Time-Resolved Analysis of the Matrix Metalloproteinase 10 Substrate Degradome
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Inflammation-Mediated Skin Tumorigenesis Induced by Epidermal C-Fos
Downloaded from genesdev.cshlp.org on September 29, 2021 - Published by Cold Spring Harbor Laboratory Press Inflammation-mediated skin tumorigenesis induced by epidermal c-Fos Eva M. Briso,1 Juan Guinea-Viniegra,1 Latifa Bakiri,1 Zbigniew Rogon,2 Peter Petzelbauer,3 Roland Eils,2 Ronald Wolf,4 Mercedes Rinco´ n,5 Peter Angel,6 and Erwin F. Wagner1,7 1BBVA Foundation-Spanish National Cancer Research Center (CNIO) Cancer Cell Biology Program, CNIO, 28029 Madrid, Spain; 2Division of Theoretical Bioinformatics, German Cancer Research Center (DKFZ), 69120 Heidelberg, Germany; 3Skin and Endothelium Research Division (SERD), Department of Dermatology, Medical University of Vienna, A-1090 Vienna, Austria; 4Department of Dermatology and Allergology, Ludwig-Maximilian University, Munich, Germany; 5Division of Immunobiology, Department of Medicine, University of Vermont, 05405 Burlington, Vermont, USA; 6Division of Signal Transduction and Growth Control, DKFZ, DKFZ-Center for Molecular Biology of the University of Heidelberg (ZMBH) Alliance, 69120 Heidelberg, Germany Skin squamous cell carcinomas (SCCs) are the second most prevalent skin cancers. Chronic skin inflammation has been associated with the development of SCCs, but the contribution of skin inflammation to SCC development remains largely unknown. In this study, we demonstrate that inducible expression of c-fos in the epidermis of adult mice is sufficient to promote inflammation-mediated epidermal hyperplasia, leading to the development of preneoplastic lesions. Interestingly, c-Fos transcriptionally controls mmp10 and s100a7a15 expression in keratinocytes, subsequently leading to CD4 T-cell recruitment to the skin, thereby promoting epidermal hyperplasia that is likely induced by CD4 T-cell-derived IL-22. Combining inducible c-fos expression in the epidermis with a single dose of the carcinogen 7,12-dimethylbenz(a)anthracene (DMBA) leads to the development of highly invasive SCCs, which are prevented by using the anti-inflammatory drug sulindac. -
Discovery and Optimization of Selective Inhibitors of Meprin Α (Part II)
pharmaceuticals Article Discovery and Optimization of Selective Inhibitors of Meprin α (Part II) Chao Wang 1,2, Juan Diez 3, Hajeung Park 1, Christoph Becker-Pauly 4 , Gregg B. Fields 5 , Timothy P. Spicer 1,6, Louis D. Scampavia 1,6, Dmitriy Minond 2,7 and Thomas D. Bannister 1,2,* 1 Department of Molecular Medicine, Scripps Research, Jupiter, FL 33458, USA; [email protected] (C.W.); [email protected] (H.P.); [email protected] (T.P.S.); [email protected] (L.D.S.) 2 Department of Chemistry, Scripps Research, Jupiter, FL 33458, USA; [email protected] 3 Rumbaugh-Goodwin Institute for Cancer Research, Nova Southeastern University, 3321 College Avenue, CCR r.605, Fort Lauderdale, FL 33314, USA; [email protected] 4 The Scripps Research Molecular Screening Center, Scripps Research, Jupiter, FL 33458, USA; [email protected] 5 Unit for Degradomics of the Protease Web, Institute of Biochemistry, University of Kiel, Rudolf-Höber-Str.1, 24118 Kiel, Germany; fi[email protected] 6 Department of Chemistry & Biochemistry and I-HEALTH, Florida Atlantic University, 5353 Parkside Drive, Jupiter, FL 33458, USA 7 Dr. Kiran C. Patel College of Allopathic Medicine, Nova Southeastern University, 3301 College Avenue, Fort Lauderdale, FL 33314, USA * Correspondence: [email protected] Abstract: Meprin α is a zinc metalloproteinase (metzincin) that has been implicated in multiple diseases, including fibrosis and cancers. It has proven difficult to find small molecules that are capable Citation: Wang, C.; Diez, J.; Park, H.; of selectively inhibiting meprin α, or its close relative meprin β, over numerous other metzincins Becker-Pauly, C.; Fields, G.B.; Spicer, which, if inhibited, would elicit unwanted effects. -
