Dietary Protein Restriction Rapidly Reduces Transforming Growth Factor
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Supplementary Table 1: Adhesion Genes Data Set
Supplementary Table 1: Adhesion genes data set PROBE Entrez Gene ID Celera Gene ID Gene_Symbol Gene_Name 160832 1 hCG201364.3 A1BG alpha-1-B glycoprotein 223658 1 hCG201364.3 A1BG alpha-1-B glycoprotein 212988 102 hCG40040.3 ADAM10 ADAM metallopeptidase domain 10 133411 4185 hCG28232.2 ADAM11 ADAM metallopeptidase domain 11 110695 8038 hCG40937.4 ADAM12 ADAM metallopeptidase domain 12 (meltrin alpha) 195222 8038 hCG40937.4 ADAM12 ADAM metallopeptidase domain 12 (meltrin alpha) 165344 8751 hCG20021.3 ADAM15 ADAM metallopeptidase domain 15 (metargidin) 189065 6868 null ADAM17 ADAM metallopeptidase domain 17 (tumor necrosis factor, alpha, converting enzyme) 108119 8728 hCG15398.4 ADAM19 ADAM metallopeptidase domain 19 (meltrin beta) 117763 8748 hCG20675.3 ADAM20 ADAM metallopeptidase domain 20 126448 8747 hCG1785634.2 ADAM21 ADAM metallopeptidase domain 21 208981 8747 hCG1785634.2|hCG2042897 ADAM21 ADAM metallopeptidase domain 21 180903 53616 hCG17212.4 ADAM22 ADAM metallopeptidase domain 22 177272 8745 hCG1811623.1 ADAM23 ADAM metallopeptidase domain 23 102384 10863 hCG1818505.1 ADAM28 ADAM metallopeptidase domain 28 119968 11086 hCG1786734.2 ADAM29 ADAM metallopeptidase domain 29 205542 11085 hCG1997196.1 ADAM30 ADAM metallopeptidase domain 30 148417 80332 hCG39255.4 ADAM33 ADAM metallopeptidase domain 33 140492 8756 hCG1789002.2 ADAM7 ADAM metallopeptidase domain 7 122603 101 hCG1816947.1 ADAM8 ADAM metallopeptidase domain 8 183965 8754 hCG1996391 ADAM9 ADAM metallopeptidase domain 9 (meltrin gamma) 129974 27299 hCG15447.3 ADAMDEC1 ADAM-like, -
Collagen VI-Related Myopathy
Collagen VI-related myopathy Description Collagen VI-related myopathy is a group of disorders that affect skeletal muscles (which are the muscles used for movement) and connective tissue (which provides strength and flexibility to the skin, joints, and other structures throughout the body). Most affected individuals have muscle weakness and joint deformities called contractures that restrict movement of the affected joints and worsen over time. Researchers have described several forms of collagen VI-related myopathy, which range in severity: Bethlem myopathy is the mildest, an intermediate form is moderate in severity, and Ullrich congenital muscular dystrophy is the most severe. People with Bethlem myopathy usually have loose joints (joint laxity) and weak muscle tone (hypotonia) in infancy, but they develop contractures during childhood, typically in their fingers, wrists, elbows, and ankles. Muscle weakness can begin at any age but often appears in childhood to early adulthood. The muscle weakness is slowly progressive, with about two-thirds of affected individuals over age 50 needing walking assistance. Older individuals may develop weakness in respiratory muscles, which can cause breathing problems. Some people with this mild form of collagen VI-related myopathy have skin abnormalities, including small bumps called follicular hyperkeratosis on the arms and legs; soft, velvety skin on the palms of the hands and soles of the feet; and abnormal wound healing that creates shallow scars. The intermediate form of collagen VI-related myopathy is characterized by muscle weakness that begins in infancy. Affected children are able to walk, although walking becomes increasingly difficult starting in early adulthood. They develop contractures in the ankles, elbows, knees, and spine in childhood. -
The Beneficial Regulation of Extracellular Matrix
cosmetics Article The Beneficial Regulation of Extracellular Matrix and Heat Shock Proteins, and the Inhibition of Cellular Oxidative Stress Effects and Inflammatory Cytokines by 1α, 25 dihydroxyvitaminD3 in Non-Irradiated and Ultraviolet Radiated Dermal Fibroblasts Neena Philips *, Xinxing Ding, Pranathi Kandalai, Ilonka Marte, Hunter Krawczyk and Richard Richardson School of Natural Sciences, Fairleigh Dickinson University, Teaneck, NJ 07601, USA * Correspondence: [email protected] or [email protected] Received: 30 June 2019; Accepted: 20 July 2019; Published: 1 August 2019 Abstract: Intrinsic skin aging and photoaging, from exposure to ultraviolet (UV) radiation, are associated with altered regulation of genes associated with the extracellular matrix (ECM) and inflammation, as well as cellular damage