Extracellular Matrix Genes provides some of the interesting complexities of the structure of the entire family of extracellular matrix genes. This book illustrates the permanent role that molecular biology and molecular genetics play in the detailed understanding of the normal biology of extracellular matrix. Organized into 10 chapters, this book begins with an overview of the structural and sequence aspects of the entire family of genomic sequences with a view to establishing common functional domains among collagens and their genes. This text then examines the status of the literature concerning human types. III and V. Other chapters consider the FACIT collagen gene family. This book discusses as well the development in understanding the structure of small proteoglycan core proteins and their role in proteoglycan biosynthesis and function as a result of their molecular cloning and expression. The final chapter deals with mutations in collagen genes. This book is a valuable resource for biochemists.

Table of Contents:
ContributorsPrefaceConserved and Divergent Sequence and Functional Elements within Collagen Genes I. Introduction II. Collagens III. Fibrillar Collagen Gene Structure IV. Exon Sizes in the C- and N-Terminal Domains of Fibrillar Collagen Genes V. The Structure of the Nonfibrillar Collagen Genes VI. Introns VII. The Origins of the Structure of Present Day Collagen Genes VIII. Regulatory Sequences—Promotors IX. Regulatory Sequences—CpG Islands X. Regulatory Sequences—Enhancer Elements XI. Alternative Exon Usage in Collagen Genes XII. Untranslated Exon Sequences in Collagen Genes XIII. Conclusions ReferencesType III and V Procollagens: Homology in Genetic Organization and Diversity in Structure I. Introduction II. Cloning and Sequencing of a1(III) and a2(V) cDNA Recombinants III. The Types III and V Genes Are Structurally Related to Types I and II IV. The a1(III) and a2(V) Procollagen Genes Are Syntenic on Human Chromosome 2 V. Restriction Fragment Length Polymorphisms Associated with the a1(III) Locus VI. Multiple mRNAs Are Transcribed from the a1(III) and a2(V) Procollagen Genes VII. Primary and Secondary Structural Comparisons of the Triple Helix and C-Propeptide Domains of the Types I, III, and V Procollagen Chains VIII. Concluding Remarks ReferencesThe Molecular Biology of Collagens with Short Triple-Helical Domains I. Introduction II. Type IX Collagen Genes III. The Type XII Collagen Gene IV. The Function of Type IX and XII Collagens V. The Type X Collagen Gene VI. Type VIII Collagen Genes VII. The Function of Type VIII and X Collagens ReferencesStructure and Evolution of Collagen IV Genes I. Introduction II. Properties of Collagen IV III. Two Collagen IV Chains Are Linked on Human Chromosome 13 IV. Extensive Similarity between the C-Terminal Peptides of Collagens IV V. Rate of Evolution in Collagen IV VI. Collagen IV Genes Are Different VII. How Similar Are a1(IV) and a2(IV)? VIII. Summary ReferencesMolecular Biology of Cartilage Proteoglycan (Aggrecan) and Link Protein I. Introduction II. Link Protein cDNA and Gene Structure III. Aggrecan cDNA and Gene Structure IV. Conclusion ReferencesStructure and Role of Cloned Small Proteoglycans I. Introduction II. Syndecan III. Fibroblast Cell Surface Heparan Sulfate Proteoglycan IV. Serglycin V. Invariant Chain Proteoglycan VI. Decorin VII. Biglycan (PGI) VIII. Glycosaminoglycan Attachment Signal ReferencesGenes for the Human Laminin B1 and B2 Chains I. Introduction II. cDNA Clones Encoding Human Laminin BI and B2 Chains III. Structure of the Genes for Human Laminin BI and ?2 Chains ReferencesThe Fibronectin Gene I. Protein Structure and Function II. The Structure of the Gene III. Concluding Remarks ReferencesStructure of the Elastin Gene and Alternative Splicing of Elastin mRNA I. Introduction II. cDNA Cloning and Sequence Analysis III. Structure of Elastin Genes IV. Species Comparison of Elastin Genes V. Intron Structure VI. Abundance of Repetitive Sequences of the Alu Family VII. Copy Number of Elastin Gene VIII. Alternative Splicing of Elastin mRNA IX. Conclusions ReferencesMutations in Collagen Genes: Biochemical and Phenotypic Consequences I. Introduction II. Approaches to the Identification of Mutations in Collagen Genes III. Multiexon Rearrangements in Type I Collagen Genes Are Lethal but Are Tolerated in Type III Collagen if the Protein Product Is Synthesized IV. Point Mutations: Relation of the Phenotype to the Location and Nature of the Substituting Amino Acid V. Exon Deletion: Mechanisms and Phenotypic Correlates VI. Altered "Expression" Usually Results in Mild Phenotypes VII. Molecular-Phenotypic Correlation VIII. Concluding Remarks ReferencesIndex