2335 Roles of Molecules Involved in Epithelial/Mesenchymal Transition
[Frontiers in Bioscience 13, 2335-2355, January 1, 2008] Roles of molecules involved in epithelial/mesenchymal transition during angiogenesis Giulio Ghersi Dipartimento di Biologia Cellulare e dello Sviluppo, Universita di Palermo, Italy TABLE OF CONTENTS 1. Abstract 2. Introduction 3. Extracellular matrix 3.1. ECM and integrins 3.2. Basal lamina components 4. Cadherins. 4.1. Cadherins in angiogenesis 5. Integrins. 5.1. Integrins in angiogenesis 6. Focal adhesion molecules 7. Proteolytic enzymes 7.1. Proteolytic enzymes inhibitors 7.2. Proteolytic enzymes in angiogenesis 8. Perspective 9. Acknowledgements 10. References 1.ABSTRACT 2. INTRODUCTION Formation of vessels requires “epithelial- Growth of new blood vessels (angiogenesis) mesenchymal” transition of endothelial cells, with several plays a key role in several physiological processes, such modifications at the level of endothelial cell plasma as vascular remodeling during embryogenesis and membranes. These processes are associated with wound healing tissue repair in the adult; as well as redistribution of cell-cell and cell-substrate adhesion pathological processes, including rheumatoid arthritis, molecules, cross talk between external ECM and internal diabetic retinopathy, psoriasis, hemangiomas, and cytoskeleton through focal adhesion molecules and the cancer (1). Vessel formation entails the “epithelial- expression of several proteolytic enzymes, including matrix mesenchymal” transition of endothelial cells (ECs) “in metalloproteases and serine proteases. These enzymes with vivo”; a similar phenotypic exchange can be induced “in their degradative action on ECM components, generate vitro” by growing ECs to low cell density, or in “wound molecules acting as activators and/or inhibitors of healing” experiments or perturbing cell adhesion and angiogenesis. The purpose of this review is to provide an associated molecule functions. -
On and Polymorphisms in Q Fever
Matrix metalloproteinase expression, produc3on and polymorphisms in Q fever Anne F.M. Jansen1,2, Teske Schoffelen1,2, Julien Textoris3, Jean Louis Mege3, Chantal P. Bleeker-Rovers1,2, Esther van de Vosse4, Hendrik Jan Roest5, Marcel van Deuren1,2 1. Department of Internal Medicine, Division of Experimental Medicine, Radboud university medical center, Nijmegen, The Netherlands 2. Radboud Expert Centre for Q fever, Radboud university medical center, Nijmegen, the Netherlands, 3. URMITE, CNRS UMR 7278, IRD 198, INSERM 1095 Aix-Marseille University, Marseille, France 4. Department of Infec3ous Diseases, Leiden University Medical Center, Leiden, The Netherlands 5. Department of Bacteriology and TSEs, Central Veterinary Instute, part of Wageningen UR, Lelystad, the Netherlands Background C. burnei induces MMP-1 and MMP-9 produc3on in PBMCs Chronic Q fever is a life threatening condi3on caused by the Gram-negave bacterium Coxiella burnei, manifes3ng as an infec3on of aneurysms, aor3c prosthesis or heart valves. Matrix metalloproteinases (MMPs) are proteoly3c enzymes that cleave extracellular matrix and are implicated in the pathology of aneurysms and endocardi3s. Currently, the contribu3on of MMPs to the pathogenesis of chronic Q fever is unknown. Methods We inves3gated the C. burnei specific gene expression of MMPs in PBMCs and protein produc3on by ELISA in chronic Q fever paents (n=6, n=10, respec3vely), cardiovascular paents with a history of Q fever (n=10) and healthy controls (n=4, n=10, respec3vely), in some experiments, the controls had vascular disease (n=10). Circulang MMP levels were assessed with Luminex technology and these groups were also genotyped for 20 SNPs in MMP and Tissue Inhibitor of MMP (TIMP) genes. -