from oxidative stress. The regulatory properties of 1α, 25dihydroxyvitamin D3 (vitamin D) include endocrine, ECM regulation, cell differentiation, photoprotection, and anti-inflammation. The goal of this research was to identify the beneficial effects of vitamin D in preventing intrinsic skin aging and photoaging, through its direct effects as well as its effects on the ECM, associated heat shock proteins (HSP-47, and -70), cellular oxidative stress effects, and inflammatory cytokines [interleukin (IL)-1 and IL-8] in non-irradiated, UVA-radiated, UVB-radiated dermal fibroblasts. With regard to the ECM, vitamin D stimulated type I collagen and inhibited cellular elastase activity in non-irradiated fibroblasts; and stimulated type I collagen and HSP-47, and inhibited elastin expression and elastase activity in UVA-radiated dermal fibroblasts. With regard to cellular protection, vitamin D inhibited oxidative damage to DNA, RNA, and lipids in non-irradiated, UVA-radiated and UVB-radiated fibroblasts, and, in addition, increased cell viability of UVB-radiated cells. -
Extracellular Matrix Grafts: from Preparation to Application (Review)
INTERNATIONAL JOURNAL OF MOleCular meDICine 47: 463-474, 2021 Extracellular matrix grafts: From preparation to application (Review) YONGSHENG JIANG1*, RUI LI1,2*, CHUNCHAN HAN1 and LIJIANG HUANG1 1Science and Education Management Center, The Affiliated Xiangshan Hospital of Wenzhou Medical University, Ningbo, Zhejiang 315700; 2School of Chemistry, Sun Yat-sen University, Guangzhou, Guangdong 510275, P.R. China Received July 30, 2020; Accepted December 3, 2020 DOI: 10.3892/ijmm.2020.4818 Abstract. Recently, the increasing emergency of traffic acci- Contents dents and the unsatisfactory outcome of surgical intervention are driving research to seek a novel technology to repair trau- 1. Introduction matic soft tissue injury. From this perspective, decellularized 2. ECM-G characterization matrix grafts (ECM-G) including natural ECM materials, and 3. Methods of decellularization treatments their prepared hydrogels and bioscaffolds, have emerged as 4. Removal of residual cellular components and chemicals possible alternatives for tissue engineering and regenerative 5. Application of ECM-P in regenerative medicine medicine. Over the past decades, several physical and chemical 6. Challenges and future outlook on ECM-P decellularization methods have been used extensively to deal 7. Conclusions with different tissues/organs in an attempt to carefully remove cellular antigens while maintaining the non-immunogenic ECM components. It is anticipated that when the decellular- 1. Introduction ized biomaterials are seeded with cells in vitro or incorporated into irregularly shaped defects in vivo, they can provide the The extracellular matrix (ECM) derived from organs/tissues is appropriate biomechanical and biochemical conditions for a complex, highly organized assembly of macromolecules with directing cell behavior and tissue remodeling. -
Supplementary Materials
Supplementary Materials Figure S1. Bioinformatics evaluation of dystrophin isoform Dp427 and its central position in the molecular pathogenesis of X-linked muscular dystrophy. In order to generate a protein interaction map with known and predicted protein associations that include direct physical and indirect functional protein linkages, the bioinformatics STRING database [1,2] was used to analyse mass spectrometrically-identified proteins with a changed abundance in mdx-4cv skeletal muscles (Tables 1 and 2). S2 Figure S2. Focus of the bioinformatics evaluation of dystrophin isoform Dp427 and its central position in the molecular pathogenesis of X-linked muscular dystrophy. Shown is the middle part of the interaction map of altered muscle-associated proteins from mdx-4cv hind limb muscles, focusing on the central position of the dystrophin protein Dp427 (marked in yellow). In order to generate a protein interaction map with known and predicted protein associations that include direct physical and indirect functional protein linkages, the bioinformatics STRING database [1,2] was used to analyse mass spectrometrically-identified proteins with a changed abundance in mdx-4cv skeletal muscles (Tables 1 and 2). S3 Table S1. List of identified proteins that exhibit a significantly altered concentration in crude mdx-4cv hind limb muscle preparations as revealed by label-free LC-MS/MS analysis. This table contains the statistical q-values of the proteins listed in Tables 1 and 2. Accession Peptide Max Fold Highest Mean Description q Value Number -
