Immunohistochemical Expression of Tenascin and Elastin In
Total Page:16
File Type:pdf, Size:1020Kb
Load more
Recommended publications
-
Recombinant Laminin Α5 LG1-3 Domains Support the Stemness of Human Mesenchymal Stem Cells
EXPERIMENTAL AND THERAPEUTIC MEDICINE 21: 166, 2021 Recombinant laminin α5 LG1-3 domains support the stemness of human mesenchymal stem cells SUJIN LEE1*, DONG‑SUNG LEE2* and JUN‑HYEOG JANG1 1Department of Biochemistry, College of Medicine, Inha University, Incheon 22212; 2College of Pharmacy, Chosun University, Gwangju 61452, Republic of Korea Received April 23, 2020; Accepted November 24, 2020 DOI: 10.3892/etm.2020.9597 Abstract. The extracellular matrix components laminin and be met by mimicking the in vivo extracellular matrix (ECM) elastin serve key roles in stem cell therapy. Elastin‑like poly‑ configuration, thereby modulating the activity of stem cells peptides (ELPs), derived from a soluble form of elastin, affect in vitro (2). The principle behind this hypothesis is that the the proliferation and differentiation of various types of cells. ECM not only functions as structural support for stem cells In the present study, a novel protein was designed containing in vivo but also provides biochemical cues for their mainte‑ globular domains 1‑3 of laminin α5 (Lα5LG1‑3) fused to nance versus directed differentiation (3). ELPs (Lα5LG1‑3/ELP). Lα5LG1‑3/ELP was expressed in Basement membranes (BMs) are a subgroup of the ECM Escherichia coli and displayed a molecular size of ~70 kDa that is necessary for cell differentiation during early devel‑ on 12% SDS‑polyacrylamide gels. The cellular activities, opmental processes. In addition, BMs are critical for the such as cellular adhesion (adhesion assay) and proliferation formation and maintenance of mature tissues (4,5). Laminin, (MTT cytotoxicity assay), of human mesenchymal stem one of the components of BMs, consists of three genetically cells (hMSCs) treated with 1 µg/ml of Lα5LG1‑3/ELP were distinct subunits called α, β and γ chains, which are assembled enhanced compared with those of untreated cells. -
Collagen and Elastin Fibres
J Clin Pathol: first published as 10.1136/jcp.s3-12.1.49 on 1 January 1978. Downloaded from J. clin. Path., 31, Suppl. (Roy. Coll. Path.), 12, 49-58 Collagen and elastin fibres A. J. BAILEY From the Agricultural Research Council, Meat Research Institute, Langford, Bristol Although an understanding of the intracellular native collagen was generated from type I pro- biosynthesis of both collagen and elastin is of collagen. Whether this means that the two pro- considerable importance it is the subsequent extra- collagens are converted by different enzyme systems cellular changes involving fibrogenesis and cross- and the type III enzyme was deficient in these linking that ensure that these proteins ultimately fibroblast cultures, or that the processing of pro become the major supporting tissues of the body. type III is extremely slow, is not known. The latter This paper summarises the formation and stability proposal is consistent with the higher proportion of collagen and elastin fibres. of soluble pro type III extractable from tissue (Lenaers and Lapiere, 1975; Timpl et al., 1975). Collagen Basement membrane collagens, on the other hand, do not form fibres and this property may be The non-helical regions at the ends of the triple due to the retention of the non-helical extension helix of procollagen probably provide a number of peptides (Kefalides, 1973). In-vivo biosynthetic different intracellular functions-that is, initiating studies showing the absence of any extension peptide rapid formation of the triple helix; inhibiting intra- removal support this (Minor et al., 1976), but other cellular fibrillogenesis; and facilitating transmem- workers have reported that there is some cleavage brane movement. -
Evaluation of Elastin/Collagen Content in Human Dermis In-Vivo by Multiphoton Tomography—Variation with Depth and Correlation with Aging
