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Tissue Printing. Tools for the Study of Anatomy, Histochemistry, And Gene Expression PDF

190 Pages·1992·4.424 MB·English
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Preview Tissue Printing. Tools for the Study of Anatomy, Histochemistry, And Gene Expression

ISSUE P R I N T I NG T O O LS F OR T HE S T U DY OF A N A T O M Y, H I S T O C H E M I S T R Y, A ND G E NE E X P R E S S I ON Edited by Philip D. Reid Rafael F. Pont-Lezica Centre de Physiologie Vegetale Department of Biological Sciences Universite Paul Sabatier Smith College Toulouse, France Northampton, Massachusetts Associate Editors Elena del Campillo Rosannah Taylor Department of Plant Biology Weed Science Laboratory University of California at Berkeley Behsville Agricultural Research Center Berkeley, California Agricultural Research Service United States Department of Agriculture Beltsville, Maryland ACADEMIC PRESS, INC. Harcourt Brace Jovanovich, Publishers San Diego New York Boston London Sydney Tokyo Toronto This book is printed on acid-free paper. @ Copyright © 1992 by ACADEMIC PRESS, INC. All Rights Reserved. No part of this publication may be reproduced or transmitted in any form or by any means, electronic or mechanical, including photocopy, recording, or any information storage and retrieval system, without permission in writing from the publisher. Academic Press, Inc. 1250 Sixth Avenue, San Diego, California 92101-4311 United Kingdom Edition published by Academic Press Limited 24-28 Oval Road, London NW1 7DX Library of Congress Cataloging-in-Publication Data Tissue printing: tools for the study of anatomy, histochemistry, and gene expression / Philip D. Reid .. . [et al.]. p. cm. Includes bibliographical references and index. ISBN 0-12-585970-8 1. Histochemistry—Methodology. I. Reid, Philip Dean, date QH613.T57 1992 574.8'212O28-dc20 92-7412 CIP PRINTED IN THE UNITED STATES OF AMERICA 92 93 94 95 96 97 BC 9 8 7 6 5 4 3 2 1 This b o ok is dedicated to P r o f e s s or J o s e ph E. V a r n e r, C h a r l es R e b s t o ck P r o f e s s or of Biology, W a s h i n g t on University, St. Louis, Missouri. T e a c h e r, colleague, friend, and inspiration to us all. P. D. R., R. P. -L., E. d. C, & R. T". Contributors Numbers in parentheses indicate the pages on which the authors' contributions begin. James D. Anderson, (54), Plant Hormone Laboratory, Beltsville Agricultural Re­ search Center (West), Agricultural Research Service, United States Depart­ ment of Agriculture, Beltsville, Maryland 20705 Brian A. Bailey, (54), Plant Hormone Laboratory, Beltsville Agricultural Research Center (West), Agricultural Research Service, United States Department of Agriculture, Beltsville, Maryland 20705 Roger N. Beachy, (127), Department of Biology, Washington University, St. Louis, Missouri 63130 Fraulein Cabanag, (89), Department of Chemistry, Silliman University, Dumaguete City 6200, The Philippines Hilconida Calumpong, (89), Department of Biology, Silliman University, Dumaguete City 6200, The Philippines Gladys I. Cassab, (23, 63), Instituto de Biotecnologia, Universidad Autonoma de Mexico, Cuernavaca, Morelos, 62271 Mexico1 John Castelloe, (19), Department of Biology, Washington University, St. Louis, Missouri 63130 Jeffrey F. D. Dean, (54), Plant Hormone Laboratory, Beltsville Agricultural Research Center (West), Agricultural Research Service, United States Department of Agriculture, Beltsville, Maryland 20705 Elena del Campillo, (41), Department of Plant Biology, University of California at Berkeley, Berkeley, California 94720 1Current affiliation: Department of Plant Biology, University of California at Berkeley, Berkeley, California 94720. xi xii / Contributors Erwinia S. Duran, (89), Department of Biology, Silliman University, Dumaguete City 6200, The Philippines William H. Flurkey, (60), Department of Chemistry, Indiana State