJ. ROBIN HARRIS, University of Mainz, Mainz, GermanyASSISTANT EDITORP.J. QUINN, King’s College London, London, U.K.Recent Volumes in this SeriesVolume 33 Bacterial Invasion into Eukaryotic CellsTobias A. Oelschlaeger and Jorg HackerVolume 34 Fusion of Biological Membranes and Related ProblemsEdited by Herwig Hilderson and Stefan FullerVolume 35 Enzyme-Catalyzed Electron and Radical TransferAndreas Holzenburg and Nigel S. ScruttonVolume 36 Phospholipid Metabolism in ApoptosisEdited by Peter J. Quinn and Valerian E. KaganVolume 37 Membrane Dynamics and DomainsEdited by P.J. QuinnVolume 38 Alzheimer’s Disease: Cellular and Molecular Aspects of Amyloid betaEdited by R. Harris and F. FahrenholzVolume 39 Biology of Inositols and PhosphoinositidesEdited by A. Lahiri Majumder and B.B. BiswasVolume 40 Reviews and Protocols in DT40 ResearchEdited by Jean-Marie Buerstedde and Shunichi TakedaVolume 41 Chromatin and DiseaseEdited by Tapas K. Kundu and Dipak DasguptaVolume 42 Inflammation in the Pathogenesis of Chronic DiseasesEdited by Randall E. HarrisVolume 43 Subcellular ProteomicsEdited by Eric Bertrand and Michel FaupelVolume 44 Peroxiredoxin SystemsEdited by Leopold Flohd J. Robin HarrisVolume 45 Calcium Signalling and DiseaseEdited by Ernesto Carafoli and Marisa BriniVolume 46 Creatine and Creatine Kinase in Health and DiseaseEdited by Gajja S. Salomons and Markus WyssVolume 47 Molecular Mechanisms of Parasite InvasionEdited by Barbara A. Burleigh and Dominique Soldati-FavreVolume 48 The Coronin Family of ProteinsEdited by Christoph S. Clemen, Ludwig Eichinger and Vasily RybakinVolume 49 Lipids in Health and DiseaseEdited by Peter J. Quinn and Xiaoyuan WangVolume 50 Genome Stability and Human DiseasesEdited by Heinz Peter Nasheuer
J. Robin HarrisEditorCholesterol Binding andCholesterol TransportProteinsStructure and Function in Health and Disease123
EditorProf. J. Robin Harris11 Hackwood ParkHexham, NorthumberlandUnited Kingdom NE46 1AXTel. (00)44 (0)1434 606981ISBN 978-90-481-8621-1e-ISBN 978-90-481-8622-8DOI 10.1007/978-90-481-8622-8Springer Dordrecht Heidelberg London New YorkLibrary of Congress Control Number: 2010921984 Springer Science Business Media B.V. 2010No part of this work may be reproduced, stored in a retrieval system, or transmitted in any form or byany means, electronic, mechanical, photocopying, microfilming, recording or otherwise, without writtenpermission from the Publisher, with the exception of any material supplied specifically for the purposeof being entered and executed on a computer system, for exclusive use by the purchaser of the work.Printed on acid-free paperSpringer is part of Springer Science Business Media (www.springer.com)
INTERNATIONAL ADVISORY EDITORIAL BOARDR. BITTMAN, Queens College, City University of New York, New York, USAD. DASGUPTA, Saha Institute of Nuclear Physics, Calcutta, IndiaL. FLOHE, MOLISA Gmbh, Magdeburg, GermanyH. HERRMANN, German Cancer Research Center, Heidelberg, GermanyA. HOLZENBURG, Texas A&M University, Texas, USAH-P. NASHEUER, National University of Ireland, Galway, IrelandS. ROTTEM, The Hebrew University, Jerusalem, IsraelM. WYSS, DSM Nutritional Products Ltd., Basel, Switzerland
FrontispieceAn electron micrograph showing a negatively stained cholesterol microcrystal, surface-decorated with Pyolysin domain 4 fragment (the cholesterol-bindingdomain), The underlying crystalline cholesterol imposes the quasi 2-dimensionalcrystal lattice of the Pyolysin domain 4 molecules (J. Robin Harris and MichaelPalmer, previously unpublished data).vii
