DOCSLIB.ORG

UNIVERSITY of CALIFORNIA, SAN DIEGO the Role of Collagen on The

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
UNIVERSITY of CALIFORNIA, SAN DIEGO the Role of Collagen on The UNIVERSITY OF CALIFORNIA, SAN DIEGO The role of collagen on the structural response of dermal layers in mammals and fish A dissertation submitted in partial satisfaction of the requirements for the degree of Doctor of Philosophy in Materials Science and Engineering by Vincent Robert Sherman Committee in charge: Professor Marc A. Meyers, Chair Professor Shengqiang Cai Professor Xanthippi Markenscoff Professor Joanna McKittrick Professor Jan Talbot 2016 Copyright Vincent Robert Sherman, 2016 All rights reserved The Dissertation of Vincent Robert Sherman is approved, and is acceptable in quality and form for publication on microfilm and electronically: ____________________________________________________________ ____________________________________________________________ ____________________________________________________________ ____________________________________________________________ ____________________________________________________________ Chair University of California, San Diego 2016 iii TABLE OF CONTENTS SIGNATURE PAGE ......................................................................................................... iii TABLE OF CONTENTS ................................................................................................... iv LIST OF FIGURES ........................................................................................................... ix LIST OF TABLES ........................................................................................................... xiii ACKNOWLEDGEMENTS ............................................................................................. xiv VITA ............................................................................................................................... xvii ABSTRACT OF DISSERTATION ................................................................................. xix CHAPTER 1: INTRODUCTION AND OBJECTIVES ..................................................... 1 1.1 Introduction to biological materials science......................................................... 1 1.2 Objective of studying skin.................................................................................... 3 1.3 Objective of studying scales ................................................................................. 4 CHAPTER 2: BACKGROUND OF COLLAGEN ............................................................ 6 2.1 Types of collagen and its ubiquity in nature ........................................................ 6 2.2 Fibril collagens ..................................................................................................... 8 2.2.1 FACIT collagens ........................................................................................... 9 2.2.2 Beaded filament collagen ............................................................................ 10 2.2.3 Basement membrane collagens ................................................................... 10 2.2.4 Short chain collagens .................................................................................. 11 2.2.5 Transmembrane collagens .......................................................................... 11 2.3 Genesis and formation of fibril collagen ............................................................ 11 iv 2.4 Mechanical response of fibril collagen .............................................................. 14 2.4.1 The molecular scale .................................................................................... 16 2.4.2 The fibril scale ............................................................................................ 17 2.4.3 The microscale ............................................................................................ 20 2.4.4 The macroscale ........................................................................................... 22 2.4.5 Effects of mineralization ............................................................................. 24 2.4.6 Effects of hydration..................................................................................... 26 2.5 Models for collagen extension (tensile response) .............................................. 28 2.5.1 Hyperelastic macroscopic models based on strain energy .......................... 29 2.5.2 Macroscopic mathematical fits ................................................................... 30 2.5.3 Structurally and physically based models ................................................... 33 2.5.4 Viscoelasticity in collagen structures.......................................................... 37 2.6 Collagen in skin .................................................................................................. 42 2.6.1 Rhinoceros (Ceratotherium simum) ............................................................ 42 2.6.2 New Zealand white rabbit (Oryctolagus cuniculus) ................................... 43 2.6.3 Chicken (Gallus gallus) .............................................................................. 45 2.7 Collagen in fish scales ........................................................................................ 47 2.7.1 Alligator gar (Atractosteus spatula)............................................................ 47 2.7.2 Arapaima (Arapaima gigas) ....................................................................... 48 2.7.3 Coelacanth (Latimeria chalumnae)............................................................. 53 2.8 Collagen in bones, teeth, and other tissues ........................................................ 55 2.9 Designer collagen ............................................................................................... 