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Fluorescence Studies on Biological Membranes PDF

479 Pages·1988·11.866 MB·English
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Subcellular Biochemistry 13 Volume Fluorescence Studies on Biological Membranes SERIES EDITOR J. R. HARRIS, North East Thames Regional Transfusion Centre, Brentwood, Essex, England ASSISTANT EDITORS H. J. HILDERSON, University of Antwerp, Antwerp, Belgium J. J. M. BERGERON, McGill University, Montreal, Canada INTERNATIONAL ADVISORY EDITORIAL BOARD J. L. AVILA, Institutode Biomedicina, Caracas, Venezuela B. B. BISWAS, Bose Institute, Calcutta, India N. BORGESE, CNR Center for Pharmacological Study, Milan, Italy M. J. COSTELLO, Duke University Medical Center, Durham, North Carolina, USA N. CRAWFORD, Royal College of Surgeons, London, England C. de DUVE, International Institute of Cellular and Molecular Pathology, Brussels, Belgium A.-H. ETEMADI, University of Paris VI, Paris, France W. H. EVANS, National Institute for Medical Research, London, England H. GLAUMANN, Karolinska Institute, Huddinge, Sweden D. R. HEADON, University College Galway, Galway, Ireland P. L. J(Z)RGENSEN, University of Aarhus, Aarhus, Denmark J. KIM, Osaka University, Osaka, Japan J. B. LLOYD, University of Keele, Keele, England J. A. LUCY, Royal Free Hospital School of Medicine, London, England A. H. MADDY, University of Edinburgh, Edinburgh, Scotland A. MONNERON, Institut Pasteur, Paris, France D.J. MORRE, Purdue University, West Lafayette, Indiana, USA M. OSBORNE, Max Planck Institute for Biophysical Chemistry, G6ttingen, FRG P. QUINN, King's College London, London, England G. RALSTON, The University of Sydney, Sydney, Australia S. ROTTEM, The Hebrew University, Jerusalem, Israel M. R. J. SALTON, New York University Medical Center, New York, New York, USA G. SCHATTEN, University of Wisconsin-Madison, Madison, Wisconsin, USA F. S. SJOSTRAND, University of California, Los Angeles, Los Angeles, California, USA T. TAKAHASHI, Aichi Cancer Center, Nagoya, Japan G. B. WARREN, Imperial Cancer Research Fund, London, England F. WUNDERLICH, University of Dusseldorf, Dusseldorf, FRG G. ZAMPIGHI, University of California, Los Angeles, Los Angeles, California, USA I. B. ZBARSKY, Academy of Sciences of the USSR, Moscow, USSR A Continuation Order Plan is available for this series. A continuation order wiD bring delivery of each new volume immediately upon publication. Volumes are billed only upon actual shipment. For further informa tion please contact the publisher. Subcellular Biochemistry 13 Volume Fluorescence Studies on Biological Membranes Edited by H. J. Hilderson University of Antwerp Antwerp, Belgium Series Editor J. R. Harris North East Thames Regional Transfusion Centre Brentwood, Essex, England PLENUM PRESS • NEW YORK AND LONDON The Library of Congress cataloged the fust volume of this title as follows: SulH:ellular biochemistry. London, New York, Plenum Press. v. illus. 23 cm. quarterly. Began with Sept. 1971 issue. Cf. New serial titles. 1. Cytochemistry - Periodicals. 2. Cell organelles - Periodicals. QH611.S84 574.8'76 73-643479 ISBN-13: 978-1-4613-9361-0 e-ISBN-13: 978-1-4613-9359-7 DOl: 10.1007/978-1-4613-9359-7 This series is a continuation of the journal Sub-Cellular Biochemistry, Volumes 1 to 4 of which were published quarterly from 1972 to 1975 © 1988 Plenum Press, New York A Division of Plenum Publishing Corporation 233 Spring Street, New York, N.Y. 10013 Softcover reprint of the hardcover 1st edition 1988 All rights reserved No part of this book may be reproduced, stored in a retrieval system, or transmitted in any form or by any means, electronic, mechanical, photocopying, microfilming, recording, or otherwise, without written permission from the Publisher Contributors Edward Blatt Division of Applied Organic Chemistry, CSIRO, Melbourne, Victoria 3001, Australia Robert Blumenthal National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892 Nor Chejanovsky Institute of Life Sciences, The Hebrew University of Je rusalem, Jerusalem 91904, Israel Jeffrey Clarke Division of Molecular Biology and Biochemistry, School of Basic Life Sciences, University of Missouri, Kansas City, Missouri 64110- 2499 Hugo Depauw RUCA-Laboratory for Human Biochemistry, University of Antwerp, B2020 Antwerp, Belgium Marc De Wolf RUCA-Laboratory for Human Biochemistry, University of Antwerp, B2020 Antwerp, Belgium Wilfried Dierick RUCA-Laboratory for Human Biochemistry, University of Antwerp, B2020 Antwerp, Belgium Jacques Gallay Laboratoire pour l'Utilisation du Rayonnement Electro magnetique (L.U.R.E.)