Type XVIII Collagen Modulates Keratohyalin Granule Formation and Keratinization in Oral Mucosa
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New Concepts in Basement Membrane Biology Willi Halfter1, Philipp Oertle2, Christophe A
REVIEW ARTICLE New concepts in basement membrane biology Willi Halfter1, Philipp Oertle2, Christophe A. Monnier2,*, Leon Camenzind2, Magaly Reyes-Lua1, Huaiyu Hu3, Joseph Candiello4, Anatalia Labilloy5,†, Manimalha Balasubramani6, Paul Bernhard Henrich1 and Marija Plodinec2,7 1 Department of Ophthalmology, University Hospital Basel, Switzerland 2 Biozentrum and the Swiss Nanoscience Institute, University of Basel, Switzerland 3 Department of Neurobiology and Physiology, Upstate University Hospital, SUNY University, Syracuse, NY, USA 4 Department of Bioengeneering, University of Pittsburgh, PA, USA 5 Department of Renal Physiology, University of Pittsburgh, PA, USA 6 Proteomics Core Facility of the University of Pittsburgh, PA, USA 7 Department of Pathology, University Hospital Basel, Switzerland Keywords Basement membranes (BMs) are thin sheets of extracellular matrix that basal lamina; basement membrane; outline epithelia, muscle fibers, blood vessels and peripheral nerves. The biomechanical properties; collagen IV; current view of BM structure and functions is based mainly on transmis- laminin; membrane asymmetry; nidogen; sion electron microscopy imaging, in vitro protein binding assays, and phe- perlecan notype analysis of human patients, mutant mice and invertebrata. Correspondence Recently, MS-based protein analysis, biomechanical testing and cell adhe- W. Halfter, Department of Ophthalmology, sion assays with in vivo derived BMs have led to new and unexpected University Hospital Basel, Mittlere insights. Proteomic analysis combined with ultrastructural studies showed Strasse 91, 4031 Basel, Switzerland that many BMs undergo compositional and structural changes with Fax: +41 61 267 21 09 advancing age. Atomic force microscopy measurements in combination Tel: +49 7624 982528 with phenotype analysis have revealed an altered mechanical stiffness that E-mail: [email protected] M. -
Ophthalmological Features Associated with COL4A1 Mutations
OPHTHALMIC MOLECULAR GENETICS SECTION EDITOR: JANEY L. WIGGS, MD, PhD Ophthalmological Features Associated With COL4A1 Mutations Isabelle Coupry, PhD; Igor Sibon, MD, PhD; Bruno Mortemousque, MD; Franc¸ois Rouanet, MD; Manuele Mine, PharmD, PhD; Cyril Goizet, MD, PhD Objective: To investigate the wide variability of ocular Conclusions: The COL4A1 mutations may be associ- manifestations associated with mutations in the COL4A1 ated with various ophthalmologic developmental anoma- gene that encodes collagen IV␣1. lies of anterior segment dysgenesis type, which are reminiscent of Axenfeld-Rieger anomalies (ARA). Cere- Methods: We clinically evaluated 7 patients from 2 un- brovascular disorders should be added to the list of signs related families in whom ocular features segregated with potentially associated with ARA. COL4A1 mutations that were identified by direct se- quencing. Clinical Relevance: These data suggest that cerebral magnetic resonance imaging may be recommended in Results: The G2159A transition (c.2159GϾA) that leads the clinical treatment of patients with apparently iso- tothemissensemutationp.Gly720Aspwasidentifiedinfam- lated ARA, even when neurological symptoms or signs ily A. An ocular phenotype of variable severity was observed are lacking. in all affected relatives. The missense mutation c.2263GϾA, p.Gly755Arg was identified in family B. One patient from family B also displayed notable ocular features. Arch Ophthalmol. 2010;128(4):483-489 NEW FORM OF HEREDITARY constellation of ocular findings that in- cerebrovascular disorder clude anomalies of the anterior chamber was recently associated angle and aqueous drainage structures (iri- with mutations in the dogoniodysgenesis), iris hypoplasia, ec- COL4A1 gene that en- centric pupil (corectopia), iris tears (poly- Acodes collagen IV␣1.1,2 Mutations in coria), and iridocorneal adhesions COL4A1 were initially associated with ce- traversing the anterior chamber. -
Repair, Regeneration, and Fibrosis Gregory C