58 v CHAPTER 3: RESULTS ON FISH SCALES ................................................................. 60 3.1 Introduction to scales ......................................................................................... 60 3.2 The protective scales of Atractosteus spatula .................................................... 66 3.2.1 Background ................................................................................................. 66 3.2.2 Methods....................................................................................................... 69 3.2.3 The hierarchical structure of alligator gar scales ........................................ 71 3.2.4 Mechanical performance of the gar scale ................................................... 81 3.2.5 Failure aversion strategies in the gar scale ................................................. 89 3.2.6 Summary ..................................................................................................... 95 3.3 The protective scales of Arapaima gigas ........................................................... 96 3.3.1 Background ................................................................................................. 96 3.3.2 Methods..................................................................................................... 100 3.3.3 Results ....................................................................................................... 107 3.3.4 Discussion ................................................................................................. 130 3.3.5 Summary ................................................................................................... 133 3.4 The protective scales of Latimeria chalumnae ................................................ 135 3.4.1 Structure .................................................................................................... 135 3.4.2 Mechanical response ................................................................................. 138 3.4.3 Failure prevention strategies ..................................................................... 139 3.4.4 Summary ................................................................................................... 141 3.5 Comparison of the three fish scales.................................................................. 141 3.6 Bioinspired flexible armor ............................................................................... 143 vi 3.7 Summary of fish scales .................................................................................... 149 CHAPTER 4: RESULTS ON SKIN ............................................................................... 152 4.1 Introduction ...................................................................................................... 152 4.1.1 Rabbit (Oryctolagus cuniculus) ................................................................ 154 4.1.2 Brown Chicken (Gallus gallus) ................................................................ 154 4.2 Structure and mechanical response of rabbit skin ............................................ 158 4.2.1 Background ............................................................................................... 158 4.2.2 Experimental and computational methods ................................................ 159 4.2.3 The hierarchy of the dermis ...................................................................... 162 4.2.4 Deformation imaged by small angle x-ray scattering ............................... 166 4.2.5 The constitutive model .............................................................................. 169 4.2.6 Summary ................................................................................................... 179 4.3 On the tear resistance of rabbit skin ................................................................
Load more

Recommended publications
  • Expression of Type XVI Collagen in Human Skin Fibroblasts: Enhanced Expression in Fibrotic Skin Diseases
    View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector Expression of Type XVI Collagen in Human Skin Fibroblasts: Enhanced Expression in Fibrotic Skin Diseases Atsushi Akagi, Shingo Tajima, Akira Ishibashi,* Noriko Yamaguchi,† and Yutaka Nagai Department of Dermatology, National Defense Medical College, Tokorozawa, Saitama, Japan; *Department of Cell Biology, Harvard Medical School, Boston, Massachusetts, U.S.A.; †Koken Bioscience Institute, Shinjuku-ku, Tokyo, Japan Abundance of type XVI collagen mRNA in normal level was elevated 2.3-fold in localized scleroderma human dermal fibroblasts explanted from different and 3.6-fold in systemic scleroderma compared with horizontal layers was determined using RNase protec- keloid and normal controls. Immunofluorescent study tion assays. Type XVI collagen mRNA level in the revealed that an intense immunoreactivity with the fibroblasts explanted from the upper dermis was antibody was observed in the upper to lower dermal greater than those of the middle and lower dermis. matrix and fibroblasts in the skin of systemic The antibody raised against the synthetic N-terminal scleroderma as compared with normal skin. The noncollagenous region reacted with ≈210 kDa colla- results suggest that expression of type XVI collagen, a genous polypeptide in the culture medium of member of fibril-associated collagens with interrupted fibroblasts. Immunohistochemical study of normal triple helices, in human skin fibroblasts can be human skin demonstrated that the antibody reacted heterogeneous in the dermal layers and can be preferentially with the fibroblasts and the extracellular modulated by some fibrotic diseases. Key words: matrix in the upper dermis rather than those in the dermal fibroblast/scleroderma/type XVI collagen.