Cosmetics 2014, 1, 211-221; doi:10.3390/cosmetics1030211 OPEN ACCESS cosmetics ISSN 2079-9284 www.mdpi.com/journal/cosmetics Article Evaluation of Elastin/Collagen Content in Human Dermis in-Vivo by Multiphoton Tomography—Variation with Depth and Correlation with Aging Jean-Christophe Pittet 1,*, Olga Freis 2,†, Marie-Danielle Vazquez-Duchêne 2,†, Gilles Périé 2,† and Gilles Pauly 2,† 1 Orion Concept, 100 Rue de Suède, 37100 Tours, France 2 BASF Beauty Care Solutions France SAS, 3 Rue de Seichamps, CS 71040 Pulnoy, 54272 Essey-lès-Nancy Cedex, France; E-Mails: [email protected] (O.F.); [email protected] (M.-D.V.-D.); [email protected] (G.Pé.); [email protected] (G.Pa.) † These authors contributed equally to this work. * Author to whom correspondence should be addressed; E-Mail: [email protected]; Tel.: +33-247-052-316; Fax: +33-610-786-695. Received: 14 March 2014; in revised form: 31 July 2014 / Accepted: 1 August 2014 / Published: 20 August 2014 Abstract: The aim of this study was to evaluate the influence of the depth of the dermis on the measured collagen and elastin levels and to establish the correlation between the amount of these two extracellular matrix (ECM) components and age. Multiphoton Microscopy (MPM) that measures the autofluorescence (AF) and second harmonic generation (SHG) was used to quantify the levels of elastin and collagen and to determine the SAAID (SHG-to-AF Aging Index of Dermis) at two different skin depths. A 50 MHz ultrasound scanner was used for the calculation of the Sub Epidermal Non Echogenic Band (SENEB). -
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. -
Proteins and Peptides As Important Modifiers of the Polymer Scaffolds
polymers Review Proteins and Peptides as Important Modifiers of the Polymer Scaffolds for Tissue Engineering Applications—A Review Katarzyna Klimek * and Grazyna Ginalska Chair and Department of Biochemistry and Biotechnology, Medical University of Lublin, Chodzki 1 Street, 20-093 Lublin, Poland; [email protected] * Correspondence: [email protected]; Tel.: +48-81-448-7028; +48-81-448-7020 Received: 29 January 2020; Accepted: 2 April 2020; Published: 6 April 2020 Abstract: Polymer scaffolds constitute a very interesting strategy for tissue engineering. Even though they are generally non-toxic, in some cases, they may not provide suitable support for cell adhesion, proliferation, and differentiation, which decelerates tissue regeneration. To improve biological properties, scaffolds are frequently enriched with bioactive molecules, inter alia extracellular matrix proteins, adhesive peptides, growth factors, hormones, and cytokines. Although there are many papers describing synthesis and properties of polymer scaffolds enriched with proteins or peptides, few reviews comprehensively summarize these bioactive molecules. Thus, this review presents the current knowledge about the most important proteins and peptides used for modification of polymer scaffolds for tissue engineering. This paper also describes the influence of addition of proteins and peptides on physicochemical, mechanical, and biological properties of polymer scaffolds. Moreover, this article sums up the major applications of some biodegradable natural and synthetic polymer scaffolds modified with proteins and peptides, which have been developed within the past five years. Keywords: bioactive construct; biocompatibility; biomolecules; cytotoxicity; ECM; hydrogels; protein carrier; regenerative medicine; stem cells; tissue repair 1. Introduction: The Role of Proteins and Peptides in TE Tissue engineering (TE) is a multidisciplinary field, which constitutes an alternative and promising approach for grafts, i.e., autografts, allografts, and xenografts [1–3]. -
Elastin Biology and Tissue Engineering with Adult Cells
DOI 10.1515/bmc-2012-0040 BioMol Concepts 2013; 4(2): 173–185 Review Cassandra B. Saitow * , Steven G. Wise, Anthony S. Weiss , John J. Castellot Jr. and David L. Kaplan Elastin biology and tissue engineering with adult cells Abstract: The inability of adult cells to produce well-organ- collagen to allow for repeated cycles of expansion and ized, robust elastic fibers has long been a barrier to the contraction in response to pulsatile flow (3) . This review successful engineering of certain tissues. In this review, focuses primarily on blood vessel tissue engineering, we focus primarily on elastin with respect to tissue-engi- particularly the challenge of inducing sufficient elastin neered vascular substitutes. To understand elastin regu- expression from cells that colonize vascular constructs. lation during normal development, we describe the role Developmental regulation of elastin dictates that of various elastic fiber accessory proteins. Biochemical synthesis is predominantly in utero and early childhood pathways regulating expression of the elastin gene are (4) . New elastic fibers are not produced in appreciable addressed, with particular focus on tissue-engineering amounts under normal physiological circumstances in research using adult-derived cells. adult cells. This deficit presents a significant challenge in tissue engineering of vascular constructs that seek Keywords: elastin; heparin; smooth muscle cell; vascular to replicate the elastin content of natural vessels. This tissue engineering. review considers factors involved in elastic fiber forma- tion during normal development and addresses recent advances in the induction of elastin expression by cells *Corresponding author : Cassandra B. Saitow, Tufts University, from adult donors. Department of Biomedical Engineering, Medford, MA, 02155 , USA, e-mail: [email protected] Steven G. -
