Biochemistry of Collagens, Laminins, and Elastin: Structure, Function, and Biomarkers provides a comprehensive introduction to collagen and structural proteins. Type I collagen is one of the most abundant molecules in the body, playing essential roles in different tissues, particularly bone and skin. A key aspect of type I collagen is its post-translational modifications which are essential for correct synthesis and structural integrity of collagens, for tissue-specific functionality, as well as for application as biomarkers of different pathologies. This volume summarizes current data on key structural proteins (collagens, laminins and elastin), reviews how these molecules affect pathologies, and describes selected modifications of proteins that result in altered signaling properties of the original extracellular matrix component. Further, it discusses the novel concept that an increasing number of components of the ECM harbor cryptic signaling functions that may be viewed as endocrine functions. Additionally, it highlights how this knowledge can be exploited to modulate fibrotic disease. - Provides a comprehensive introduction to collagen and structural proteins - Provides insight into emerging analytical technologies that can detect biomarkers of extracellular matrix degradation - Includes a chapter dedicated to the biomarkers of structural proteins - Contains insights into the biochemical interactions and changes to structural composition of proteins in disease states

This work provides detailed knowledge about the molecular features of the laminins and describes the structure-function relationships and interactions that define their biologically active domains. Many of the discoveries concerning the tissue-specific laminins and the role of different laminins are addressed. By covering topics such as gene coding for laminins, genetic diseases affecting laminins, evolutionary aspects, embryonic development, apoptosis, neurite outgrowth and cancer, this study provides a basis for understanding the role of laminins in development and disease.

"Yet another cell and molecular biology book? At the very least, you would think that if I was going to write a textbook, I should write one in an area that really needs one instead of a subject that already has multiple excellent and definitive books. So, why write this book, then? First, it's a course that I have enjoyed teaching for many years, so I am very familiar with what a student really needs to take away from this class within the time constraints of a semester. Second, because it is a course that many students take, there is a greater opportunity to make an impact on more students' pocketbooks than if I were to start off writing a book for a highly specialized upper- level course. And finally, it was fun to research and write, and can be revised easily for inclusion as part of our next textbook, High School Biology."--Open Textbook Library.

There are 28 different collagens, with 46 unique chains, which allows for a collagen for each time and place. Some collagens are specialized for basement membrane, whereas others are the central structural component of the interstitial matrix. There are eight collagens among the 20 most abundant proteins in the body, which makes these molecules essential building blocks of tissues. In addition, lessons learned from monogenomic mutations in these proteins result in grave pathologies, exemplifying their importance in development. These molecules, and their post-translationally modified products serve as biomarkers of diseases in a range of pathologies associated with the extracellular matrix. Biochemistry of Collagens, Laminins, and Elastin: Structure, Function, and Biomarkers, Second Edition provides researchers and students current data on key structural proteins (collagens, laminins, and elastin), reviews on how these molecules affect pathologies, and information on how selected modifications of proteins can result in altered signaling properties of the original extracellular matrix component. Further, it discusses the novel concept that an increasing number of components of the extracellular matrix harbor cryptic signaling functions that may be viewed as endocrine function, and it highlights how this knowledge can be exploited to modulate fibrotic disease. - Provides an updated comprehensive introduction to collagen and structural proteins - Gives insight into emerging analytical technologies that can detect biomarkers of extracellular matrix degradation - Includes seven new chapters, including one on how collagen biomarkers are used in clinical research to support drug development and in precision medicine - Contains insights into the biochemical interactions and changes to structural composition of proteins in disease states - Proves the importance of proteins for collagen assembly, function, and durability

Cancer was thought to originate from alterations in intercellular signaling that resulted in the transformation of cells, their uncontrolled proliferation and metastasis. There is now an increasing body of evidence demonstrating that the surrounding matrix and cell-matrix interactions are also major players in this process. Cells adhere and receive signals from various extracellular matrices via transmembrane receptors, the best known of which are the heterodimeric glycoproteins, integrins.

Three types of skin cancer account for nearly 100 per cent of all diagnosed cases. Each of these three cancers begins in a different type of cell within the skin, and each cancer is named for the type of cell in which it begins. Skin cancers are divided into one of two classes - non-melanoma skin cancers and melanoma. Melanoma is the deadliest form of skin cancer. The different types of skin cancer are: Basal cell carcinoma (BCC); Squamous cell carcinoma (SCC); and Melanoma. All other skin cancers combined account for less than 1 per cent of diagnosed cases. These are classified as non-melanoma skin cancers and include Merkel cell carcinoma, dermatofibromasarcoma protuberans, Paget's disease and cutaneous T-cell lymphoma. This book examines the latest research in this field.

Cancer was thought to originate from alterations in intercellular signaling that resulted in the transformation of cells, their uncontrolled proliferation and metastasis. There is now an increasing body of evidence demonstrating that the surrounding matrix and cell-matrix interactions are also major players in this process. Cells adhere and receive signals from various extracellular matrices via transmembrane receptors, the best known of which are the heterodimeric glycoproteins, integrins.

This book provides a new compilation of information that link changes in the basic structure of synapses and brain diseases. The book shows that specific secreted proteins, and short peptide mimicking the function of neural cell adhesion molecules can significantly enhance the formation of synapses in the brain. It describes recent advances in research that lay necessary scientific groundwork to develop pharmacological treatments.

This volume gives a comprehensive overview on the most relevant leukocyte and endothelial adhesion molecules. The chapters are written by leaders in the field and focus on the biology, structure, function, and regulation of adhesion molecules. Currently approved adhesion molecule-based therapies are reviewed and an outlook for future approaches is also provided. The book is of interest to clinicians and scientists from immunology, physiology, cancer research, rheumatology, allergology, infectious diseases, gastroenterology, pulmonology and cardiology.