    [Show full text]
  • Collagen and Creatine
    COLLAGEN AND CREATINE : PROTEIN AND NONPROTEIN NITROGENOUS COMPOUNDS Color index: . Important . Extra explanation “ THERE IS NO ELEVATOR TO SUCCESS. YOU HAVE TO TAKE THE STAIRS ” 435 Biochemistry Team • Amino acid structure. • Proteins. • Level of protein structure. RECALL: 435 Biochemistry Team Amino acid structure 1- hydrogen atom *H* ( which is distictive for each amino 2- side chain *R* acid and gives the amino acid a unique set of characteristic ) - Carboxylic acid group *COOH* 3- two functional groups - Primary amino acid group *NH2* ( except for proline which has a secondary amino acid) .The amino acid with a free amino Group at the end called “N-Terminus” . Alpha carbon that is attached to: to: thatattachedAlpha carbon is .The amino acid with a free carboxylic group At the end called “ C-Terminus” Proteins Proteins structure : - Building blocks , made of small molecules unit called amino acid which attached together in long chain by a peptide bond . Level of protein structure Tertiary Quaternary Primary secondary Single amino acids Region stabilized by Three–dimensional attached by hydrogen bond between Association of covalent bonds atoms of the polypeptide (3D) shape of called peptide backbone. entire polypeptide multi polypeptides chain including forming a bonds to form a Examples : linear sequence of side chain (R functional protein. amino acids. Alpha helix group ) Beta sheet 435 Biochemistry Team Level of protein structure 435 Biochemistry Team Secondary structure Alpha helix: - It is right-handed spiral , which side chain extend outward. - it is stabilized by hydrogen bond , which is formed between the peptide bond carbonyl oxygen and amide hydrogen. - each turn contains 3.6 amino acids.
    [Show full text]
  • A Novel Mechanism of Metastasis in Postpartum Breast Cancer
    WEANING-INDUCED LIVER INVOLUTION: A NOVEL MECHANISM OF METASTASIS IN POSTPARTUM BREAST CANCER By Erica T. Goddard A THESIS/DISSERTATION Presented to the Cancer Biology Program & the Oregon Health & Science University School of Medicine in partial fulfillment of the requirements for the degree of Doctor of Philosophy January 2017 School of Medicine Oregon Health & Science University CERTIFICATE OF APPROVAL ______________________________ This is to certify that the PhD dissertation of Erica Thornton Goddard has been approved _________________________________ Pepper J. Schedin, PhD, Mentor/Advisor _________________________________ Virginia F. Borges, MD, MMSc, Clinical Mentor/Advisor _________________________________ Melissa H. Wong, PhD, Oral Exam Committee Chair _________________________________ Lisa Coussens, PhD, Member _________________________________ Amanda W. Lund, PhD, Member _________________________________ Caroline Enns, PhD, Member _________________________________ Willscott E. Naugler, MD, Member Table of Contents List of Figures ........................................................................................................................... iv List of Tables ............................................................................................................................ vii List of abbreviations ............................................................................................................ viii Acknowledgements .............................................................................................................
    [Show full text]
  • The Close-Packed Triple Helix As a Possible New Structural Motif for Collagen
    The close-packed triple helix as a possible new structural motif for collagen Jakob Bohr∗ and Kasper Olseny Department of Physics, Technical University of Denmark Building 307 Fysikvej, DK-2800 Lyngby, Denmark Abstract The one-dimensional problem of selecting the triple helix with the highest volume fraction is solved and hence the condition for a helix to be close-packed is obtained. The close-packed triple helix is ◦ shown to have a pitch angle of vCP = 43:3 . Contrary to the conventional notion, we suggest that close packing form the underlying principle behind the structure of collagen, and the implications of this suggestion are considered. Further, it is shown that the unique zero-twist structure with no strain- twist coupling is practically identical to the close-packed triple helix. Some of the difficulties for the current understanding of the structure of collagen are reviewed: The ambiguity in assigning crystal structures for collagen-like peptides, and the failure to satisfactorily calculate circular dichroism spectra. Further, the proposed new geometrical structure for collagen is better packed than both the 10=3 and the 7=2 structure. A feature of the suggested collagen structure is the existence of a central channel with negatively charged walls. We find support for this structural feature in some of the early x-ray diffraction data of collagen. The central channel of the structure suggests the possibility of a one-dimensional proton lattice. This geometry can explain the observed magic angle effect seen in NMR studies of collagen. The central channel also offers the possibility of ion transport and may cast new light on various biological and physical phenomena, including biomineralization.