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. -
Incorporation of Recombinant Fibronectin Into Genetically Engineered Elastin-Based Polymers
Incorporation of Recombinant Fibronectin Into Genetically Engineered Elastin-based Polymers A Thesis Presented to The Academic Faculty by Fanor Alberto Balderrama In Partial Fulfillment of the Requirements for the Degree Master of Science in the School of Bioengineering Georgia Institute of Technology December 2009 Incorporation of Recombinant Fibronectin Into Genetically Engineered Elastin-based Polymers Approved by: Dr. Elliot L. Chaikof, Advisor School of Biomedical Engineering Georgia Institute of Technology Department of Surgery Emory University School of Medicine Dr. Hanjoong Jo School of Biomedical Engineering Georgia Institute of Technology Division of Cardiology Emory University School of Medicine Dr. Vincent P. Conticello School of Chemistry Emory University Date Approved: November 11, 2009 ACKNOWLEDGEMENTS I would like to thank my advisor, Dr. Elliot Chaikof, for the opportunity of working on this research and for all the guidance. I would also like to thank Dr. Carolyn Haller for all her priceless guidance, her supervision and patience, without which this thesis would have not been possible. My sincere appreciation goes out to members of my committee: Dr. Hanjoong Jo and Dr. Vincent Conticello for their help with the direction and the review of this thesis. I would also like to thank all the other members of the Chaikof laboratory for their friendship, their help and their advice, without which my research experience would have not been so enjoyable. Last, but absolutely not least, I thank my family for all their support (professional, emotional and even financial) and their faith in me. iii TABLE OF CONTENTS Acknowledgements iii List of figures vii List of abbreviations viii Summary x Chapter I: Introduction 1 1.1. -
Concepts of Extracellular Matrix Remodelling in Tumour Progression and Metastasis ✉ Juliane Winkler 1,2 , Abisola Abisoye-Ogunniyan 1,2, Kevin J
REVIEW ARTICLE https://doi.org/10.1038/s41467-020-18794-x OPEN Concepts of extracellular matrix remodelling in tumour progression and metastasis ✉ Juliane Winkler 1,2 , Abisola Abisoye-Ogunniyan 1,2, Kevin J. Metcalf 1 & Zena Werb 1,3 Tissues are dynamically shaped by bidirectional communication between resident cells and the extracellular matrix (ECM) through cell-matrix interactions and ECM remodelling. 1234567890():,; Tumours leverage ECM remodelling to create a microenvironment that promotes tumour- igenesis and metastasis. In this review, we focus on how tumour and tumour-associated stromal cells deposit, biochemically and biophysically modify, and degrade tumour- associated ECM. These tumour-driven changes support tumour growth, increase migration of tumour cells, and remodel the ECM in distant organs to allow for metastatic progression. A better understanding of the underlying mechanisms of tumourigenic ECM remodelling is crucial for developing therapeutic treatments for patients. ellular phenotypes and molecular functions are fundamentally dependent on signals from Coutside the cell such as the interactions with the extracellular matrix (ECM). The core matrisome is composed of ~300 unique matrix macromolecules and can be classified into collagens, proteoglycans (such as heparan sulphate proteoglycans, versican and hyaluronan) and glycoproteins (such as laminins, elastin, fibronectin and tenascins)1. These ECM compo- nents are modified post-translationally by an array of secreted remodelling enzymes, such as oxidases and proteases. In addition, the ECM binds soluble factors, such as growth factors and other ECM-associated proteins. Cell surface receptors interact with ECM components and ECM- bound factors to mediate cell adhesion and cell signalling thereby regulating processes as diverse as proliferation, differentiation, migration and apoptosis2. -
Spatial and Temporal Changes in Extracellular Elastin and Laminin