-CNRS-CEA-MEN, Universite Paris-Sud, 91405 Orsay-Cedex, France Jose-Carlos Garcia-Borron Division of Molecular Biology and Biochemis try, School of Basic Life Sciences, University of Missouri, Kansas City, Missouri 64110-2499 Jose-Manuel Gonzalez-Ros Division of Molecular Biology and Biochemis try, School of Basic Life Sciences, University of Missouri, Kansas City, Missouri 64110-2499 Josef Gut Stanford University, Stanford, California 94025 Herwig Hilderson RUCA-Laboratory for Human Biochemistry, University of Antwerp, B2020 Antwerp, Belgium v vi Contributors Akira Ikegami Institute of Physical and Chemical Research, Wako-shi, Sai tama 351-01, Japan Kazuhiko Kinosita, Jr. Institute of Physical and Chemical Research, Wako shi, Saitama 351-01, Japan Tsutomu Kouyama Institute of Physical and Chemical Research, Wako-shi, Saitama 351-01, Japan Barbara C. Kunz National Institutes of Health, Bethesda, Maryland 20205 Albert Lagrou RUCA-Laboratory for Human Biochemistry, University of Antwerp, B2020 Antwerp, Belgium Joseph R. Lakowicz Department of Biological Chemistry, School of Medi cine, University of Maryland, Baltimore, Maryland 21201 Abraham Loyter Institute of Life Sciences, The Hebrew University of Jeru salem, Jerusalem 91904, Israel Marino Martinez-Carrion Division of Molecular Biology and Biochemistry, School of Basic Life Sciences, University of Missouri, Kansas City, Mis souri 64110-2499 Ofer Nussbaum Institute of Life Sciences, The Hebrew University of Jeru salem, Jerusalem 91904, Israel P. Proulx Department of Biochemistry, School of Medicine, Faculty of Health Sciences, University of Ottawa, Ottawa, Ontario K1H 8M5, Canada Christoph Richter Laboratory of Biochemistry, Swiss Federal Institute of Technology, Zurich CH-8092, Switzerland William H. Sawyer Russell Grimwade School of Biochemistry, University of Melbourne, Parkville, Victoria 3052, Australia Elsie M. B. Sorensen Department of Pharmacology and Toxicology, College of Pharmacy, University of Texas, Austin, Texas 78712 Hisako Urabe Institute of Physical and Chemical Research, Wako-shi, Sai tama 351-01, Japan Wim J. van Blitterswijk Division of Cellular Biochemistry, The Netherlands Cancer Institute, Antoni van Leeuwenhoek-Huis, 1066CX Amsterdam, The Netherlands B. Wieb Van der Meer Department of Physics and Astronomy, Western Kentucky University, Bowling Green, Kentucky 42101 Guido Van Dessel VIA-Laboratory for Pathological Biochemistry, University of Antwerp, B2020 Antwerp, Belgium Contributors vii Michel Vincent Laboratoire pour l'Utilisation du Rayonnement Electro magnetique (L.U.R.E.)-CNRS-CEA-MEN, Universite Paris-Sud, 91405 Orsay-Cedex, France Preface As stated by its first editor, Dr. D. B. Roodyn, the primary goal of the series Subcellular Biochemistry is to achieve an integrated view of the cell by bringing together results from a wide range of different techniques and disciplines. This volume deals with the applications of fluorescence spectroscopy to membrane research. It seeks to present complementary biochemical and bio physical data on both the structure and the dynamics of biological membranes. Biophysics and biochemistry are improving more and more in their ability to study biomembranes, overlapping somewhat in this area and explaining the functioning of the whole cell in terms of the properties of its individual com ponents. Therefore, we have brought together an international group of experts in order to report on and review advances in fluorescence studies on biological membranes, thereby highlighting subcellular aspects. The first chapters present a critical evaluation of the current applications of dynamic and steady-state fluorescence techniques. Subsequent chapters dis cuss more specific applications in cells, biological membranes, and their con stituents (lipids, proteins). This volume opens with a chapter by B. Wieb Van der Meer addressing two questions: (1) What are the relevant parameters that describe membrane structure and dynamics? (2) What are the various fluorescence techniques for measuring these parameters? After updating our knowledge of the theoretical aspects and providing a critical evaluation of examples giving insight into the physical state, composition, and functions of membranes, the author concludes that fluorescence can often only demonstrate a correlation between a physical and a functional parameter. By showing the way of thinking that must be fol lowed by everyone working in this area, this chapter becomes a must for those starting research in this field. If, however, the reader is discouraged by a more physical treatment of the subject, he or she is referred to Chapter 2, by Kazuhiko Kinosita, Jr., and Akira Ikegami, dealing with the optical anisotropy decay method (in particular, fluo rescence depolarization and absorption and phosphorescence anisotropy decay). As a less theoretical and more visual description of the interactions in bio- ix x Preface membranes, DNA, and actin and myosin filaments, this chapter can serve as an introduction. The aim of the authors is not to be exhaustive but rather to explain what can be learned from optical anisotropy decay. According to them, it is a powerful means of studying the structure of a key molecule incorporated into a higher-order structure. They conclude that "molecular machines" work ing in living organisms appear to be highly flexible and that the whole machine, as well as its parts, undergoes continual fluctuations. Time-resolved data are usually obtained by measurements of the time dependent emission from samples excited with brief pulses of light. In Chapter 3, Joseph R. Lakowicz describes an alternative method in which the time resolved emission is determined from the frequency response of the emission to intensity-modulated light. The examples include the resolution of closely spaced lifetimes, measurement of complex decays of fluorescence anisotropy, and cal culation of time-resolved emission spectra from the wavelength-dependent