    [Show full text]
  • Non-Linearity of the Collagen Triple Helix in Solution and Implications for Collagen Function
    Biochemical Journal (2017) 474 2203–2217 DOI: 10.1042/BCJ20170217 Research Article Non-linearity of the collagen triple helix in solution and implications for collagen function Kenneth T. Walker1, Ruodan Nan1, David W. Wright1, Jayesh Gor1, Anthony C. Bishop2, George I. Makhatadze2, Barbara Brodsky3 and Stephen J. Perkins1 1Department of Structural and Molecular Biology, Darwin Building, University College London, Gower Street, London WC1E 6BT, U.K.; 2Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, 110 8th Street, Troy, NY 12180-3590, U.S.A.; and 3 Department of Biomedical Engineering, Science and Technology Center, Tufts University, 4 Colby Street, Medford, MA 02155, U.S.A. Correspondence: S. J. Perkins ([email protected]) or B. Brodsky ([email protected]) Collagen adopts a characteristic supercoiled triple helical conformation which requires a repeating (Xaa-Yaa-Gly)n sequence. Despite the abundance of collagen, a combined experimental and atomistic modelling approach has not so far quantitated the degree of flexibility seen experimentally in the solution structures of collagen triple helices. To address this question, we report an experimental study on the flexibility of varying lengths of collagen triple helical peptides, composed of six, eight, ten and twelve repeats of the most stable Pro-Hyp-Gly (POG) units. In addition, one unblocked peptide, (POG)10unblocked, was compared with the blocked (POG)10 as a control for the significance of end effects. Complementary analytical ultracentrifugation and synchrotron small angle X-ray scattering data showed that the conformations of the longer triple helical peptides were not well explained by a linear structure derived from crystallography.
    [Show full text]
  • The Recognition of Collagen and Triple-Helical Toolkit Peptides By
    THE JOURNAL OF BIOLOGICAL CHEMISTRY VOL. 289, NO. 35, pp. 24091–24101, August 29, 2014 Author’s Choice © 2014 by The American Society for Biochemistry and Molecular Biology, Inc. Published in the U.S.A. The Recognition of Collagen and Triple-helical Toolkit Peptides by MMP-13 SEQUENCE SPECIFICITY FOR BINDING AND CLEAVAGE* Received for publication, May 30, 2014, and in revised form, July 2, 2014 Published, JBC Papers in Press, July 9, 2014, DOI 10.1074/jbc.M114.583443 Joanna-Marie Howes‡, Dominique Bihan‡, David A. Slatter‡, Samir W. Hamaia‡, Len C. Packman‡, Vera Knauper§, Robert Visse¶, and Richard W. Farndale‡1 From the ‡Department of Biochemistry, University of Cambridge, Downing Site, Cambridge CB2 1QW, United Kingdom, the §Cardiff University Dental School, Dental Drive, Cardiff CF14 4XY, United Kingdom, and the ¶Kennedy Institute of Rheumatology, Hammersmith, London W6 8LH, United Kingdom Background: MMP-13 recognizes poorly-defined sequences in collagens. Results: MMP-13 binds key residues in the canonical cleavage site and another site near the collagen N terminus. Conclusion: MMP-1 and MMP-13 differ in their recognition and cleavage of collagen, which is regulated primarily through the Downloaded from Hpx domain of MMP-13. Significance: Our data explain the preference of MMP-13 for collagen II. Remodeling of collagen by matrix metalloproteinases (MMPs) is right-handed collagen superhelix, which endows the molecule crucial to tissue homeostasis and repair. MMP-13 is a collagen- with resistance to degradation by most proteases. The fibrillar http://www.jbc.org/ ase with a substrate preference for collagen II over collagens I collagens I, II, and III contain a conserved triple-helical COL and III.