An Adverse Role for Matrix Metalloproteinase 12 After Spinal Cord Injury in Mice
The Journal of Neuroscience, November 5, 2003 • 23(31):10107–10115 • 10107 Development/Plasticity/Repair An Adverse Role for Matrix Metalloproteinase 12 after Spinal Cord Injury in Mice Jennifer E. A. Wells,1 Tiffany K. Rice,1 Robert K. Nuttall,3 Dylan R. Edwards,3 Hakima Zekki,4 Serge Rivest,4 V. Wee Yong1,2 Departments of 1Clinical Neurosciences and 2Oncology, Faculty of Medicine, University of Calgary, Calgary, Alberta T2N 4N1, Canada, 3School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, United Kingdom, and 4Laboratory of Molecular Endocrinology and Department of Anatomy and Physiology, Laval University, Quebec, Quebec G1V 4G2, Canada We investigated the role of matrix metalloproteinases (MMPs) in acute spinal cord injury (SCI). Transcripts encoding 22 of the 23 known mammalian MMPs were measured in the mouse spinal cord at various time points after injury. Although there were significant changes in the expression levels of multiple MMPs, MMP-12 was increased 189-fold over normal levels, the highest of all MMPs examined. To evaluate the role of MMP-12 in SCI, spinal cord compression was performed in wild-type (WT) and MMP-12 null mice. Behavioral analyses were conducted for 4 weeks using the Basso–Beattie–Bresnahan (BBB) locomotor rating scale as well as the inclined plane test. The results show that MMP-12 null mice exhibited significantly improved functional recovery compared with WT controls. Twenty-eight days after injury, the BBB score in the MMP-12 group was 7, representing extensive movement of all three hindlimb joints, compared with 4 in the WT group, representing only slight movement of these joints. -
Effect of Nanoparticles on the Expression and Activity of Matrix Metalloproteinases
Nanotechnol Rev 2018; 7(6): 541–553 Review Magdalena Matysiak-Kucharek*, Magdalena Czajka, Krzysztof Sawicki, Marcin Kruszewski and Lucyna Kapka-Skrzypczak Effect of nanoparticles on the expression and activity of matrix metalloproteinases https://doi.org/10.1515/ntrev-2018-0110 Received September 14, 2018; accepted October 11, 2018; previously 1 Introduction published online November 15, 2018 Matrix metallopeptidases, commonly known as matrix Abstract: Matrix metallopeptidases, commonly known metalloproteinases (MMPs), are zinc-dependent proteo- as matrix metalloproteinases (MMPs), are a group of pro- lytic enzymes whose primary function is the degradation teolytic enzymes whose main function is the remodeling and remodeling of extracellular matrix (ECM) compo- of the extracellular matrix. Changes in the activity of nents. ECM is a complex, dynamic structure that condi- these enzymes are observed in many pathological states, tions the proper tissue architecture. MMPs by digesting including cancer metastases. An increasing body of evi- ECM proteins eliminate structural barriers and allow dence indicates that nanoparticles (NPs) can lead to the cell migration. Moreover, by hydrolyzing extracellularly deregulation of MMP expression and/or activity both in released proteins, MMPs can change the activity of many vitro and in vivo. In this work, we summarized the current signal peptides, such as growth factors, cytokines, and state of knowledge on the