By Morten Karsdal
Biochemistry of Collagens, Laminins, and Elastin: constitution, functionality, and Biomarkers offers a complete creation to collagen and structural proteins. variety I collagen is without doubt one of the so much plentiful molecules within the physique, enjoying crucial roles in several tissues, fairly bone and epidermis. A key point of sort I collagen is its post-translational variations that are crucial for proper synthesis and structural integrity of collagens, for tissue-specific performance, in addition to for software as biomarkers of other pathologies.
This quantity summarizes present facts on key structural proteins (collagens, laminins and elastin), experiences how those molecules have an effect on pathologies, and describes chosen differences of proteins that lead to altered signaling houses of the unique extracellular matrix part. additional, it discusses the radical idea that a growing number of elements of the ECM harbor cryptic signaling services which may be seen as endocrine features. also, it highlights how this data should be exploited to modulate fibrotic disease.
- Provides a entire creation to collagen and structural proteins
- Provides perception into rising analytical applied sciences which could realize biomarkers of extracellular matrix degradation
- Includes a bankruptcy devoted to the biomarkers of structural proteins
- Contains insights into the biochemical interactions and adjustments to structural composition of proteins in sickness states
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Extra resources for Biochemistry of Collagens, Laminins and Elastin. Structure, Function and Biomarkers
00003-9 Copyright © 2016 Elsevier Inc. All rights reserved. 21 22 Biochemistry of Collagens, Laminins and Elastin In the extracellular matrix (ECM), type III collagen constitutes the major part of the interstitial matrix together with type I collagen. During incorporation into the ECM, N- and C-terminal propeptides are cleaved off. Cleavage of the C-terminal propeptide from soluble procollagen precursors of the fibrillar collagen is mediated by bone morphogenic protein-1 (BMP-1) and the tolloid-like proteinases, and it is the rate-limiting step in the control of fibril assembly .
Bone collagen: new clues to its mineralization mechanism from recessive osteogenesis imperfecta. Calcif Tissue Int 2013;93:338–47.  Cundy T. Recent advances in osteogenesis imperfecta. Calcif Tissue Int 2012;90:439–49.  Gensure RC, Makitie O, Barclay C, Chan C, Depalma SR, Bastepe M, et al. A novel COL1A1 mutation in infantile cortical hyperostosis (Caffey disease) expands the spectrum of collagen-related disorders. J Clin Invest 2005;115:1250–7. Type I Collagen Chapter | 1 11  Nuytinck L, Freund M, Lagae L, Pierard GE, Hermanns-Le T, De PA.
Composition and posttranslational modification of individual collagen chains from osteosarcomas and osteofibrous dysplasias. J Cancer Res Clin Oncol 1995;121:413–8.  Brinckmann J, Notbohm H, Tronnier M, Acil Y, Fietzek PP, Schmeller W, et al. Overhydroxylation of lysyl residues is the initial step for altered collagen cross-links and fibril architecture in fibrotic skin. J Invest Dermatol 1999;113:617–21.  Sell DR, Monnier VM. Structure elucidation of a senescence cross-link from human extracellular matrix.