    [Show full text]
  • Increased Expression of Several Collagen Genes Is Associated With
    Journal of Cancer 2016, Vol. 7 1295 Ivyspring International Publisher Journal of Cancer 2016; 7(10): 1295-1310. doi: 10.7150/jca.15371 Research Paper Increased Expression of Several Collagen Genes is Associated with Drug Resistance in Ovarian Cancer Cell Lines Radosław Januchowski1, Monika Świerczewska1, Karolina Sterzyńska1, Karolina Wojtowicz1, Michał Nowicki1, Maciej Zabel1,2 1. Department of Histology and Embryology, Poznań University of Medical Sciences, Poland; 2. Department of Histology and Embryology, Wroclaw Medical University, Poland. Corresponding author: Radosław Januchowski, mailing address: Department of Histology and Embryology, Poznan University of Medical Sciences, Święcickiego 6 St., Poznań, post code 61-781, phone number +48618546419, fax number +48 618546440, email address: [email protected]. © Ivyspring International Publisher. Reproduction is permitted for personal, noncommercial use, provided that the article is in whole, unmodified, and properly cited. See http://ivyspring.com/terms for terms and conditions. Received: 2016.02.25; Accepted: 2016.05.23; Published: 2016.06.25 Abstract Ovarian cancer is the most lethal gynaecological cancer. The main reason for the high mortality among ovarian cancer patients is the development of drug resistance. The expression of collagen genes by cancer cells can increase drug resistance by inhibiting the penetration of the drug into the cancer tissue as well as increase apoptosis resistance. In this study, we present data that shows differential expression levels of collagen genes and proteins in cisplatin- (CIS), paclitaxel- (PAC), doxorubicin- (DOX), topotecan- (TOP), vincristine- (VIN) and methotrexate- (MTX) resistant ovarian cancer cell lines. Quantitative real-time polymerase chain reactions were performed to determine the mRNA levels. Protein expression was detected using Western blot and immunocytochemistry assays.
    [Show full text]
  • Effect of Selenocystine on Gene Expression Profiles in Human Keloid
    View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector Genomics 97 (2011) 265–276 Contents lists available at ScienceDirect Genomics journal homepage: www.elsevier.com/locate/ygeno Effect of selenocystine on gene expression profiles in human keloid fibroblasts Bruna De Felice a,⁎, Corrado Garbi b, Robert R. Wilson a, Margherita Santoriello b, Massimo Nacca a a Department of Life Sciences, University of Naples II, Via Vivaldi 43, 81100 Caserta, Italy b Department of Cellular and Molecular Biology and Pathology, University of Naples “Federico II”, Naples, Italy article info abstract Article history: In this study, selenocystine, a nutritionally available selenoamino acid, was identified for the first time as a Received 15 October 2010 novel agent with anti proliferative activity on human keloids. Accepted 24 February 2011 The 20 μM concentration after 48 h treatment used here was the most effective to reduce keloid fibroblast Available online 1 March 2011 growth. We analyzed the gene expression profile of selenocystine treatment response in keloid fibroblasts by the microarray system to characterize the effects of selenocystine on human keloids. Keywords: The major alterations in keloid fibroblasts following selenocystine exposure included up-regulation of the Keloids Microarray genes encoding cell death and transcription factors. Prominent down-regulation of genes involved in Selenocystine development, cell adhesion and cytoskeleton, as well as extra cellular matrix genes, usually strongly up- Gene expression regulated in keloids, resulted following selenocystine exposure. The range of the down-regulated genes and the degree of the decreased expression appeared to be correlated with the degree of the morphological alterations in selenocystine treated keloids.