91731_ch03 12/8/06 7:33 PM Page 71 3 Repair, Regeneration, and Fibrosis Gregory C. Sephel Stephen C. Woodward The Basic Processes of Healing Regeneration Migration of Cells Stem cells Extracellular Matrix Cell Proliferation Remodeling Conditions That Modify Repair Cell Proliferation Local Factors Repair Repair Patterns Repair and Regeneration Suboptimal Wound Repair Wound Healing bservations regarding the repair of wounds (i.e., wound architecture are unaltered. Thus, wounds that do not heal may re- healing) date to physicians in ancient Egypt and battle flect excess proteinase activity, decreased matrix accumulation, Osurgeons in classic Greece. The liver’s ability to regenerate or altered matrix assembly. Conversely, fibrosis and scarring forms the basis of the Greek myth involving Prometheus. The may result from reduced proteinase activity or increased matrix clotting of blood to prevent exsanguination was recognized as accumulation. Whereas the formation of new collagen during the first necessary event in wound healing. At the time of the repair is required for increased strength of the healing site, American Civil War, the development of “laudable pus” in chronic fibrosis is a major component of diseases that involve wounds was thought to be necessary, and its emergence was not chronic injury. appreciated as a symptom of infection but considered a positive sign in the healing process. Later studies of wound infection led The Basic Processes of Healing to the discovery that inflammatory cells are primary actors in the repair process. Although scurvy (see Chapter 8) was described in Many of the basic cellular and molecular mechanisms necessary the 16th century by the British navy, it was not until the 20th for wound healing are found in other processes involving dynamic century that vitamin C (ascorbic acid) was found to be necessary tissue changes, such as development and tumor growth. -
A Collagen Glucosyltransferase Drives Lung Adenocarcinoma Progression in Mice
ARTICLE https://doi.org/10.1038/s42003-021-01982-w OPEN A collagen glucosyltransferase drives lung adenocarcinoma progression in mice Hou-Fu Guo 1, Neus Bota-Rabassedas 1, Masahiko Terajima 2, B. Leticia Rodriguez1, Don L. Gibbons 1, Yulong Chen1, Priyam Banerjee1, Chi-Lin Tsai 3, Xiaochao Tan1, Xin Liu1, Jiang Yu1, Michal Tokmina-Roszyk4, Roma Stawikowska4, Gregg B. Fields4, Mitchell D. Miller 5, Xiaoyan Wang3, Juhoon Lee6,7, Kevin N. Dalby6,7, Chad J. Creighton 8,9, George N. Phillips Jr 5,10, John A. Tainer 3, Mitsuo Yamauchi2 & ✉ Jonathan M. Kurie 1 Cancer cells are a major source of enzymes that modify collagen to create a stiff, fibrotic tumor stroma. High collagen lysyl hydroxylase 2 (LH2) expression promotes metastasis and 1234567890():,; is correlated with shorter survival in lung adenocarcinoma (LUAD) and other tumor types. LH2 hydroxylates lysine (Lys) residues on fibrillar collagen’s amino- and carboxy-terminal telopeptides to create stable collagen cross-links. Here, we show that electrostatic interac- tions between the LH domain active site and collagen determine the unique telopeptidyl lysyl hydroxylase (tLH) activity of LH2. However, CRISPR/Cas-9-mediated inactivation of tLH activity does not fully recapitulate the inhibitory effect of LH2 knock out on LUAD growth and metastasis in mice, suggesting that LH2 drives LUAD progression, in part, through a tLH- independent mechanism. Protein homology modeling and biochemical studies identify an LH2 isoform (LH2b) that has previously undetected collagen galactosylhydroxylysyl glucosyl- transferase (GGT) activity determined by a loop that enhances UDP-glucose-binding in the GLT active site and is encoded by alternatively spliced exon 13 A. -
Collagen Type XVIII (H-140): Sc-25720
SANTA CRUZ BIOTECHNOLOGY, INC. Collagen Type XVIII (H-140): sc-25720 The Power to Question BACKGROUND APPLICATIONS Type XV and XVIII collagens form the new subgroup MULTIPLEXIN, within the Collagen Type XVIII (H-140) is recommended for detection of Collagen α1 diverse family of collagens, which contains nineteen distinct types of collagens Type XVIII of mouse, rat and human origin by Western Blotting (starting found in vertebrates. Both type XV and XVIII collagens are characterized by dilution 1:200, dilution range 1:100-1:1000), immunoprecipitation [1–2 µg extensive interruptions in their collagenous sequences. Members of the MUL- per 100–500 µg of total protein (1 ml of cell lysate)] and immunofluores- TIPLEXIN subgroup contain polypeptides with multiple triple-helical domains cence (starting dilution 1:50, dilution range 1:50-1:500). separated and flanked by non-triple-helical regions. Type XV is predominantly Suitable for use as control antibody for Collagen Type