University, Terre Haute, Indiana 47809 Sue E. Fritz, (32), Department of Biology, Utah State University, Logan Utah 84322 Melissa A. Gee, (100), Department of Biology, University of Missouri, Columbia, Missouri 6521 I Tom J. Guilfoyle, (100), Department of Biochemistry, University of Missouri, Co­ lumbia, Missouri 6521 I Gretchen Hagen, (100), Department of Biochemistry, University of Missouri, Co­ lumbia, Missouri 65211 Avtar K. Handa, (47, 121), Department of Horticulture, Purdue University, West Lafayette, Indiana 47907 R. W. F. Harriman, (121), Department of Horticulture, Purdue University, West Lafayette, Indiana 47907 Curtis A. Holt, (125), Department of Biology, Washington University, St. Louis, Missouri 63I302 Elizabeth E. Hood, (32), Department of Biology, Utah State University, Logan, Utah 84322 Kendall R. Hood, (32), Department of Biology, Utah State University, Logan, Utah 84322 Η. T. Hsu, (131), Florist and Nursery Crops Laboratory, Beltsville Agriculture Re­ search Center, United States Department of Agriculture, Beltsville, Maryland 20705 Υ. H. Hsu, (131), Florist and Nursery Crops Laboratory, Beltsville Agriculture Re­ search Center, United States Department of Agriculture, Beltsville, Maryland 20705 Beat Keller, (35), Swiss Federal Research Station for Agronomy Zurich, Postfach 8046, Zurich, Switzerland J. Paul Knox, (35), Department of Cell Biology, John Innes Institute, Norwich NR4 7UH, United Kingdom R. Bruce Knox, (155), Department of Cell Biology, John Innes Institute, Norwich NR4 7UH, United Kingdom J.-J. Lin, (63), Department of Biology, Washington University, St. Louis, Missouri 63130 L.-S. Lin, (63), Department of Biology, Washington University, St. Louis, Missouri 63130 N. S. Lin, (131), Florist and Nursery Crops Laboratory, Beltsville Agriculture Re­ search Center, United States Department of Agriculture, Beltsville, Maryland 20705 Kurrent affiliation: Division of Plant Biology, The Scripps Research Institute, La Jolla, California 92037. Contributors / χϋί Mirasol Magbanua, (89), Department of Biology, Silliman University, Dumaguete City 6200, The Philippines Bruce A. McClure, (100), Department of Biochemistry, University of Missouri, Co­ lumbia, Missouri 6521 I Daphne J. Osborne, (65), Department of Plant Sciences, University of Oxford, Ox­ ford OX2 3RA, United Kingdom3 Rafael F. Pont-Lezica, (71,143, 147, 153), Centre de Physiologie Vegetale, Univer- site Paul Sabatier, 31062 Toulouse, France Philip D. Reid, (9, 139), Department of Biological Sciences, Smith College, Northampton, Massachusetts 01630 Keith Roberts, (35), Department of Cell Biology, John-lnnes Institute, Norwich NR4 7UH, United Kingdom Mohan B. Singh, (155), School of Botany, University of Melbourne, Parkville, Victo­ ria 3052, Australia Yan-Ru Song, (51, 95), Institute of Botany, Academia Sinica, Beijing 100044, China Nicola Stacey, (35), Department of Cell Biology, John Innes Institute, Norwich NR4 7UH, United Kingdom Cenk Suphioglu, (155), School of Botany, University of Melbourne, Parkville, Victo­ ria 3052, Australia Rosannah Taylor, (5, 15, 54, 163, 165), Weed Science Laboratory, Beltsville Agricul­ tural Research Center, Agricultural Research Service, United States Department of Agriculture, Beltsville, Maryland 20705 Denise M. Tieman, (47, 121), Department of Horticulture, Purdue University, West Lafayette, Indiana 47907 Mark L. Tucker, (118), Plant Molecular Biology, United States Department of Agri­ culture, Beltsville, Maryland 20705 Joseph E. Varner, (I, 15, 19, 51, 59, 63, 95, 163, 165), Department of Biology, Washington University, St. Louis, Missouri 63130 Valerie Vreeland, (89), Department of Plant Biology, University of California at Berkeley, Berkeley, California 94720 Zheng-Hua Ye, (51, 95), Department of Biology, Washington University, St. Louis, Missouri 63130 Kurrent affiliation: Oxford Research Unit, Open University, Foxcombe Hall, Boars Hill, Oxford