PrefaceThis book was conceived as a result of the long-standing interest of the Editorin structural and functional aspects of cholesterol, most particularly in relationto the formation and experimental use of aqueous suspensions of cholesterolmicrocrystals, and the role of cholesterol in Alzheimer’s disease and for the studyof the cholesterol-dependent cytolysins (see Frontispiece and Chapters 2 and 20to 22). It also serves as an extension from the earlier volume in the SubcellularBiochemistry series, dealing with “Cholesterol: Its Functions and Metabolism inBiology and Medicine” (Vol. 28, ed. Robert Bittman, 1997). Although the theme ofcellular membranes and cholesterol-rich plasma membrane “raft” domains appearsseveral times throughout the book, the chapters within the book fall loosely intotwo sections; the opening group concentrate primarily upon soluble proteins thatbind cholesterol and the later chapters place emphasis on membrane-bound proteinsand membrane-active toxins that have an affinity for cholesterol. Throughout thereis a strong emphasis on fundamental cellular and biochemical aspects, in particulardetailed considerations of membrane “raft” domains, as well as clinical/pathologicalconditions involving deviant cholesterol metabolism and homeostasis.The opening chapter is by Gerald Gimple, who presents a detailed accounton cholesterol reporter molecules for the study of cholesterol-protein interactions.This chapter serves well as an Introduction for the book and provides a thorough technical survey, whilst at the same time introducing the recurring theme ofcholesterol-containing membrane “raft” domains. Thus, this opening chapter linkswell with topics presented in several of the subsequent chapters. Then, my colleagueNathaniel Milton and I present a survey of the role of cholesterol in Alzheimer’s disease and other amyloidogenic disorders. This is a rapidly advancing field, currentlynot without some controversy, yet may ultimately prove to be of considerable significance, particularly if clinical benefit can be proven following cholesterol loweringby statins. Several viral proteins have the ability to bind cholesterol. This topic iscovered by Cornelia Schroeder, who considers HIV and influenza virus proteinsfrom a strong molecular stance. Emma de Fabiani and colleagues then present adetailed survey on sterol-protein interactions in cholesterol and bile acid biosynthesis. The role of bile acids in metabolic signalling is give due emphasis. Although thecholesterol oxidases have been most intensively studies in bacterial systems, theirlikely importance in animals can be predicted in view of the bioreactivity of oxidizedix
xPrefacecholesterol products. Alice Vrierlink provides a detailed account of the structureand enzymic mechanism of the bacterial cholesterol oxidases. Appropriately, theoxysterol-binding proteins are then dealt with by Neale D. Ridgeway, who placesemphasis upon the eukaryotic oxysterol binding protein (OSBP) family. The roleof high density lipoprotein (HDL) in reverse cholesterol transport is given a thorough handling by Sissel Lund-Katz and Michael C. Phillips, who deal with theapolipoprotein components in depth. The topic of lipoprotein modification anduptake by macrophages, within the context of the pathologic role of cholesterolin atherosclerosis, is reviewed in detail by Yury I. Miller and colleagues. The nextchapter, by Richard M. Epand and colleagues provides a thorough overview onthe involvement of cholesterol in membrane-related phenomena. Under the title of:Cholesterol Interaction with Proteins that Partition into Membrane Domains, theseauthors provide a useful link between all the following chapters that have an emphasis on cell membrane cholesterol. The topic of intracellular cholesterol transport ishandled by Fiedhelm Schroeder and colleagues, who place emphasis on caveolinand sterol carrier protein-2 in relation to