XVIII siRNA (h): expressed in internal organs such as adrenal gland, kidney and pancreas. Type sc-43072 and Collagen Type XVIII siRNA (m): sc-43073. XVIII encodes two different α1 chains, which have different signal peptides and variant N-terminal non-collagenous NC1 domains of 495 and 303 amino Molecular Weight of Collagen Type XVIII: 20-22 kDa. acids. The long variant NC1-434 Type XVIII mRNAs are prominently expressed Positive Controls: rat C6 glioblastoma, human PBL or rat lung extract: sc-2396. in liver, while the variant NC1-303 mRNAs are predominantly expressed in heart, kidney, placenta, prostate, ovaries, skeletal muscle and small intestine. RECOMMENDED SECONDARY REAGENTS Endostatin is a fragment of the C-terminal domain NC1 of collagen XV and XVIII that inhibits angiogenesis and tumor growth. -
Inherited Connective Tissue Disorders of Collagens: Lessons from Targeted Mutagenesis
13 Inherited Connective Tissue Disorders of Collagens: Lessons from Targeted Mutagenesis Christelle Bonod-Bidaud and Florence Ruggiero Institut de Génomique Fonctionnelle de Lyon, ENS de Lyon, UMR CNRS 5242, University Lyon 1, France 1. Introduction The extracellular matrix (ECM) is the cell structural environment in tissues and organs. The ECM is a dynamic structure that it is constantly remodelled. It contributes to tissue integrity and mechanical properties. It is also essential for maintaining tissue homeostasis, morphogenesis and differentiation, which it does, through specific interactions with cells. The ECM is composed of a mixture of water and macromolecules classified into four main categories: collagens, proteoglycans, elastic proteins, and non-collagenous glycoproteins (also called adhesive glycoproteins). The nature, concentration and ratio of the different ECM components are all important factors in the regulation of the assembly of complex tissue-specific networks tuned to meet mechanical and biological requirements of tissues. Collagens form a superfamily of 28 trimeric proteins, distinguishable from the other ECM components by their particular abundance in tissues (collagens represent up to 80-90% of total proteins in skin, tendon and bones) and their capacity to self-assemble into supramolecular organized structures (the best known being the banded fibers). The collagen superfamily is highly complex and shows a remarkable diversity in structure, tissue distribution and function (Ricard-Blum and Ruggiero, 2005). The importance -
List of Publications Taina Pihlajaniemi
List of publications Taina Pihlajaniemi 1 April, 2016 A Peer-reviewed scientific articles Journal article (refereed), original research; review article, literature review, systematic review; book section, chapters in research books; conference proceedings A.1 Savolainen E-R, Kero M, Pihlajaniemi T, and Kivirikko KI. Deficiency of galactosylhydroxylysyl glucosyltransferase, an enzyme of collagen synthesis, in a family with dominant epidermolysis bullosa simplex. N Engl J Med 304: 197-204, 1981 A.2 Pihlajaniemi T, Myllylä R, Alitalo K, Vaheri A, and Kivirikko KI. Post-translational modifications in the biosynthesis of type IV collagen by a human tumor cell line. Biochemistry 20: 7409-7415, 1981 A.3 Anttinen H, Puistola U, Pihlajaniemi T, and Kivirikko KI. Differences between proline and lysine hydroxylations in their inhibition by zinc or by ascorbate deficiency during collagen synthesis in various cell types. Biochim Biophys Acta 674: 336-344, 1981 A.4 Pihlajaniemi T, Myllylä R, Kivirikko KI, and Tryggvason K. Effects of streptozotocin diabetes, glucose, and insulin on the metabolism of type IV collagen and proteoglycan in murine basement membrane-forming EHS tumor tissue. J Biol Chem 257: 14914-14920, 1982 A.5 de Wet WJ, Pihlajaniemi T, Myers J, Kelly TE, and Prockop DJ. Synthesis of a shortened pro- 2(I) chain and decreased synthesis of pro- 2(I) chains in a proband with osteogenesis imperfecta. J Biol Chem 258: 7721-7728, 1983 A.6 Oikarinen J, Pihlajaniemi T, Hämäläinen L, and Kivirikko KI. Cortisol decreases the cellular concentration of translatable procollagen mRNA species in cultured human skin fibroblasts. Biochim Biophys Acta 741: 297-302, 1983 A.7 Myllylä R, Koivu J, Pihlajaniemi T, and Kivirikko KI. -
Binding and Endothelial Tube Formation