www.nature.com/scientificreports OPEN Spatial and temporal changes in extracellular elastin and laminin distribution during lung alveolar Received: 18 December 2017 Accepted: 17 May 2018 development Published: xx xx xxxx Yongfeng Luo1, Nan Li1, Hui Chen1, G. Esteban Fernandez1, David Warburton1,2, Rex Moats1,3, Robert P. Mecham4, Daria Krenitsky5, Gloria S. Pryhuber5 & Wei Shi1,2 Lung alveolarization requires precise coordination of cell growth with extracellular matrix (ECM) synthesis and deposition. The role of extracellular matrices in alveogenesis is not fully understood, because prior knowledge is largely extrapolated from two-dimensional structural analysis. Herein, we studied temporospatial changes of two important ECM proteins, laminin and elastin that are tightly associated with alveolar capillary growth and lung elastic recoil respectively, during both mouse and human lung alveolarization. By combining protein immunofuorescence staining with two- and three- dimensional imaging, we found that the laminin network was simplifed along with the thinning of septal walls during alveogenesis, and more tightly associated with alveolar endothelial cells in matured lung. In contrast, elastin fbers were initially localized to the saccular openings of nascent alveoli, forming a ring-like structure. Then, throughout alveolar growth, the number of such alveolar mouth ring-like structures increased, while the relative ring size decreased. These rings were interconnected via additional elastin fbers. The apparent patches and dots of elastin at the tips of alveolar septae found in two-dimensional images were cross sections of elastin ring fbers in the three-dimension. Thus, the previous concept that deposition of elastin at alveolar tips drives septal inward growth may potentially be conceptually challenged by our data. -
Tenascins in Stem Cell Niches
MATBIO-01031; No of Pages 12 Matrix Biology xxx (2014) xxx–xxx Contents lists available at ScienceDirect Matrix Biology journal homepage: www.elsevier.com/locate/matbio Tenascins in stem cell niches Ruth Chiquet-Ehrismann a,b,⁎,1,GertraudOrendc,d,e,f,1, Matthias Chiquet g,1, Richard P. Tucker h,1, Kim S. Midwood i,1 a Friedrich Miescher Institute of Biomedical Research, Novartis Research Foundation, Maulbeerstrasse 66 CH-4058 Basel, Switzerland b Faculty of Sciences, University of Basel, Switzerland c Inserm U1109, The Microenvironmental Niche in Tumorigenesis and Targeted Therapy (MNT3) Team, 3 av. Molière, 67200 Strasbourg, France d Université de Strasbourg, 67000 Strasbourg, France e LabEx Medalis, Université de Strasbourg, 67000 Strasbourg, France f Fédération de Médecine Translationnelle de Strasbourg (FMTS), 67000 Strasbourg, France g Department of Orthodontics and Dentofacial Orthopedics, University of Bern, Freiburgstrasse 7, CH-3010 Bern, Switzerland h Department of Cell Biology and Human Anatomy, University of California Davis, Davis, CA 95616, USA i The Kennedy Institute of Rheumatology, University of Oxford, Roosevelt Drive, Headington, Oxford OX3 7FY, United Kingdom article info abstract Available online xxxx Tenascins are extracellular matrix proteins with distinct spatial and temporal expression during development, tissue homeostasis and disease. Based on their expression patterns and knockout phenotypes an important Keywords: role of tenascins in tissue formation, cell adhesion modulation, regulation of proliferation and -
Tenascin-X Increases the Stiffness of Collagen Gels Without Affecting
Tenascin-X increases the stiffness of collagen gels without affecting fibrillogenesis Yoran Margaron, Luciana Bostan, Jean-Yves Exposito, Maryline Malbouyres, Ana-Maria Trunfio-Sfarghiu, Yves Berthier, Claire Lethias To cite this version: Yoran Margaron, Luciana Bostan, Jean-Yves Exposito, Maryline Malbouyres, Ana-Maria Trunfio- Sfarghiu, et al.. Tenascin-X increases the stiffness of collagen gels without affecting fibrillogenesis. Biophysical Chemistry, Elsevier, 2010, 147 (1-2), pp.87. 10.1016/j.bpc.2009.12.011. hal-00612709 HAL Id: hal-00612709 https://hal.archives-ouvertes.fr/hal-00612709 Submitted on 30 Jul 2011 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. ÔØ ÅÒÙ×Ö ÔØ Tenascin-X increases the stiffness of collagen gels without affecting fibrillo- genesis Yoran Margaron, Luciana Bostan, Jean-Yves Exposito, Maryline Mal- bouyres, Ana-Maria Trunfio-Sfarghiu, Yves Berthier, Claire Lethias PII: S0301-4622(09)00256-7 DOI: doi: 10.1016/j.bpc.2009.12.011 Reference: BIOCHE 5329 To appear in: Biophysical Chemistry Received date: 10 November 2009 Revised date: 23 December 2009 Accepted date: 27 December 2009 Please cite this article as: Yoran Margaron, Luciana Bostan, Jean-Yves Exposito, Mary- line Malbouyres, Ana-Maria Trunfio-Sfarghiu, Yves Berthier, Claire Lethias, Tenascin-X increases the stiffness of collagen gels without affecting fibrillogenesis, Biophysical Chem- istry (2010), doi: 10.1016/j.bpc.2009.12.011 This is a PDF file of an unedited manuscript that has been accepted for publication.