cholesterol-rich microdomains. NiemannPick type C (NPC) disease is a cholesterol storage disease due to a defined geneticlesion. Xiaoning Bi and Guanghong Liao review recent achievements in the investigation of the disruption of cholesterol homeostasis-induced neurodegeneration inNPC disease, and provide new insight into the development of a potential therapeutic strategy. Sterol transport across the intestinal brush border membrane is mediatedby a number of proteins. J. Mark Brown and Liqing Yu survey this complex situation,the first line of cholesterol entry into and passage across the intestinal enterocytesand the animal body, which can have a major impact upon atherosclerotic cardiovascular disease. The role of cholesterol in the endoplasmic reticulum (ER) is presentedby Teruo Hayashi and Tsung-Ping Su, who place emphasis upon the sigma-1 receptor chaperones and other ER proteins in relation to the diverse ER functions, suchas protein folding, compartmentalization and segregation of ER proteins, and sphingolipid biosynthesis. Denis Corbeil and colleagues then give a thorough accounton Prominin-1, a distinct cholesterol-binding protein of the apical plasma membrane of epithelial cells. The StAR-related lipid transfer (START) domain is anevolutionary conserved protein. This topic is presented by Pierre Lavigne and colleagues, who review the understanding of the structure and reversible cholesterolbinding mechanism of START domains. The role of membrane cholesterol in thefunction of G-protein coupled receptors (GPCRs) is handled by Yamuna Devi Pailaand Amitabha Chattopadhyay. These authors consider that deciphering moleculardetails of the GPCR-cholesterol interaction in the membrane should lead to better insight into the overall understanding of GPCR function in health and disease.Francisco J Barrantes then discusses cellular aspects of the role of cholesterol inthe nicotinic acetylcholine receptor (AchR). Indeed, the cholesterol content of theplasmalemma may homeostatically modulate AChR dynamics, cell-surface organization and the lifetime of receptor nanodomains, in turn exerting control over theion permeation process. The brain contains the highest content of cholesterol of allorgans of the animal body, largely contained in myelinated nerves. In their chapter on cholesterol and myelin biogeneis, Gesine Saher and Mikael Simons consider
Prefacexithe role of cholesterol in both the central and peripheral nervous system. The diversity of plasma membrane ion channels is almost overwhelming! Irena Levitan andcolleagues present a thorough account of the role of cholesterol in regulation ofthe major types of ion channels and discuss this in the context of the current models for channel function. As indicated above, the cholesterol-dependent cytolysins(CDCs) are toxin molecules of great personal interest. This topic is covered with astrong molecular slant by Alejandro P. Heuck and colleagues, in their chapter on thecholesterol-dependent cytolysin family of Gram-positive bacterila toxins. Evidencefor the role of cholesterol in the activity and pore-formation by a range of otherβ-barrel pore-forming Gram-negative bacterial toxins is covered by my colleagueMichael Palmer and myself. The final chapter, by Yoshiko Ohno-Iwashita and colleagues expands upon themes introduced earlier, in relation to the value of havingspecific probes for cholesterol localization. These authors describe in detail studiesusing non-cytolytic molecular fragments of the CDC perfringolysin, together withanti-cholesterol antibodies, as tools for membrane cholesterol localization.Overall, when compiling the contents of this book I have attempted to includealmost all topics of significance, and have been greatly encouraged by the positiveresponses I have received from the chapter authors, from the early contacts thoroughto the preparation of the chapter manuscripts for publication.Hexham, UKJ. Robin Harris