Proc. Natl. Acad. Sci. USA Vol. 95, pp. 7275–7280, June 1998 Biochemistry Defining the domains of type I collagen involved in heparin- binding and endothelial tube formation SHAWN M. SWEENEY†,CYNTHIA A. GUY‡,GREGG B. FIELDS§, AND JAMES D. SAN ANTONIO†¶ †Department of Medicine and the Cardeza Foundation for Hematologic Research, Jefferson Medical College of Thomas Jefferson University, Philadelphia, PA 19107; ‡Department of Laboratory Medicine and Pathology, University of Minnesota, Minneapolis, MN 55455; and §Department of Chemistry and Biochemistry, and the Center for Molecular Biology and Biotechnology, Florida Atlantic University, Boca Raton, FL 33431 Edited by Darwin J. Prockop, MCP-Hahnemann Medical School, Philadelphia, PA, and approved April 14, 1998 (received for review January 12, 1998) ABSTRACT Cell surface heparan sulfate proteoglycan To localize more precisely the heparin-binding regions on type (HSPG) interactions with type I collagen may be a ubiquitous I collagen, we studied complexes between collagen monomers cell adhesion mechanism. However, the HSPG binding sites on and heparin–albumin–gold particles by electron microscopy type I collagen are unknown. Previously we mapped heparin (6), and we observed heparin binding primarily to a region on binding to the vicinity of the type I collagen N terminus by the triple helix near the procollagen N terminus. In collagen electron microscopy. The present study has identified type I fibrils, heparin–gold bound to the a bands region within each collagen sequences used for heparin binding and endothelial D-period, which is consistent with an N-terminal heparin- cell–collagen interactions. Using affinity coelectrophoresis, binding site on its monomers. The resolution of the mapping we found heparin to bind as follows: to type I collagen with technique was insufficient to assign heparin-binding function high affinity (Kd ' 150 nM); triple-helical peptides (THPs) to any particular protein sequence. -
Adenovirus-Mediated Transfer of Type IV Collagen Α5 Chain Cdna
Gene Therapy (2001) 8, 882–890 2001 Nature Publishing Group All rights reserved 0969-7128/01 $15.00 www.nature.com/gt RESEARCH ARTICLE Adenovirus-mediated transfer of type IV collagen ␣5 chain cDNA into swine kidney in vivo: deposition of the protein into the glomerular basement membrane P Heikkila¨1, A Tibell2, T Morita1, Y Chen1,GWu2, Y Sado4, Y Ninomiya5, E Pettersson3 and K Tryggvason1 1Division of Matrix Biology, Department of Medical Biochemistry and Biophysics, Departments of 2Transplantation Surgery, and 3Nephrology, Huddinge Hospital, Karolinska Institutet, Stockholm, Sweden; 4Division of Immunology, Shigei Medical Research Institute, Okayama; 5Department of Molecular Biology and Biochemistry, Okayama University Medical School, Okayama, Japan Gene therapy of Alport syndrome (hereditary nephritis) aims a FLAG epitope in the recombinant ␣5(IV) chain. The results at the transfer of a corrected type IV collagen ␣ chain gene indicate that correction of the molecular defect in Alport syn- into renal glomerular cells responsible for production of the drome is possible. Previously, we had developed an organ glomerular basement membrane (GBM). A GBM network perfusion method for effective in vivo gene transfer into composed of type IV collagen molecules is abnormal in glomerular cells. In vivo perfusion of pig kidneys with the Alport syndrome which leads progressively to kidney failure. recombinant adenovirus resulted in expression of the ␣5(IV) The most common X-linked form of the disease is caused chain in kidney glomeruli as shown by in situ hybridization by mutations in the gene for the ␣5(IV) chain, the ␣5 chain and its deposition into the GBM was shown by immunohisto- of type IV collagen. -
Premature Aggregation of Type IV Collagen and Early Lethality in Lysyl Hydroxylase 3 Null Mice
Premature aggregation of type IV collagen and early lethality in lysyl hydroxylase 3 null mice Kati Rautavuoma*†‡, Kati Takaluoma*†‡, Raija Sormunen§, Johanna Myllyharju*†, Kari I. Kivirikko*†, and Raija Soininen†¶ *Collagen Research Unit and Departments of †Medical Biochemistry and Molecular Biology and §Pathology, Biocenter Oulu, University of Oulu, 90014 Oulu, Finland Edited by Erkki Ruoslahti, The Burnham Institute, La Jolla, CA, and approved August 17, 2004 (received for review July 9, 2004) Collagens carry hydroxylysine residues that act as attachment sites LH3 is essential for the synthesis of type IV collagen during early for carbohydrate units and are important for the stability of development and, hence, for the stability of basement mem- crosslinks but have been regarded as nonessential