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Ultrastructural Localization and Quantitation of Basal Lamina Laminin and Type Iv Collagen ¡N Normal Rat Tongue Mucosa and Induced Oral Carcinomas

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Ultrastructural Localization and Quantitation of Basal Lamina Laminin and Type Iv Collagen ¡N Normal Rat Tongue Mucosa and Induced Oral Carcinomas ì4'3'r* i. , ULTRASTRUCTURAL LOCALIZATION AND QUANTITATION OF BASAL LAMINA LAMININ AND TYPE IV COLLAGEN ¡N NORMAL RAT TONGUE MUCOSA AND INDUCED ORAL CARCINOMAS DE-JUN JIANG, MB (Shandong Medical University) Thesis submitted f or the degree of Doctor of Philosophy at The University of Adelaide (Faculty of Dentistry) 1993 Aru,*"o\uo\ 1rì9r¡ This work contains no material which has been accepted for the award of any other degree or diploma in any university or other tertiary institution and, to the best of my knowledge and belief, contains no material previously published or written by another person, except where due reference has been made in the text. I give consent to this copy of my thesis, when deposited in the University Library, being available for loan and photocopy¡ng. stcNE DArE: ...r t./,.'../Í:... CONTENTS PAGE ACKNOWLEDGMENTS vii-viii ABSTRACT x-xii LIST OF FIGURES xiii-xix LIST OF TABLES xx-xxiii PUBLICATIONS xxiv CHAPTER ONE INTRODUCTION 1-5 CHAPTER TWO LITERATURE REVIEW 6-64 2.1. lntroduction 7-10 2.2. Basal lamina comPonents 10-21 2.2.1 TYPe lV collagen 10-13 2.2.2 Laminin 13-16 2.2.3 HeParan sulfate 16-17 2.2.4 Fibronectin 18-19 2.2.5 Entacti n/N idogen 19 2.2.6 Bullous PemPhigoid antigen 19-20 2.2.7 Tenascin 20-21 2.3. Non-basal lamina extracellular matrix 21-27 comPonents 2.3.1 Other collagens 22-27 2.3.2 Other ProteoglYcans 27 2.4. Changes in basal lamina components 27-33 in Pathological situations 2.4.1 Non-neoPlastic conditions 28 2.4.2 NeoPlasms 28-33 2.5. Changes to other extracellular matrix 33-34 components in neoPlasms 2.6. Malignant neoplastic invasion-associated 34-37 enzymes 2.6.1. Collagenases 35-37 2.6.2. Other enzymes 37 2.7. SummarY 38 2.8. lmmunoelectron microscopic techniques 39-64 2.8.1 Tissue PreParation 40-58 2.8.2 lmmunostaining 58-62 2.8.3 Quantitation and immunogold 62-63 techniques 2.8.4 SummarY 63-64 CHAPTER THREE ESTABLISHMENT OF OPTIMUM 65-1 49 METHODS FOR THE ULTRASTRUCTURAL LOCALIZATION OF BASAL LAMINA LAMININ AND TYPE IV COLLAGEN IN RAT ORAL MUCOSA 3.1 . lntroduction 66-69 3.2. Materials and methods 70-74 3.3. Effect of different fixatives on the 75-80 morphology of lingual mucosa and immunolabelling of laminin and type lV collagen ¡¡i 3.4. Effect of fixative concentration on 81-84 the morphology of lingual mucosa and immunolabelling of laminin and type lV collagen 3.5. Effect of fixation additive on the 85-91 morphology of lingual mucosa and immunolabelling of laminin and type lV collagen 3.6. Effect of buffer system on the 92-95 morphology of lingual mucosa and immunolabelling of laminin and type lV collagen 3.7. Effect of fixation osmolarity on the 96-100 morphology of lingual mucosa and immunolabelling of laminin and type lV collagen 3.8. Effect of dehydration condition on 101-104 the morphology of lingual mucosa and immunolabelling of laminin and type lV collagen 3.9. Effect of polymerization temperature 105-11 1 for L.R.White resin on the morphology of lingual mucosa and immunolabelling of laminin and type lV collagen IV 3.10. lnvestigation of causes of Poor 112-123 labelling and high non-sPecific background staining in immunolabelling for type lV collagen 3.11. Establishment of controls for 124-127 immunolabelling of laminin and type lV collagen 3.12 Discussion 128-149 CHAPTER FOUR ULTRASTRUCTU RAL I MMU NOLOCA- 150-174 LIZATION OF BASAL LAMINA LAMININ AND TYPE IV COLI.AGEN ¡N NORMAL RAT TONGUE MUCOSA AND INDUCED ORAL CARCINOMAS 4.1. lntroduction 151-152 4.2. Materials and methods 153-158 4.3. Ultrastructural observation of basal 1 59-1 63 lamina and the distribution of laminin and type lV collagen in normal rat tongue mucosa and induced oral carcinomas 4.4. lmmunocytochemical controls 164-165 4.5. Discussion 166-174 CHAPTER FIVE U LTRASTRUCTU RAL MORPHOM ETRY 175-232 OF BASAL LAMINA LAMININ AND TYPE IV COLI-AGEN IN NORMAL RAT TONGUE MUCOSA AND INDUCED ORAL CARCINOMAS V 5.1. lntroduction 176-177 5.2. Materials and methods 178 5.3. Sam pling 178-182 5.4. Determination of an oPtimum 183 magnification of electronmicrographs. 