Contents1 Cholesterol–Protein Interaction: Methods and CholesterolReporter Molecules . . . . . . . . . . . . . . . . . . . . . . . . . . .Gerald Gimpl12 Cholesterol in Alzheimer’s Disease and otherAmyloidogenic Disorders . . . . . . . . . . . . . . . . . . . . . . .J. Robin Harris and Nathaniel G.N. Milton473 Cholesterol-Binding Viral Proteins in Virus Entry andMorphogenesis . . . . . . . . . . . . . . . . . . . . . . . . . . . . .Cornelia Schroeder774 Sterol–Protein Interactions in Cholesterol and BileAcid Synthesis . . . . . . . . . . . . . . . . . . . . . . . . . . . . .Emma De Fabiani, Nico Mitro, Federica Gilardi, andMaurizio Crestani1095 Cholesterol Oxidase: Structure and Function . . . . . . . . . . . .Alice Vrielink1376 Oxysterol-Binding Proteins . . . . . . . . . . . . . . . . . . . . . .Neale D. Ridgway1597 High Density Lipoprotein Structure–Function and Role inReverse Cholesterol Transport . . . . . . . . . . . . . . . . . . . .Sissel Lund-Katz and Michael C. Phillips8 Lipoprotein Modification and Macrophage Uptake: Role ofPathologic Cholesterol Transport in Atherogenesis . . . . . . . . .Yury I. Miller, Soo-Ho Choi, Longhou Fang, andSotirios Tsimikas9 Cholesterol Interaction with Proteins That Partition intoMembrane Domains: An Overview . . . . . . . . . . . . . . . . . .Richard M. Epand, Annick Thomas, Robert Brasseur, andRaquel F. Epand183229253xiii
xiv10ContentsCaveolin, Sterol Carrier Protein-2, MembraneCholesterol-Rich Microdomains and IntracellularCholesterol Trafficking . . . . . . . . . . . . . . . . . . . . . . . . .Friedhelm Schroeder, Huan Huang, Avery L. McIntosh,Barbara P. Atshaves, Gregory G. Martin, and Ann B. Kier11Cholesterol in Niemann–Pick Type C disease . . . . . . . . . . . .Xiaoning Bi and Guanghong Liao12Protein Mediators of Sterol Transport Across IntestinalBrush Border Membrane . . . . . . . . . . . . . . . . . . . . . . .J. Mark Brown and Liqing Yu1314151617Cholesterol at the Endoplasmic Reticulum: Roles of theSigma-1 Receptor Chaperone and Implications thereof inHuman Diseases . . . . . . . . . . . . . . . . . . . . . . . . . . . .Teruo Hayashi and Tsung-Ping SuProminin-1: A Distinct Cholesterol-Binding MembraneProtein and the Organisation of the Apical PlasmaMembrane of Epithelial Cells . . . . . . . . . . . . . . . . . . . . .Denis Corbeil, Anne-Marie Marzesco, Christine A. Fargeas,and Wieland B. HuttnerMammalian StAR-Related Lipid Transfer (START)Domains with Specificity for Cholesterol: StructuralConservation and Mechanism of Reversible Binding . . . . . . . .Pierre Lavigne, Rafael Najmanivich, and Jean-Guy LeHoux279319337381399425Membrane Cholesterol in the Function and Organizationof G-Protein Coupled Receptors . . . . . . . . . . . . . . . . . . . .Yamuna Devi Paila and Amitabha Chattopadhyay439Cholesterol Effects on Nicotinic Acetylcholine Receptor:Cellular Aspects . . . . . . . . . . . . . . . . . . . . . . . . . . . .Francisco J. Barrantes46718Cholesterol and Myelin Biogenesis . . . . . . . . . . . . . . . . . .Gesine Saher and Mikael Simons48919Cholesterol and Ion Channels . . . . . . . . . . . . . . . . . . . . .Irena Levitan, Yun Fang, Avia Rosenhouse-Dantsker, andVictor Romanenko50920The Cholesterol-Dependent Cytolysin Familyof Gram-Positive Bacterial Toxins . . . . . . . . . . . . . . . . . . .Alejandro P. Heuck, Paul C. Moe, and Benjamin B. Johnson551Cholesterol Specificity of Some Heptameric β-BarrelPore-Forming Bacterial Toxins: Structural and Functional AspectsJ. Robin Harris and Michael Palmer57921