    [Show full text]
  • Protein Physics A
    PROTEIN PHYSICS A. V. Finkelstein & O. B. Ptitsyn LECTURE 7 Secondary Structures ¾ Regular Secondary Structures - helices (not just α-helix) - β-sheet - superhelices ¾ Irregular Secondary Structure - β-turns - β-bulges Secondary Structures Helices - one continuous region of the polypeptide - stabilized by hydrogen bonds between carbonyl and amide groups and van der Waals interactions across the helical axis (i,i+2) (i,i+3) (i,i+4) (i,i+5) L-handed There are helices without any hydrogen bonds, stabilized only by van der Waals interactions ( synthetic: Poly(Pro)I-II, Poly(Gly)I-II) R-handed Structure Residues per Rise per Radius of Observed turn residue (Å) helix (Å) 310 - helix +3.0 2.0 1.9 Small pieces αR -helix +3.6 1.5 2.3 Abundant αL -helix -3.6 1.5 2.3 absent π-helix +4.3 1.1 2.8 absent β -2.3 3.2 1.0 Abundant β -2.3 3.4 1.0 Abundant Collagen helix -3 2.9 1.6 In fibers αR – helix is the most abundant and the most stable Helices Alpha(R) - helix • 4 – 100 components • average length ~10 residues, corresponding to 15Å • the helix is a long dipole; N-terminus is capped by negative phosphate groups C- • tendency to appear in an alpha helix: Met, Ala, Leu, Lys, Gln •Proline– tends to bend/break helices, though often appears as the first residue of the helix •Glycine– tends to disrupt the helix, it is entropically expensive state N+ ALA, etc. GLY only Location of an α - helix Helical Wheel – axis view 11 11 11 7 7 7 4 10 4 4 10 3 3 10 3 8 1 8 1 1 8 6 6 2 6 2 5 2 5 5 9 9 9 K-E-D-A-K-G-K-S-E-E-E L-S-F-A-A-A-M-N-G-L-A totally buried I-N-E-G-F-D-L-L-R-S-G
    [Show full text]
  • Cell-Deposited Matrix Improves Retinal Pigment Epithelium Survival on Aged Submacular Human Bruch’S Membrane
    Retinal Cell Biology Cell-Deposited Matrix Improves Retinal Pigment Epithelium Survival on Aged Submacular Human Bruch’s Membrane Ilene K. Sugino,1 Vamsi K. Gullapalli,1 Qian Sun,1 Jianqiu Wang,1 Celia F. Nunes,1 Noounanong Cheewatrakoolpong,1 Adam C. Johnson,1 Benjamin C. Degner,1 Jianyuan Hua,1 Tong Liu,2 Wei Chen,2 Hong Li,2 and Marco A. Zarbin1 PURPOSE. To determine whether resurfacing submacular human most, as cell survival is the worst on submacular Bruch’s Bruch’s membrane with a cell-deposited extracellular matrix membrane in these eyes. (Invest Ophthalmol Vis Sci. 2011;52: (ECM) improves retinal pigment epithelial (RPE) survival. 1345–1358) DOI:10.1167/iovs.10-6112 METHODS. Bovine corneal endothelial (BCE) cells were seeded onto the inner collagenous layer of submacular Bruch’s mem- brane explants of human donor eyes to allow ECM deposition. here is no fully effective therapy for the late complications of age-related macular degeneration (AMD), the leading Control explants from fellow eyes were cultured in medium T cause of blindness in the United States. The prevalence of only. The deposited ECM was exposed by removing BCE. Fetal AMD-associated choroidal new vessels (CNVs) and/or geo- RPE cells were then cultured on these explants for 1, 14, or 21 graphic atrophy (GA) in the U.S. population 40 years and older days. The explants were analyzed quantitatively by light micros- is estimated to be 1.47%, with 1.75 million citizens having copy and scanning electron microscopy. Surviving RPE cells from advanced AMD, approximately 100,000 of whom are African explants cultured for 21 days were harvested to compare bestro- American.1 The prevalence of AMD increases dramatically with phin and RPE65 mRNA expression.