fre quency of the sample. A new application is described by which the distribution of distances between two sites on a flexible molecule can be recovered. Ac cording to the author, correlation times as short as 8 psec can be measured. An excellent and profound review of the use of probes to study the effects of sterols and unsaturation on the lipid order parameter in biomembranes has been written by Michel Vincent and Jacques Gallay. In Chapter 4, the authors focus on the use of pulse fluorescence anisotropy techniques to investigate the effect of cholesterol and its derivatives on membrane lipid order and dynamics. Fluorescence lifetimes are extremely sensitive to the environment, but until recently they were very difficult to interpret with certainty. Very recent analysis methods (the maximum entropy method) are expected to allow a precise de scription of the multiexponential behavior of the total fluorescence decay in terms of a continuous distribution of excited-state lifetimes. The authors believe that the advent of such a powerful tool calls for a systematic reevaluation of probe behavior in membranes and other systems. Fluorescence polarization results also provide valuable insights into ion membrane interactions. Based on a recognition of the inherent limitations of fluorescence polarization procedures, Elsie M. B. Sorensen summarizes in Chapter 5 a portion of the scientific data base on ion-membrane interactions. The prev alence of reported studies on calcium-induced alterations of membrane fluidity results in our having more data for calcium than for other ions. From this study ratios of ions appear to be important, as does ionic charge, ionic radius, and binding affinity to the components of the plasma membrane. The author con cludes that much research remains to be done to elucidate the interactions of a complex mixture of extracellular ions with plasma membranes. Moreover, ionic interactions with the internal surface of the phospholipid bilayer might prove to be as important as those with the external surface. Preface xi In Chapter 6, Hugo Depauw et al. apply fluorescence polarization proce dures to the study of the fluidity of thyroid plasma membranes, bringing together biophysical methods and subcellular biochemistry. The isolation of enriched plasma membrane fractions and subfractions is described. From reconstitution experiments, it becomes clear that both lipids and proteins display a major effect on thyroid membrane fluidity, SDPH being mainly affected by neutral lipids and Ddiff being more sensitive to proteins. The authors demonstrate that adenylate cyclase activity can be modulated by manipulating the plasma membrane com position (incorporation of phospholipids, gangliosides, dolichol and derivatives, membrane-perturbing drugs). In this respect they claim that there is not always a parallel effect of drugs on bilayer fluidity and adenylate cyclase stimulation. In Chapter 7, Akira Ikegami et al. describe a spectroscopic analysis of the structure of bacteriorhodopsin using the fluorescence energy transfer technique and polarized resonance Raman scattering. The application of x-ray crystallo graphic analysis to the study of membrane proteins is restricted, since the crys tallization of the proteins is prevented by their hydrophobic nature. The authors thus turned to these methods in a new attempt to determine the three-dimensional location and orientation of the retinal chromophore in intact purple membrane. They also estimated the location of Lys-41 using fluorescence depolarization and predicted from free-energy calculations seven amino acid sequences corre sponding to seven transmembrane a-helixes. Finally, they estimated possible folding of the polypeptide chain of bacteriorhodopsin in the purple membrane. As the visual pigment rhodopsin is considered a prototype of a G-protein-linked receptor (1. L. Marx, 1987, Science 238:615-616), the elucidation of its struc ture and function in different organs and membranes is now of major importance. Another group of proteins studied in native membranes is the liver micro somal monoxygenase system (Chapter 8). Christoph Richter et al. give an ex tensive review of the literature and their own work. Mter highlighting the biophysical consequences of lipid peroxidation and the mobility of membrane bound cytochrome P-450 (as studied by delayed fluorescence polarization and fluorescence recovery after photobleaching using fluorescently labeled P-450), the rotational mobility and structure of the free and membrane-bound molecule are described. The authors also focus on the structure of NADPH-cytochrome P-450 reductase and the interactions of cytochrome P-450 reductase, as well as on lipid-protein interactions as studied by DPH fluorescence anisotropy. Chapter 9 by P. Proulx is devoted to some of the numerous applications of fluorescence spectroscopy to the study of prokaryotic membranes. Using a large number of examples the author shows how this technique, applied in a coordinated manner with other physical techniques, provides useful information on the physical state of the membrane and helps define the molecular interactions that form the basis for the membrane structure. Particular attention is given to

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