Contents22Cholesterol-Binding Toxins and Anti-cholesterol Antibodiesas Structural Probes for Cholesterol Localization . . . . . . . . . .Yoshiko Ohno-Iwashita, Yukiko Shimada, Masami Hayashi,Machiko Iwamoto, Shintaro Iwashita, and Mitsushi InomataIndex . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .xv597623
ContributorsBarbara P. Atshaves Department of Physiology and Pharmacology, Texas A&MUniversity, TVMC College Station, TX 77843-4, USAFrancisco J. Barrantes UNESCO Chair of Biophysics and MolecularNeurobiology and Instituto de Investigaciones Bioquímicas de Bahía Blanca, C.C.857, B8000FWB Bahía Blanca, ArgentinaXiaoning Bi Department of Basic Medical Sciences, COMP, Western Universityof Health Sciences, Pomona, CA 91766, USA, xbi@westernu.eduRobert Brasseur Centre de Biophysique Moléculaire Numérique, AgroBiotech ofGembloux, ULg, Passage des déportés, 2, 5030 Gembloux, BelgiumJ. Mark Brown Department of Pathology Section on Lipid Sciences, Wake ForestUniversity School of Medicine, Winston-Salem, NC, USAAmitabha Chattopadhyay Centre for Cellular and Molecular Biology, Council ofScientific and Industrial Research, Uppal Road, Hyderabad 500 007, IndiaSoo-Ho Choi Department of Medicine, University of California, San Diego,La Jolla, CA 92037-0682, USADenis Corbeil Tissue Engineering Laboratories, BIOTEC, Technische UniversitätDresden, Tatzberg 47-49, 01307 Dresden, GermanyMaurizio Crestani “Giovanni Galli” Laboratory of Biochemistry and MolecularBiology of Lipids, Department of Pharmacological Sciences, Via Balzaretti, 9,20133 Milan, ItalyRaquel F. Epand Department of Biochemistry and Biomedical Sciences,McMaster University, Hamilton, Ontario L8N 3Z5, CanadaRichard M. Epand Department of Biochemistry and Biomedical Sciences,McMaster University, Hamilton, Ontario L8N 3Z5, Canada, epand@mcmaster.caEmma De Fabiani “Giovanni Galli” Laboratory of Biochemistry and MolecularBiology of Lipids, Department of Pharmacological Sciences, Via Balzaretti, 9,20133 Milan, Italy, emma.defabiani@unimi.itxvii
xviiiContributorsLonghou Fang Department of Medicine, University of California, San Diego,La Jolla, CA 92037-0682, USAYun Fang Institute for Medicine and Engineering, University of Pennsylvania,3340 Smith Walk, Philadelphia, PA, USAChristine A. Fargeas Tissue Engineering Laboratories, BIOTEC, TechnischeUniversität Dresden, Tatzberg 47-49, 01307 Dresden, GermanyFederica Gilardi “Giovanni Galli” Laboratory of Biochemistry and MolecularBiology of Lipids, Department of Pharmacological Sciences, Via Balzaretti, 9,20133 Milan, ItalyGerald Gimpl Institut für Biochemie, Johannes Gutenberg-University of Mainz,Johann-Joachim-Becherweg 30, D-55128 Mainz, Germany, Gimpl@uni-mainz.deJ. Robin Harris Institute of Zoology, University of Mainz, D-55099 Mainz,Germany and Institute of Cell and Molecular Biosciences, University ofNewcastle, Newcastle-upon-Tyne, NE2 4HH, UK, rharris@uni-mainz.deMasami Hayashi Research Team for Functional Genomics, Tokyo MetropolitanInstitute of Gerontology, 35-2 Sakae-cho, Itabashi-ku, Tokyo 173-0015, JapanTeruo Hayashi Cellular Pathobiology Section, Cellular Neurobiology ResearchBranch, Intramural Research Program, National Institute on Drug Abuse,Department of Health and Human Services, National Institutes of Health, 333Cassell Drive, Baltimore, Maryland 21224, USAAlejandro P. Heuck Department of Biochemistry and Molecular Biology,University of Massachusetts, Amherst, MA 01003, USAHuan Huang Department of Physiology and Pharmacology, Texas A&MUniversity, TVMC College Station, TX 77843-4, USAWieland B. Huttner Max-Planck-Institute of Molecular Cell Biology andGenetics, Pfotenhauerstrasse 108, 01307 Dresden, GermanyMitsushi Inomata Research Team for Functional Genomics, Tokyo MetropolitanInstitute of Gerontology, 35-2 Sakae-cho, Itabashi-ku, Tokyo 173-0015, JapanMachiko Iwamoto Research Team for Functional Genomics, Tokyo MetropolitanInstitute of Gerontology, 35-2 Sakae-cho, Itabashi-ku, Tokyo 173-0015, JapanShintaro Iwashita Faculty of Pharmacy, Iwaki Meisei University, 5-5-1 ChuodaiIino, Iwaki City, Fukushima 970-8551, JapanBenjamin B. Johnson Department of Biochemistry and Molecular Biology,University of Massachusetts, Amherst, MA 01003, USAAnn B. Kier Department of Pathobiology, Texas A&M University, TVMC,College Station, TX 77843-4467, USA