impact of NPs on MMPs. The chemokines. MMPs are involved in many physiological literature analysis showed that the impact of NPs on MMP processes, such as embryogenesis, reproduction cycle, or expression and/or activity is inconclusive. NPs exhibit wound healing; however, their increased activity is also both stimulating and inhibitory effects, which might be associated with a number of pathological conditions, such dependent on multiple factors, such as NP size and coat- as diabetes, cardiovascular diseases and neurodegenera- ing or a cellular model used in the research. -
(MMP10) Moderates Inflammation by Controlling Macrophage Activation
Stromelysin-2 (MMP10) Moderates Inflammation by Controlling Macrophage Activation This information is current as Ryan S. McMahan, Timothy P. Birkland, Kate S. Smigiel, of September 26, 2021. Tyler C. Vandivort, Maryam G. Rohani, Anne M. Manicone, John K. McGuire, Sina A. Gharib and William C. Parks J Immunol 2016; 197:899-909; Prepublished online 17 June 2016; doi: 10.4049/jimmunol.1600502 Downloaded from http://www.jimmunol.org/content/197/3/899 Supplementary http://www.jimmunol.org/content/suppl/2016/06/16/jimmunol.160050 Material 2.DCSupplemental http://www.jimmunol.org/ References This article cites 72 articles, 15 of which you can access for free at: http://www.jimmunol.org/content/197/3/899.full#ref-list-1 Why The JI? Submit online. • Rapid Reviews! 30 days* from submission to initial decision by guest on September 26, 2021 • No Triage! Every submission reviewed by practicing scientists • Fast Publication! 4 weeks from acceptance to publication *average Subscription Information about subscribing to The Journal of Immunology is online at: http://jimmunol.org/subscription Permissions Submit copyright permission requests at: http://www.aai.org/About/Publications/JI/copyright.html Email Alerts Receive free email-alerts when new articles cite this article. Sign up at: http://jimmunol.org/alerts The Journal of Immunology is published twice each month by The American Association of Immunologists, Inc., 1451 Rockville Pike, Suite 650, Rockville, MD 20852 Copyright © 2016 by The American Association of Immunologists, Inc. All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. The Journal of Immunology Stromelysin-2 (MMP10) Moderates Inflammation by Controlling Macrophage Activation Ryan S. -
Peptides and Peptidomimetics As Inhibitors of Enzymes Involved in Fibrillar Collagen Degradation
materials Review Peptides and Peptidomimetics as Inhibitors of Enzymes Involved in Fibrillar Collagen Degradation Patrycja Ledwo ´n 1,2 , Anna Maria Papini 3 , Paolo Rovero 2,* and Rafal Latajka 1,* 1 Department of Bioorganic Chemistry, Faculty of Chemistry, Wroclaw University of Science and Technology, 50-370 Wroclaw, Poland; [email protected] 2 Interdepartmental Research Unit of Peptide and Protein Chemistry and Biology, Department of Neurosciences, Psychology, Drug Research and Child Health-Section of Pharmaceutical Sciences and Nutraceutics, University of Florence, 50019 Sesto Fiorentino, Firenze, Italy 3 Interdepartmental Research Unit of Peptide and Protein Chemistry and Biology, Department of Chemistry “Ugo Schiff”, University of Florence, 50019 Sesto Fiorentino, Firenze, Italy; annamaria.papini@unifi.it * Correspondence: paolo.rovero@unifi.it (P.R.); [email protected] (R.L.) Abstract: Collagen fibres degradation is a complex process involving a variety of enzymes. Fibrillar collagens, namely type I, II, and III, are the most widely spread collagens in human body, e.g., they are responsible for tissue fibrillar structure and skin elasticity. Nevertheless, the hyperactivity of fibrotic process and