Effects of Collagen-Derived Bioactive Peptides and Natural Antioxidant
www.nature.com/scientificreports OPEN Efects of collagen-derived bioactive peptides and natural antioxidant compounds on Received: 29 December 2017 Accepted: 19 June 2018 proliferation and matrix protein Published: xx xx xxxx synthesis by cultured normal human dermal fbroblasts Suzanne Edgar1, Blake Hopley1, Licia Genovese2, Sara Sibilla2, David Laight1 & Janis Shute1 Nutraceuticals containing collagen peptides, vitamins, minerals and antioxidants are innovative functional food supplements that have been clinically shown to have positive efects on skin hydration and elasticity in vivo. In this study, we investigated the interactions between collagen peptides (0.3–8 kDa) and other constituents present in liquid collagen-based nutraceuticals on normal primary dermal fbroblast function in a novel, physiologically relevant, cell culture model crowded with macromolecular dextran sulphate. Collagen peptides signifcantly increased fbroblast elastin synthesis, while signifcantly inhibiting release of MMP-1 and MMP-3 and elastin degradation. The positive efects of the collagen peptides on these responses and on fbroblast proliferation were enhanced in the presence of the antioxidant constituents of the products. These data provide a scientifc, cell-based, rationale for the positive efects of these collagen-based nutraceutical supplements on skin properties, suggesting that enhanced formation of stable dermal fbroblast-derived extracellular matrices may follow their oral consumption. Te biophysical properties of the skin are determined by the interactions between cells, cytokines and growth fac- tors within a network of extracellular matrix (ECM) proteins1. Te fbril-forming collagen type I is the predomi- nant collagen in the skin where it accounts for 90% of the total and plays a major role in structural organisation, integrity and strength2. -
Tendon Extracellular Matrix Remodeling and Defective Cell Polarization in the Presence of Collagen VI Mutations
cells Article Tendon Extracellular Matrix Remodeling and Defective Cell Polarization in the Presence of Collagen VI Mutations Manuela Antoniel 1,2, Francesco Traina 3,4, Luciano Merlini 5 , Davide Andrenacci 1,2, Domenico Tigani 6, Spartaco Santi 1,2, Vittoria Cenni 1,2, Patrizia Sabatelli 1,2,*, Cesare Faldini 7 and Stefano Squarzoni 1,2 1 CNR-Institute of Molecular Genetics “Luigi Luca Cavalli-Sforza”-Unit of Bologna, 40136 Bologna, Italy; [email protected] (M.A.); [email protected] (D.A.); [email protected] (S.S.); [email protected] (V.C.); [email protected] (S.S.) 2 IRCCS Istituto Ortopedico Rizzoli, 40136 Bologna, Italy 3 Ortopedia-Traumatologia e Chirurgia Protesica e dei Reimpianti d’Anca e di Ginocchio, Istituto Ortopedico Rizzoli di Bologna, 40136 Bologna, Italy; [email protected] 4 Dipartimento di Scienze Biomediche, Odontoiatriche e delle Immagini Morfologiche e Funzionali, Università Degli Studi Di Messina, 98122 Messina, Italy 5 Department of Biomedical and Neuromotor Sciences, University of Bologna, 40123 Bologna, Italy; [email protected] 6 Department of Orthopedic and Trauma Surgery, Ospedale Maggiore, 40133 Bologna, Italy; [email protected] 7 1st Orthopaedic and Traumatologic Clinic, IRCCS Istituto Ortopedico Rizzoli, 40136 Bologna, Italy; [email protected] * Correspondence: [email protected]; Tel.: +39-051-6366755; Fax: +39-051-4689922 Received: 20 December 2019; Accepted: 7 February 2020; Published: 11 February 2020 Abstract: Mutations in collagen VI genes cause two major clinical myopathies, Bethlem myopathy (BM) and Ullrich congenital muscular dystrophy (UCMD), and the rarer myosclerosis myopathy. In addition to congenital muscle weakness, patients affected by collagen VI-related myopathies show axial and proximal joint contractures, and distal joint hypermobility, which suggest the involvement of tendon function. -
Biglycan Expression and Its Function in Human Ligamentum Flavum