ContributorsxixPierre Lavigne Département de Pharmacologie, Institut de Pharmacologie,Faculté de médecine et des sciences de la santé, Université de Sherbrooke 3001 12eAvenue Nord, Sherbrooke, QC, Canada J1H 5N4Jean-Guy LeHoux Département de Biochimie, Faculté de médecine et dessciences de la santé, Université de Sherbrooke, 3001 12e Avenue Nord,Sherbrooke, QC, Canada J1H 5N4Irena Levitan Department of Medicine, Sections of Pulmonary, Critical Care andSleep Medicine, University of Illinois at Chicago, 840 S Wood St, Chicago60612, USAGuang
Springer is part of Springer Science Business Media (www.springer.com) . tigation of the disruption of cholesterol homeostasis-induced neurodegeneration in NPC disease, and provide new insight into the development of a potential therapeu- . Methods and Cholesterol Reporter Molecules.
blockage forms in a narrowed artery, heart attack or stroke can result. High-Density Lipoprotein (HDL) or Good Cholesterol - The Bad Cholesterol Eater About one-fourth to one-third of blood cholesterol is carried by HDL. HDL cholesterol is known as "good" cholesterol, because high levels of HDL seem to protect against heart attack.
Cholesterol is a waxy, fat-like substance found in the body. The body uses cholesterol to create hormones and substances to digest food. The body produces enough cholesterol to complete all functions cholesterol is needed for. Cholesterol is also found in many foods. There are two different types of ch
Transport Management System of Nepal Nepalese transport management is affected by existing topographical condition of the country. Due to this only means of transport used in the country are road transport and air transport. In this paper only road transport is discussed. During the Tenth Plan period, the vehicle transport management
The øX174 DNA binding protein contains two DNA binding domains, containing a series of DNA binding basic amino acids, separated by a proline-rich linker region. Within each DNA binding domain, there is a conserved glycine residue. Glycine and proline residues were mutated and the effects on virion structure were examined.
d Mutational disruption of DNA binding to XRCC1 impairs recruitment to DNA damage d Disruption of DNA binding by XRCC1 impairs repair of DNA single-strand breaks . observed perturbations upon DNA binding occurred in residues that were not strongly affected by PAR (Figure 2C), suggesting that the DNA and PAR molecules were binding to distinct .
To further quantify the SA2 binding specificity for DNA ends, we applied analysis the based on the fractional occupancies of SA2 at DNA ends (46). SA2 binding specificities for DNA ends (S DNA binding constant for specific sites/DNA binding constant for nonspecific sites K SP/K NSP) are 2945 ( 77), 2604 ( 68), and 2129 ( 76),
bridge and late-binding design. Figure 2: Network stacks to illustrate the changes made to the Linux to implement late-binding. 1. Minimize or eliminate packet bu ering below the bind-ing point. A consequence is that after the binding, the packet is almost immediately sent on the air. 2. Keep ows in separate queues above the binding point
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