The Beneficial Regulation of Extracellular Matrix
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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. -
Immunohistochemical Expression of Tenascin and Elastin In
Clinical Obstetrics, Gynecology and Reproductive Medicine Research Article ISSN: 2059-4828 Immunohistochemical expression of tenascin and elastin in women with pelvic organ prolapse and/or without stress urinary incontinence Ilias Liapis1, Panagiotis Bakas2, Pafiti-Kondi Agatha3, Matrona Frangou-Plemenou4, Charalampos Karachalios5*, Dimos Sioutis6 and Aggelos Liapis2 1Birmingham Women’s and Children’s Hospital, NHS Foundation Trust, Health Education England Midlands and East-West Midlands, Birmingham, England, United Kingdom 2Second Department of Obstetrics and Gynecology, Aretaieio University Hospital, School of Health Sciences, Medical School, National and Kapodistrian University of Athens, Athens, Attica, Greece 3Pathology Laboratory, Aretaieio University Hospital, School of Health Sciences, Medical School, National and Kapodistrian University of Athens, Athens, Attica, Greece 4Microbiology Laboratory, Aretaieio University Hospital, School of Health Sciences, Medical School, National and Kapodistrian University of Athens, Athens, Attica, Greece 5Second Department of Obstetrics and Gynecology, Aretaieio University Hospital, School of Health Sciences, Medical School, National and Kapodistrian University of Athens, Athens, Attica, Greece 6Third Department of Obstetrics and Gynecology, Attikon University Hospital, School of Health Sciences, Medical School, National and Kapodistrian University of Athens, Athens, Attica, Greece Abstract Background and aim: Pelvic organ prolapse (POP) and stress urinary incontinence (SUI) constitute entities of pelvic floor disorders and most often occur simultaneously in the same patient, adversely affecting women’s quality of life. The pathogenesis of pelvic organ prolapse and stress urinary incontinence is not fully understood. The pelvic viscera are maintained in their place thanks to interconnection of levator ani muscles, cardinal and uterosacral ligaments, and pubocervical and rectovaginal fascia. Ligaments and fascia consist mainly of connective tissue. -
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). -
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. -
Dietary Protein Restriction Rapidly Reduces Transforming Growth Factor
Proc. Natl. Acad. Sci. USA Vol. 88, pp. 9765-9769, November 1991 Medical Sciences Dietary protein restriction rapidly reduces transforming growth factor p1 expression in experimental glomerulonephritis (extraceliular matrix/transforming growth factor 8/glomerulonephritis) SEIYA OKUDA*, TAKAMICHI NAKAMURA*, TATSUO YAMAMOTO*, ERKKI RUOSLAHTIt, AND WAYNE A. BORDER*t *Division of Nephrology, University of Utah School of Medicine, Salt Lake City, UT 84132; and tCancer Research Center, La Jolla Cancer Research Foundation, La Jolla, CA 92037 Communicated by Eugene Roberts, August 19, 1991 (receivedfor review April 29, 1991) ABSTRACT Dietary protein restriction has been shown to TGF-/31 on both cell types is to regulate the synthesis of two slow the rate of loss of kidney function in humans with chondroitin/dermatan sulfate proteoglycans, biglycan and progressive glomerulosclerosis due to glomerulonephritis or decorin, both of which can bind TGF-P1 (23). In an experi- diabetes mellitus. A central feature of glomerulosclerosis is the mental model ofglomerulonephritis in the rat, we have found pathological accumulation of extracellular matrix within the a close association between elevated expression of the diseased glomeruli. Transforming growth factor j1 (TGF-.81) TGF-131 gene and the development of glomerulonephritis is known to have widespread regulatory effects on extracellular (10). Seven days after glomerular injury, at the time of matrix and has been implicated as a major cause of increased significant extracellular matrix accumulation, the glomeruli extracellular matrix synthesis and buildup of pathological showed a 5-fold increase in TGF-f31 mRNA and a nearly matrix within glomeruli in experimental glomerulonephritis. 50-fold increase in production ofbiglycan and decorin. -
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. -
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. -
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.