www.nature.com/scientificreports OPEN Biglycan expression and its function in human ligamentum favum Hamidullah Salimi, Akinobu Suzuki*, Hasibullah Habibi, Kumi Orita, Yusuke Hori, Akito Yabu, Hidetomi Terai, Koji Tamai & Hiroaki Nakamura Hypertrophy of the ligamentum favum (LF) is a major cause of lumbar spinal stenosis (LSS), and the pathology involves disruption of elastic fbers, fbrosis with increased cellularity and collagens, and/or calcifcation. Previous studies have implicated the increased expression of the proteoglycan family in hypertrophied LF. Furthermore, the gene expression profle in a rabbit experimental model of LF hypertrophy revealed that biglycan (BGN) is upregulated in hypertrophied LF by mechanical stress. However, the expression and function of BGN in human LF has not been well elucidated. To investigate the involvement of BGN in the pathomechanism of human ligamentum hypertrophy, frst we confrmed increased expression of BGN by immunohistochemistry in the extracellular matrix of hypertrophied LF of LSS patients compared to LF without hypertrophy. Experiments using primary cell cultures revealed that BGN promoted cell proliferation. Furthermore, BGN induces changes in cell morphology and promotes myofbroblastic diferentiation and cell migration. These efects are observed for both cells from hypertrophied and non-hypertrophied LF. The present study revealed hyper-expression of BGN in hypertrophied LF and function of increased proteoglycan in LF cells. BGN may play a crucial role in the pathophysiology of LF hypertrophy through cell proliferation, myofbroblastic diferentiation, and cell migration. Lumbar spinal stenosis (LSS) is the most common spinal disorder among the elderly population. Hypertrophic changes in the ligamentum favum (LF) are one of the major factors of LSS. -
Biglycan Recruits Utrophin to the Sarcolemma and Counters Dystrophic Pathology in Mdx Mice
Biglycan recruits utrophin to the sarcolemma and counters dystrophic pathology in mdx mice Alison R. Amentaa, Atilgan Yilmazb, Sasha Bogdanovichc, Beth A. McKechniea, Mehrdad Abedid, Tejvir S. Khuranac, and Justin R. Fallona,1 aDepartment of Neuroscience and bDepartment of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, RI 02912; cDepartment of Physiology and Pennsylvania Muscle Institute, University of Pennsylvania School of Medicine, Philadelphia, PA 19104; and dDivision of Hematology and Oncology, University of California–Davis Medical Center, Sacramento, CA 95817 Edited by Louis M. Kunkel, Children’s Hospital Boston, Boston, MA, and approved November 22, 2010 (received for review September 2, 2010) Duchenne muscular dystrophy (DMD) is caused by mutations in dys- associated utrophin in cultured myotubes. Importantly, rhBGN trophin and the subsequent disruption of the dystrophin-associated can be delivered systemically to dystrophin-deficient mdx mice, protein complex (DAPC). Utrophin is a dystrophin homolog ex- where it up-regulates utrophin and other DAPC components at pressed at high levels in developing muscle that is an attractive the sarcolemma, ameliorates muscle pathology, and improves target for DMD therapy. Here we show that the extracellular matrix function. Several lines of evidence indicate that biglycan acts by protein biglycan regulates utrophin expression in immature muscle recruiting utrophin to the plasma membrane. We propose rhBGN and that recombinant human biglycan (rhBGN) increases utrophin as a candidate therapeutic for DMD. expression in cultured myotubes. Systemically delivered rhBGN up- regulates utrophin at the sarcolemma and reduces muscle pathology Results in the mdx mouse model of DMD. RhBGN treatment also improves Endogenous Biglycan Regulates Utrophin Expression in Immature muscle function as judged by reduced susceptibility to eccentric Muscle. -
Type VI Collagen Regulates Dermal Matrix Assembly and Fibroblast Motility
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by LSBU Research Open Accepted Article Preview: Published ahead of advance online publication www.jidonline.org Type VI Collagen Regulates Dermal Matrix Assembly and Fibroblast Motility Georgios Theocharidis, Zoe Drymoussi, Alexander P Kao, Asa H Barber, David A Lee, Kristin M Braun, John T Connelly Cite this article as: Georgios Theocharidis, Zoe Drymoussi, Alexander P Kao, Asa H Barber, David A Lee, Kristin M Braun, John T Connelly, Type VI Collagen Regulates Dermal Matrix Assembly and Fibroblast Motility, Journal of Investigative Dermatology accepted article preview 9 September 2015; doi: 10.1038/jid.2015.352. This is a PDF file of an unedited peer-reviewed manuscript that has been accepted for publication. NPG are providing this early version of the manuscript as a service to our customers. The manuscript will undergo copyediting, typesetting and a proof review before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers apply. Received 31 March 2015; revised 16 July 2015; accepted 17 August 2015; Accepted article preview online 9 September 2015 © 2015 The Society for Investigative Dermatology Type VI collagen regulates dermal matrix assembly and fibroblast motility Georgios Theocharidis1, Zoe Drymoussi1, Alexander P. Kao2, Asa H. Barber2,3 David A. Lee2, Kristin M. Braun1, John T. Connelly1* 1. Centre for Cell Biology and Cutaneous Research, Barts and the London School of Medicine and Dentistry, Queen Mary, University of London. 