Biochemistry of Collagens, Laminins and Elastin

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.

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.