for vertebrate branes (BMs). survival. We generated mice with targeted inactivation of the gene for one of the three lysyl hydroxylase isoenzymes, LH3. The null Materials and Methods embryos developed seemingly normally until embryonic day 8.5, Targeting of the Plod3 Gene and Generation of Mutant Mice. The but development was then retarded, with death around embryonic genomic clone used to clone the targeting construct was isolated day 9.5. Electron microscopy (EM) revealed fragmentation of base- from a 129SV mouse genomic library with human LH3 cDNA ment membranes (BMs), and immuno-EM detected type IV collagen (5) as a probe. The construct contains 1.2- and 5-kb genomic within the dilated endoplasmic reticulum and in extracellular arms and the -gal-PGK-neo cassette inserted in-frame into exon aggregates, but the typical BM staining was absent. Amorphous 1. Embryonic stem cells were targeted, and mice were generated intracellular and extracellular particles were also seen by collagen by standard techniques. -
Original Article Glycation of Matrix Proteins in the Artery Inhibits Migration of Smooth Muscle Cells from the Media to the Intima
Original Article Glycation of Matrix Proteins in the Artery Inhibits Migration of Smooth Muscle Cells from the Media to the Intima (glycation / advanced glycation end products / collagen / elastin / myocytes / atherosclerosis) A. KUZAN1, O. MICHEL1, A. GAMIAN1,2 1Department of Medical Biochemistry, Wroclaw Medical University, Wrocław, Poland 2Laboratory of Medical Microbiology, Ludwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Wroclaw, Poland Abstract. Formation and growth of atherosclerotic Introduction plaques have serious clinical consequences. One mechanism that occurs during atherogenesis is mi- Smooth muscle cells (SMC) are predominantly lo- gration of smooth muscle cells from the middle layer cated in the middle layer of the artery, where they play a of the artery to the intima, where they proliferate crucial role: they determine the contractility of the tis- and are transformed into foam cells. This degenera- sue, hereby adjusting the blood flow through the artery. tive process is accompanied by glycation, by which In such a case, they are called contractile smooth muscle proteins are modified and change the biomechanical cells, which are characterized by the richness in actin and biochemical properties. The aim of the study filaments. They may, however, undergo phenotype was to determine whether glycation of collagen and switching and migration and become cells that reside in elastin building the walls of blood vessels alters the the intima. Then, they are called synthetic type SMC, adhesion and rate of myocyte migration. In vitro ex- are rich in rough endoplasmic reticulum and character- periments included migration assays and immuno- ized by active metabolism (Stary et al., 1992, 1994; cytochemical staining with anti α-actin, β-catenin Tukaj, 2010). -
Type IV Collagens and Basement Membrane Diseases: Cell Biology and Pathogenic Mechanisms
CHAPTER THREE Type IV Collagens and Basement Membrane Diseases: Cell Biology and Pathogenic Mechanisms Mao Mao, Marcel V. Alavi, Cassandre Labelle-Dumais and Douglas B. Gould* Departments of Ophthalmology and Anatomy, Institute for Human Genetics, UCSF School of Medicine, San Francisco, CA, USA *Corresponding author: E-mail: [email protected] Contents 1. Genomic Organization and Protein Structure of Type IV Collagens 62 1.1 Introduction and history 62 1.2 Genomic structure 64 1.3 Protein domain structure 66 1.3.1 7S domain 68 1.3.2 Triple helical domain 69 1.3.3 NC1 domain 70 2. Type IV Collagen Biosynthesis 72 2.1 Heat shock protein 47 72 2.2 Protein disulfide isomerase 73 2.3 Peptidylprolyl isomerases 74 2.4 Prolyl 4-hydroxylases 74 2.5 Prolyl 3-hydroxylases 75 2.6 Lysyl hydroxylases 76 2.7 Transport and Golgi organization 1 78 3. Type IV Collagen-Related Pathology 78 3.1 COL4A3eA6-associated pathology 78 3.1.1 Goodpasture disease 78 3.1.2 Alport syndrome 79 3.2 COL4A1/COL4A2-associated pathology 81 3.2.1 Ocular dysgenesis 81 3.2.2 Porencephaly 82 3.2.3 Small vessel disease 83 3.2.4 Cerebral cortical lamination defects 84 3.2.5 Myopathy 85 3.2.6 HANAC syndrome and nephropathy 85 4. Mechanisms for Type IV Collagen-Related Pathology 86 4.1 Overview 86 Current Topics in Membranes, Volume 76 ISSN 1063-5823 © 2015 Elsevier Inc. http://dx.doi.org/10.1016/bs.ctm.2015.09.002 All rights reserved. 61 j 62 Mao Mao et al.