2. Institute of Bioengineering, School of Engineering and Materials Science, Queen Mary, University of London. -
Decorin and Biglycan Expression and Distribution During
DECORIN AND BIGLYCAN EXPRESSION AND DISTRIBUTION DURING PALATAL SHELF ADHESION A Thesis by ISRA M. IBRAHIM Submitted to the Office of Graduate and Professional Studies of Texas A&M University in partial fulfillment of the requirements for the degree of MASTER OF SCIENCE Chair of Committee, Kathy Svoboda Committee Members, Louis-Bruno Ruest Xiaofang Wang Head of Department, Paul Dechow May 2015 Major Subject: Oral Biology Copyright 2015 Isra M. Ibrahim ABSTRACT Understanding the molecular events in palate development is a prerequisite to more effective treatments of cleft palate. The secondary palate in humans and mice forms from shelves of mesenchyme covered with medial edge epithelium (MEE). These shelves adhere to form the midline epithelial seam (MES). MES cells then proceed through epithelial to mesenchymal transition (EMT) and/or apoptosis to yield a fused palate. Adhesion of opposing MEE is a crucial event whose alteration causes cleft palate. Previous studies showed that chondroitin sulphate proteoglycans (CSPG) on the apical surfaces of MEE was an important factor in palatal shelf adhesion. In this study we investigated decorin and biglycan, being expressed in numerous craniofacial tissues, as potential proteoglycans involved in palatal shelf adhesion. We used a laser capture microdissection (LCM) technique to collect MEE cells and real-time polymerase chain reaction, to determine mRNA levels of decorin and biglycan that correctly reflect changes in gene expression during various stages of palatal shelf fusion (Embryonic days 13.5, 14.0 and 14.5). Both decorin and biglycan were expressed on the apical surface as well as between the MEE cells. We found that biglycan protein and mRNA levels peaked as the palatal shelves adhered. -
The Structure and Function of Cartilage Proteoglycans
PJEuropean Roughley Cells and Materials Vol. 12. 2006 (pages 92-101) DOI: 10.22203/eCM.v012a11 Cartilage ISSN proteoglycans 1473-2262 THE STRUCTURE AND FUNCTION OF CARTILAGE PROTEOGLYCANS P.J. Roughley* Genetics Unit, Shriners Hospital for Children and Department of Surgery, McGill University, Montreal, Quebec, Canada Abstract Introduction Cartilage contains a variety of proteoglycans that are Cartilagenous tissues are present throughout the body at essential for its normal function. These include aggrecan, numerous sites and are classified histologically as being decorin, biglycan, fibromodulin and lumican. Each hyaline, elastic or fibrocartilagenous in nature, depending proteoglycan serves several functions that are determined on their molecular composition. Elastic cartilage is by both its core protein and its glycosaminoglycan chains. associated with the ear and the larynx, whereas This review discusses the structure/function relationships fibrocartilage is associated with the menisci of the knee of the cartilage proteoglycans, and the manner in which and the intervertebral discs. Hyaline cartilage is the perturbations in proteoglycan structure or abundance can predominant form of cartilage, and is most commonly adversely affect tissue function. associated with the skeletal system, where it forms the anlage for many bones in the embryo, the growth plate Key Words: Proteoglycan, aggrecan, link protein, via which many bones increase their size during juvenile hyaluronan, decorin, biglycan, fibromodulin, lumican, development, and the bearing surface upon which bones cartilage. articulate in movable joints. It is not clear whether articular cartilage can be defined as a distinct tissue in the juvenile, as it forms a continuum with the hyaline cartilage of the central epiphysis, which is destined to be resorbed.