ΟΧΙ 5HR, United Kingdom. Preface The elegant simplicity of the technique of making tissue prints on ap­ propriate substrate materials has resulted in many new applications for both teaching and research, especially following the recent discovery of nitrocellulose as a printing medium. The binding properties of ap­ propriately treated nitrocellulose membranes have made possible the localization of proteins, nucleic acids, and certain carbohydrate moi­ eties in a tissue specific, or in some cases, developmentally specific mode. Some tissues, especially plant tissue that has undergone some lignification, can be used to produce tissue prints that reveal a remark­ able amount of anatomical detail without staining. These have been used to permanently record developmental changes over time. This volume is a collection of protocols detailing uses of tissue prints. Some of these have yet to be fully exploited. We believe that tissue printing will be used increasingly as a technique to study a wide variety of biological problems. The protocols presented here can be easily modified by research biologists or teachers as quick and power­ ful tools to approach as yet undefined problems. We also believe that tissue printing will gain wide use in studying animal systems, although printing soft tissue presents particular problems. Whenever possible we have included protocols written by au­ thors of research articles in which tissue printing has been used. It is our belief that having information presented by those who are actively using the method adds both a sense of excitement and a clarity to the xv XVI / Preface protocols as presented here. In some instances it was necessary for the editors to extract protocols from the literature. We have indicated such adaptations in the credit lines for each protocol. We refer the reader to the paper cited for any details that may have resulted from our own omission. Philip D. Reid Rafael F. Pont-Lezica C H A P T ER π Introduction Joseph E. Varner Department of Biology Washington University St. Louis, Missouri I. Historical Aspects II. Tissue Printing Demonstration I. Historical Aspects In 1957 R. Daoust published the first in a series of papers on substrate film printing. This paper and succeeding ones described the localiza­ tion of protease, amylase, RNase, and DNase by the simple expedient of placing cryostat sections of various organs (liver, kidney, pancreas, and intestine) on substrate films of gelatin, starch, or gelatin-nucleic acid; when the films were incubated for a few minutes and then stained for the substrate, negative images were obtained (Daoust, 1965). The surprisingly sharp images were possible because both the substrates and the enzymes were macromolecules with slow diffusion rates. Ex­ amples of the resolutions possible with Daoust's procedures are shown in Figs. I.I and 1.2. The subcellular resolution of the α-amylase distribution in barley aleurone layer cells in Fig. 1.3 is possible because Additional contributions to this chapter have been made by Rosannah Taylor. TISSUE PRINTING Copyright © 1992 by Academic Press, Inc. I All rights of reproduction in any form reserved. 2 / Joseph Ε. Varner Figure I.I (A) A negative image in a gelatin-DNA film exposed to sections of rat ileum for 10 min and stained with toluidine blue (40X magnification). (B) Corresponding tissue section (X 40 magnification) stained with toluidine blue. From "Localization of Deoxyribonuclease in Tissue Sections" by R. Daoust (1957). Journal of Experimental Cell Research 12, 203-21 I. Figure 1.2 Rabbit spermatozoa on gelatin membrane stained with India ink. The light halos result from the proteolytic dispersion of India ink particles (800X magnification). From "Proteolytic Reaction of Mammalian Spermatozoa on Gelatin Membranes" by P. Gaddum and R.J. Blandau (1970). Science 170, 749-751.

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