collagen accumulation results with joints, bone, heart, lungs, kidneys or liver fibroses. Per contra, dysfunctional collagen turnover and its increased degradation leads to wound healing disruption, skin photoaging, and loss of firmness and elasticity. In this review we described the main enzymes participating in collagen degradation pathway, paying particular attention to enzymes degrading fibrillar collagen. Therefore, collagenases (MMP-1, -8, and -13), elastases, and cathepsins, together with their peptide and peptidomimetic inhibitors, are reviewed. This information, related Citation: Ledwo´n,P.; Papini, A.M.; to the design and synthesis of new inhibitors based on peptide structure, can be relevant for future Rovero, P.; Latajka, R. -
Parallel Expression of Macrophage Metalloelastase (MMP-12) in Duodenal and Skin Lesions of Gut: First Published As 10.1136/Gut.48.4.496 on 1 April 2001
496 Gut 2001;48:496–502 Parallel expression of macrophage metalloelastase (MMP-12) in duodenal and skin lesions of Gut: first published as 10.1136/gut.48.4.496 on 1 April 2001. Downloaded from patients with dermatitis herpetiformis M T Salmela, SLFPender, T Reunala, T MacDonald, U Saarialho-Kere Abstract intraepithelial lymphocytes.2 The rash and Background—Dermatitis herpetiformis enteropathy improve on a gluten free diet, (DH) is a specific dermatological manifes- implying that DH is a specific skin manifesta- tation of coeliac disease and 80% of DH tion of mainly subclinical coeliac disease patients have gluten sensitive enteropathy (CD).23 manifested by crypt hyperplasia and vil- Matrix metalloproteinases (MMPs) are a lous atrophy. Matrix degradation mediated family of extracellular matrix (ECM) degrad- by collagenase 1 (MMP-1) and stromelysin ing enzymes that are collectively capable of 1 (MMP-3) has previously been implicated degrading essentially all ECM components in the pathobiology of coeliac intestine and and that can further be subdivided into cutaneous DH blisters. collagenases (MMP-1, -8, and -13), gelatinases Aims—To study expression of stromelysin (MMP-2 and -9), stromelysins (MMP-3, -7, 2, metalloelastase, collagenase 3, and mat- -10, and –12), membrane-type MMPs, and rilysin in the intestine and skin of DH other MMPs.45 The extracellular activity of patients. MMPs is regulated by TIMPs 1–4.6 We have Methods—In situ hybridisation using 35S previously reported that expression of MMP-1 labelled cRNA probes was performed on and -3 is enhanced in basal keratinocytes 7 duodenal biopsies of 15 DH patients, three surrounding neutrophil abscesses in DH skin. -
Handbook of Proteolytic Enzymes Second Edition Volume 1 Aspartic and Metallo Peptidases
Handbook of Proteolytic Enzymes Second Edition Volume 1 Aspartic and Metallo Peptidases Alan J. Barrett Neil D. Rawlings J. Fred Woessner Editor biographies xxi Contributors xxiii Preface xxxi Introduction ' Abbreviations xxxvii ASPARTIC PEPTIDASES Introduction 1 Aspartic peptidases and their clans 3 2 Catalytic pathway of aspartic peptidases 12 Clan AA Family Al 3 Pepsin A 19 4 Pepsin B 28 5 Chymosin 29 6 Cathepsin E 33 7 Gastricsin 38 8 Cathepsin D 43 9 Napsin A 52 10 Renin 54 11 Mouse submandibular renin 62 12 Memapsin 1 64 13 Memapsin 2 66 14 Plasmepsins 70 15 Plasmepsin II 73 16 Tick heme-binding aspartic proteinase 76 17 Phytepsin 77 18 Nepenthesin 85 19 Saccharopepsin 87 20 Neurosporapepsin 90 21 Acrocylindropepsin 9 1 22 Aspergillopepsin I 92 23 Penicillopepsin 99 24 Endothiapepsin 104 25 Rhizopuspepsin 108 26 Mucorpepsin 11 1 27 Polyporopepsin 113 28 Candidapepsin 115 29 Candiparapsin 120 30 Canditropsin 123 31 Syncephapepsin 125 32 Barrierpepsin 126 33 Yapsin 1 128 34 Yapsin 2 132 