Introductory Remarks.- I. What is Extracellular Matrix?.- 1 Collagen.- 1. Introduction.- 2. The Collagen Molecule.- 2.1. Triple-Helical Region.- 2.2. Non-Triple-Helical Region.- 3. Posttranslational Modifications.- 3.1. Proline.- 3.2. Lysine.- 4. Molecular Arrangement in Native Fibrils.- 5. Procollagen.- 6. Genetic Types of Collagen.- 6.1. The Interstitial Collagens: Types I, II, and III.- 6.2. Collagen Types IV and V.- 7. Immunology of Collagen.- 7.1. Conventional Antibodies.- 7.2. Monoclonal Antibodies.- 8. Concluding Remarks.- References.- 2 Proteoglycans.- 1. Introduction.- 2. Cartilage Proteoglycans.- 2.1. Structure.- 2.2. Assembly, Secretion, and Aggregation.- 2.3. Functional Aspects.- 3. Proteoglycans in Other Tissues.- 3.1. Aorta.- 3.2. Corneal Stroma.- 3.3. Ovarian Follicular Fluid.- 3.4. Basal Lamina.- 3.5. Plasma Membranes.- 4. Concluding Remarks.- References.- 3 Elastin.- 1. Introduction.- 2. Isolation of Elastin.- 3. Solubilization of Elastin.- 3.1. Chemical.- 3.2. Enzymatic.- 4. Mechanical Properties.- 5. Morphology and Distribution.- 6. Amino Acid Composition.- 7. Cross-Linking.- 8. Soluble Elastins.- 8.1. Tropoelastin.- 8.2. Relationship of Tropoelastin to Insoluble Elastin.- 8.3. Peptide Models of Tropoelastin.- 8.4. Other Soluble Elastins.- 8.5. Sequencing of Tropoelastin.- 8.6. Antigenicity of Elastin and Its Derivatives.- 8.7. Cell-Free Translations.- 9. Microfibrils.- 10. Formation of Elastin in Cell and Organ Cultures.- 11. Concluding Remarks.- References.- 4 Fibronectin and Other Structural Proteins.- 1. Introduction.- 2. Fibronectin.- 2.1. Types of Fibronectin.- 2.2. Location of Fibronectin.- 2.3. Molecular Properties of Fibronectin.- 2.4. Specific Structural and Functional Domains.- 2.5. Cell Receptor for Fibronectin.- 2.6. Biosynthesis of Fibronectin.- 3. Laminin.- 4. Chondronectin.- 5. Concluding Remarks.- References.- II. How Do Cells Produce the Matrix?.- 5 Proteoglycan Biosynthesis.- 1. Introduction.- 2. Synthesis of Core Protein.- 2.1. Variation in Structure of Core Protein.- 2.2. Cell-Free Synthesis of Core Protein.- 3. Synthesis of Chondroitin Sulfate.- 3.1. Chain Initiation.- 3.2. Synthesis of Galactosyl-Xylosyl Protein Linkage.- 3.3. Completion of Linkage Region.- 3.4. Chain Elongation.- 3.5. Sulfation.- 3.6. Chain Termination.- 4. Keratan Sulfate Synthesis.- 5. Hyaluronic Acid Synthesis.- 6. Study of Proteoglycan Synthesis in Vivo.- 6.1. Sulfate Incorporation.- 6.2. Measurement of Core Protein.- 6.3. Measurement of Xylosyltransferase.- 6.4. Use of Xylosides.- 7. Control and Localization of Synthesis of Matrix Components.- 7.1. Control of Synthesis of Matrix Components.- 7.2. Localization of Proteoglycan Synthesis, Secretion, and Aggregation.- 8. Concluding Remarks.- References.- 6 Collagen Biosynthesis.- 1. Introduction.- 2. Structure of Procollagens.- 3. Collagen Gene Structure and Regulation of mRNA Levels.- 3.1. Synthesis and Cloning of Collagen cDNA Probes.- 3.2. Isolation of Collagen Gene Fragments from Genomic Libraries.- 3.3. Structure of a Collagen Gene.- 3.4. Regulation of Collagen mRNA Levels.- 4. Cotranslational and Posttranslational Modifications of Intracellular Procollagen.- 4.1. Cell-Free Translation of Collagen mRNA.- 4.2. Intracellular Location of Posttranslational Modifications.- 4.3. Hydroxylation of Prolyl and Lysyl Residues.- 4.4. Disulfide-Bond Formation and Triple-Helix Formation.- 4.5. Glycosylation of Hydroxylysyl Residues.- 4.6. Glycosylation of Asparagine Residues in Propeptides.- 5. Intracellular Transport of Procollagen.- 5.1. The Role of the Golgi Complex in Procollagen Processing and Packaging.- 5.2. The Packaging of Procollagen Aggregates in Secretory Granules.- 6. Extracellular Processing of Procollagen.- 6.1. Procollagen Proteases.- 6.2. Dermatosparaxis—A Procollagen Processing Defect.- 7. Regulation of Collagen Synthesis.- 8. Concluding Remarks.- References.- 7 Matrix Assembly.- 1. Introduction.- 2. Chemical Sequences Dictate Matrix Structure.- 3. Mechanism of Collagen Assembly.- 4. Thermodynamic Analysis of Assembly.- 4.1. General Considerations.- 4.2. Thermodynamics of Collagen Assembly.