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      Collagen: a network for regenerative medicine

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          Abstract

          Collagen, as the basic building block of native extracellular matrix, possesses an inherent biocompatibility which makes it ideal for regenerative medicine.

          Abstract

          The basic building block of the extra-cellular matrix in native tissue is collagen. As a structural protein, collagen has an inherent biocompatibility making it an ideal material for regenerative medicine. Cellular response, mediated by integrins, is dictated by the structure and chemistry of the collagen fibers. Fiber formation, via fibrillogenesis, can be controlled in vitro by several factors: pH, ionic strength, and collagen structure. After formation, fibers are stabilized via cross-linking. The final bioactivity of collagen scaffolds is a result of both processes. By considering each step of fabrication, scaffolds can be tailored for the specific needs of each tissue, improving their therapeutic potential.

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          Integrins: bidirectional, allosteric signaling machines.

          Richard O. Hynes (2002)
          In their roles as major adhesion receptors, integrins signal across the plasma membrane in both directions. Recent structural and cell biological data suggest models for how integrins transmit signals between their extracellular ligand binding adhesion sites and their cytoplasmic domains, which link to the cytoskeleton and to signal transduction pathways. Long-range conformational changes couple these functions via allosteric equilibria.
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            Lysyl oxidase: properties, specificity, and biological roles inside and outside of the cell.

            Herbert M Kagan, Wande Li (2003)
            Lysyl oxidase (LO) plays a critical role in the formation and repair of the extracellular matrix (ECM) by oxidizing lysine residues in elastin and collagen, thereby initiating the formation of covalent crosslinkages which stabilize these fibrous proteins. Its catalytic activity depends upon both its copper cofactor and a unique carbonyl cofactor and has been shown to extend to a variety of basic globular proteins, including histone H1. Although the three-dimensional structure of LO has yet to be determined, the present treatise offers hypotheses based upon its primary sequence, which may underlie the prominent electrostatic component of its unusual substrate specificity as well as the catalysis-suppressing function of the propeptide domain of prolysyl oxidase. Recent studies have demonstrated that LO appears to function within the cell in a manner, which strongly modifies cellular activity. Newly discovered LO-like proteins also likely play unique roles in biology. Copyright 2002 Wiley-Liss, Inc.
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              Third-generation biomedical materials.

              Larry L Hench, Julia Polak (2002)
              Whereas second-generation biomaterials were designed to be either resorbable or bioactive, the next generation of biomaterials is combining these two properties, with the aim of developing materials that, once implanted, will help the body heal itself.
              Article 0 comments Cited 186 times – based on 0 reviews     Review now
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                Author and article information

                Journal
                Journal ID (nlm-ta): J Mater Chem B Mater Biol Med
                Journal ID (iso-abbrev): J Mater Chem B Mater Biol Med
                Title: Journal of Materials Chemistry. B, Materials for Biology and Medicine
                Publisher: Royal Society of Chemistry
                ISSN (Print): 2050-750X
                ISSN (Electronic): 2050-7518
                Publication date (Print): 28 October 2016
                Publication date (Electronic): 22 August 2016
                Volume: 4
                Issue: 40
                Pages: 6484-6496
                Affiliations
                [a ] University of Michigan , 2350 Hayward Ave , Ann Arbor , MI 48109 , USA
                [b ] Cambridge Centre for Medical Materials , University of Cambridge , Cambridge , CB3 0FS , UK . Email: rec11@ 123456cam.ac.uk
                Article
                Publisher ID: c6tb00807k
                DOI: 10.1039/c6tb00807k
                PMC ID: 5123637
                PubMed ID: 27928505
                SO-VID: 2a43215d-e2a0-479b-8bf7-fd01977c72b1
                Copyright © This journal is © The Royal Society of Chemistry 2016
                License:

                This is an Open Access article distributed under the terms of the Creative Commons Attribution 3.0 Unported License ( http://creativecommons.org/licenses/by/3.0/) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                Date received : 31 March 2016
                Date accepted : 20 August 2016
                Categories
                Subject: Chemistry

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