5.5. Selection of an apProPriate 184-185 measurement grid for estimating the surface area of basal lamina on sections 5.6. Analysis of appearances of basal 186-190 lamina and hemidesmosomes in different given planes 5.7 Establishment of structural criteria 191-193 for the ultrastructural morphometry of basal lamina laminin and type lV collagen in normal rat tongue mucosa and induced oral carcinomas 5.8. Determination of the optimum number 193-198 of electronmicrograPhs for the ultrastructural morphometry of basal lamina laminin and type lV collagen in normal rat tongue mucosa and induced oral carcinomas VI 5.9. Quantitative analysis of the expression 199-216 of basal lamina laminin and type lV collagen in normal rat tongue mucosa and induced oral carcinomas 5.10. Test of reproducibility of results in 217 this study 5.11. Discussion 218-232 CHAPTERSIX SUMMARYANDCONCLUSIONS 233-239 CHAPTER SEVEN SUGGESTIONS FOR PROSPECTIVE 240-242 STUDIES 243-267 APPENDIX 268 ERRATA Page 5 The following hypothesis has been added at the end of Chapter one (Page 5) Hypothesis: There is no difference in the quantitative expression of basal lamina laminin and type lV collagen when normal oral mucosal epithelium and induced oral mucosal carcinomas are comPared Page 59, line 20: "makers" should read "markers" Page 130, line 21 PH should read pH Page 142, line 1: delete "the" Page 171 , line 9: "neuclei" should read "nuclei" Page 173, line 6: lnsert "out" after "ruled" Page 174, line 4: Comma after carcinoma, in that ...delete comma after "that" Page 179, line 1 : "representing" should read " re presentative" Page 186, line 1 1 Replace semicolon with colon after "planes" Page 191 , line 16: "4 cm" should read "4 centimetre" Page 218, line 2: "Ultrastructural" should be ultrastructural Page 219, line 1: delete a after "is" line 3: lnsert comma after "levels" Page 22O, line2: Replace semicolon with colon after "aspects" line 4: lnsert comma after "Accordingly" line 7: lnsert comma after "satisfactory" line 15: lnsert comma after "sections" Page 221, line 6: lnsert comma after "(1988)" line 10: Delete to after "were" line 16: lnsert comma after "methodology" Page 224, line 5: lnsert comma after "image" line 15: "can not" should read cannot Page 226, line 11: Replace semicolon with colon after " e xist" line 13: lnsert inverted commas after "component" line 23: Delete "arìd" after "subsequently" Page 232, line 3: Add "the" after "out" Page 258, line 11: "neoplartic" should read "neoplastic" Page 259, line 8: "Enzyme-labeled" should read "Enzyme- labelled" vil ACKNOWLEDGMENTS I would like to gratefully thank my supervisor Dr. David F.Wilson Department of Dentistry, University of Adelaide for his guidance, encouragement and constructive criticism throughout the duration of this research, for his help in the preparation of this thesis and for providing the environment and facilities allowing this work to be done. I also thank Dr. P.S.Smith (The lnstitute of Medical and Veterinary Science, Adelaide)(IMVS) for his f reely given advice and assistance during this studY. t would like to thank Dr. J. C. Fanning, Director of The Centre for Electron Microscopy and Microstructure Analysis (CEMMSA), University of Adelaide, for supplying me with animals and reagents during my pilot work and for providing the electron microscopic facilities. I wish to thank Professor H.J.G.Gundersen and Dr. B. Parkkenberg, Copenhagen, Denmark, for reviewing quantitative pilot study work during a "stereological course" in Melbourne in 1992 and for their positive encouragement. vilt I also wish to express my appreciation to Professor A.N. Goss, Department of Oral Maxillofacial Surgery, University of Adelaide, for initially accepting me as a candidate for a training program in his Department and for introducing me to Dr. D.F.Wilson for this research work. My appreciation is extended to Mr. P.l.Leppard, Department of Statistics, University of Adelaide for his statistic advice and processing of data in this study. My thanks also go to Mr. J. Milios, lmmunohistochemical Laboratory (IMVS) and Mrs. B. Reinboth, Department of Pathology, University of Adelaide for advice and for supplying some of the antibodies used in this research. I also extend my thanks to Ms. S. Powell, Mr. P. Dent and Dr. Darmatin of Department of Dentistry, University of Adelaide for help with animal handling and photography. I would like to acknowledge the People's Republic of China for awarding me a State Education Commission Scholarship allowing me to undertake this program of study and research. I also thank The Graduate School, Shandong Medical University, P.R. Ghina for nominating me for a State Education Commission Scholarship. ix ln Dedication to my wife X.-W. Song and my son C. Jiang for their constant love, encouragement, understanding and patience throughout the years. X ABSTRACT tn this study, special methods for the ultrastructural localization of basal lamina laminin and type lV collagen in animal oral mucosa were developed in a series of experiments aimed at determining optimum methods for tissue fixation, dehydration, embedding and immunoincubation. Furthermore, the distribution of laminin and type lV collagen in normal rat tongue mucosa and induced carcinomas was characterized. Quantitative descriptions of basal lamina laminin and type lV collagen in normal rat tongue mucosa and experimentally induced oral carcinomas were also established. The results of these studies provide a tool enabling further understanding of the molecular organization of normal oral mucosal basal lamina and basal lamina in squamous cell carcinomas.
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