- 5. Kinetic Analysis of Assembly.- 5.1. General Considerations.- 5.2. Kinetics of Collagen Assembly.- 6. Ultrastructure of Matrix Aggregates.- 7. Ultrastructure of Collagen Assembly Intermediates.- 8. Cells Regulate the Multistep Assembly Process.- 9. Matrix Macrostructure and Function.- 10. Biomechanics.- 11. Concluding Remarks.- References.- 8 An Essay on Biological Degradation of Collagen.- 1. Introduction.- 1.1. Examples of Physiologic Removal of Collagen in Remodeling.- 1.2. Healing and Scarring.- 1.3. Influence of Tissue Structure on Collagen Removal.- 2. Characteristics of the Animal Collagenases.- 2.1. General Mode of Action.- 3. Substrate and Enzyme Specificity.- 3.1. Properties of the Cleavage-Site Region.- 3.2. Substrate Accessibility.- 3.3. Enzyme and Substrate Heterogeneity.- 4. Regulation of Collagenase.- 4.1. Inhibition and Stimulation of Active Enzyme.- 4.2. Activation of Latent Enzyme.- 4.3. Regulation of Collagenase-Producing Cells in Culture by Added Substances.- 4.4. Regulation by Cellular Interactions.- 5. Tissue Localization of Collagenase.- 6. Some Puzzles Remaining.- References.- III. What Does Matrix Do for Cells?.- 9 Glycosaminoglycans in Morphogenesis.- 1. Introduction.- 2. Transitions in Glycosaminoglycans during Morphogenesis and Differentiation.- 2.1. Hyaluronate Synthesis and Removal.- 2.2. Transitions in Structure and Source of Sulfated Proteoglycans.- 3. Glycosaminoglycan-Containing Cell Surface Coats.- 3.1. Glycosaminoglycan-Cell Surface Interactions.- 3.2. Structure of Hyaluronate-Rich Cell Surface Coats.- 4. Glycosaminoglycans and Cell-Cell Interactions.- 5. Glycosaminoglycans and Cell Movement.- 5.1. Cell-Substratum Interactions.- 5.2. Hydrated Space Formation.- 6. Glycosaminoglycans and Cell Proliferation.- 7. Basal Lamina Glycosaminoglycans and Epithelial Morphogenesis.- 8. Stabilization of Phenotype by Extracellular Macromolecules.- 9. Concluding Remarks.- References.- 10 Fibronectin and Its Relation to Cellular Structure and Behavior.- 1. Introduction.- 2. Occurrence of Fibronectin in Vitro.- 2.1. Distribution.- 2.2. Arrangement.- 3. Functions of Fibronectin in Vitro.- 3.1. Adhesion and Morphology.- 3.2. Cytoskeletal Organization.- 3.3. Migration.- 3.4. Phagocytosis.- 3.5. Growth Control.- 3.6. Cellular Differentiation.- 4. Fibronectin Distribution in Vivo.- 5. Possible Functions of Fibronectin in Vivo.- 5.1. Fibronectin as a Molecule with Multiple Binding Sites.- 5.2. Possible Effects of Fibronectin on Cellular Behavior.- 6. Concluding Remarks.- References.- 11 The Glomerular Basement Membrane: A Selective Macromolecular Filter.- 1. Introduction.- 1.1. What Are Basement Membranes and Where Are They Found?.- 1.2. What Is the Structure and Function of the Kidney Glomerulus?.- 2. Structural Organization of the GBM and Mesangial Matrix.- 3. Chemical Composition of the GBM.- 3.1. Background Information.- 3.2. Proteoglycans.- 3.3. Collagenous Components.- 3.4. Laminin.- 3.5. Fibronectin.- 3.6. Other Components.- 3.7. Comments on Techniques for Isolating the GBM.- 3.8. Summary of Nature and Location of GBM Components.- 4. What Do We Know about the Biosynthesis of GBM Components?.- 4.1. Which Glomerular Cells Make GBM Components?.- 4.2. Synthesis of Collagenous Peptides.- 4.3. Synthesis of GAG.- 4.4. Synthesis of Fibronectin and Laminin.- 5. What Do We Know about the Function of the GBM as a Filter?.- 5.1. Clearance Studies.- 5.2. Studies Using Electron-Dense Tracers.- 5.3. Nature and Location of Anionic Sites in Glomeruli.- 5.4. Role of GAG in the Permeability of the GBM to Macromolecules.- 5.5. What Are the Permeability Properties of the Lamina Densa?.- 6. Concluding Remarks.- References.- 12 Collagen and Embryonic Development.- 1. Introduction.- 2. Tissue Interaction in the Developing Embryo.- 2.1. Mesenchymal-Epithelial Interactions.- 2.2. Epithelial-Mesenchymal Interactions.- 2.3. Epithelial-Epithelial Interactions.- 3. Cell Shape, Growth, and Polarity in Vitro.- 4. Cell Adhesion and Migration.- 5. Dedifferentiation and Collagen Type Transitions.- 6. Concluding Remarks.- References.