    [Show full text]
  • Identification and Structural Analysis of Type I Collagen Sites in Complex with Fibronectin Fragments
    Identification and structural analysis of type I collagen sites in complex with fibronectin fragments Miche` le C. Erata, David A. Slatterb, Edward D. Lowec, Christopher J. Millarda, Richard W. Farndaleb, Iain D. Campbella, and Ioannis Vakonakisa,1 aDepartment of Biochemistry and cLaboratory of Molecular Biophysics, University of Oxford, Oxford OX1 3QU, United Kingdom; and bDepartment of Biochemistry, University of Cambridge, Cambridge CB2 1QW, United Kingdom Edited by John Kuriyan, University of California, Berkeley, CA, and approved January 28, 2009 (received for review December 9, 2008) Collagen and fibronectin are major components of vertebrate ments bind the same peptide sequence just C-terminal to the extracellular matrices. Their association and distribution control MMP-1 cleavage site; the tightest binding, however, is mediated 8–9 the development and properties of diverse tissues, but thus far no by the FnI domain pair that also binds ␣2(I). A 2.1-Å crystal 8–9 structural information has been available for the complex formed. structure of FnI in complex with the ␣1(I) peptide shows an ␣ Here, we report binding of a peptide, derived from the 1 chain of extended single-strand peptide conformation, which suggests type I collagen, to the gelatin-binding domain of human fibronec- that FN stabilizes a noncanonical collagen structure upon bind- tin and present the crystal structure of this peptide in complex with ing. We explore this hypothesis in thermal denaturation exper- 8–9 the FnI domain pair. Both gelatin-binding domain subfrag- iments using model triple-helical peptides. The results presented 6 1–2 7 8–9 ments, FnI FnII FnI and FnI, bind the same specific sequence show the first atomic resolution picture of the interaction ␣ on D-period 4 of collagen I 1, adjacent to the MMP-1 cleavage site.
    [Show full text]
  • Outcome of Split Thickness Skin Grafts on Excised Burns with Different Dermal Compositions
    Department of Plastic Surgery and Department of Pharmacology Faculty of Medicine University of Helsinki Finland Outcome of split thickness skin grafts on excised burns with different dermal compositions Heli Lagus Academic dissertation To be presented, with the permission of the Faculty of Medicine of the University of Helsinki, for public examination Porthania lecture hall P674, Helsinki, on June 26th 2020, at 12 o’clock noon. Helsinki 2020 Supervised by Professor Jyrki Vuola, M.D., Ph.D. Department of Plastic Surgery Helsinki Burn Centre Helsinki University Hospital and University of Helsinki Finland Docent Esko Kankuri, M.D., Ph.D. Department of Pharmacology University of Helsinki Finland Reviewed by Julian Dye, MA (Oxon), Ph.D. (Lon) CBiol, FRSB Institute of Biomedical Engineering University of Oxford United Kingdom Docent Ilkka Kaartinen, M.D., Ph.D. Department of Plastic Surgery Tampere University Hospital Finland Opponent Professor Esther Middelkoop, Ph.D. in biochemistry Plastic, Reconstructive and Hand Surgery Amsterdam UMC - Vrije Universiteit Amsterdam The Netherlands The Faculty of Medicine uses the Urkund system (plagiarism recognition) to examine all doctoral dissertations. ISBN: 978-951-51-6066-9 (print) ISBN: 978-951-51-6067-6 (on-line) University Printing House Helsinki 2020 To my family 3 Table of Contents List of original publications........................................................................................................... 6 Abbreviations ...............................................................................................................................
    [Show full text]