35 Yapsin A 133 36 Pregnancy-associated glycoproteins 135 37 Pepsin F 137 38 Rhodotorulapepsin 139 39 Cladosporopepsin 140 40 Pycnoporopepsin 141 Family A2 and others 41 Human immunodeficiency virus 1 retropepsin 144 42 Human immunodeficiency virus 2 retropepsin 154 43 Simian immunodeficiency virus retropepsin 158 44 Equine infectious anemia virus retropepsin 160 45 Rous sarcoma virus retropepsin and avian myeloblastosis virus retropepsin 163 46 Human T-cell leukemia virus type I (HTLV-I) retropepsin 166 47 Bovine leukemia virus retropepsin 169 48 -
Cov-2 Infection in the Small Intestine
Gastroenterology and Hepatology From Bed to Bench. ORIGINAL ARTICLE ©2020 RIGLD, Research Institute for Gastroenterology and Liver Diseases Investigating the human protein-host protein interactome of SARS- CoV-2 infection in the small intestine Mahmoud Khodadoost1, Zahra Niknam2, Masoumeh Farahani2, Mohammadreza Razzaghi3, Mohsen Norouzinia4 1Department of Traditional Medicine, School of Traditional Medicine, Shahid Beheshti University of Medical Sciences, Tehran, Iran 2Proteomics Research Center, Shahid Beheshti University of Medical Sciences, Tehran, Iran 3Laser Application in Medical Sciences Research Center, Shahid Beheshti University of Medical Sciences, Tehran, Iran 4 Gastroenterology and Liver Diseases Research Center, Research Institute for Gastroenterology and Liver Diseases, Shahid Beheshti University of Medical Sciences, Tehran, Iran ABSTRACT Aim: The present study aimed to identify human protein–host protein interactions of SARS-CoV-2 infection in the small intestine to discern the potential mechanisms and gain insights into the associated biomarkers and treatment strategies. Background: Deciphering the tissue and organ interactions of the SARS-CoV-2 infection can be important to discern the potential underlying mechanisms. In the present study, we investigated the human protein–host protein interactions in the small intestine. Methods: Public databases and published works were used to collect data related to small intestine tissue and SARS-CoV-2 infection. We constructed a human protein-protein interaction (PPI) network and showed interactions of host proteins in the small intestine. Associated modules, biological processes, functional pathways, regulatory transcription factors, disease ontology categories, and possible drug candidates for therapeutic targets were identified. Results: Thirteen primary protein neighbors were found for the SARS-CoV-2 receptor ACE2. ACE2 and its four partners were observed in a highly clustered module; moreover, 8 host proteins belonged to this module. -
Discovery and Optimization of Selective Inhibitors of Meprin Α (Part I)
Preprints (www.preprints.org) | NOT PEER-REVIEWED | Posted: 14 December 2020 doi:10.20944/preprints202012.0354.v1 Discovery and Optimization of Selective Inhibitors of Meprin α (Part I) Shurong Hou1,3 Juan Diez2, Chao Wang3, Christoph Becker-Pauly4, Gregg B. Fields5, Thomas Bannister3, Timothy P. Spicer1,3 Louis D. Scampavia1,3 and Dmitriy Minond2,6 1 - The Scripps Research Molecular Screening Center, Department of Molecular Medicine, Scripps Research, Jupiter, Florida 33458 2 - Rumbaugh-Goodwin Institute for Cancer Research, Nova Southeastern University, 3321 College Avenue, CCR r.605, Fort Lauderdale, FL 33314 3 - Department of Molecular Medicine, Scripps Research, Jupiter, Florida 33458 4 - University of Kiel, Institute of Biochemistry, Unit for Degradomics of the Protease Web, Rudolf-Höber-Str.1, 24118 Kiel, Germany 5 - Department of Chemistry & Biochemistry and I-HEALTH, Florida Atlantic University, 5353 Parkside Drive, Jupiter, FL 33458 6 - Dr. Kiran C. Patel College of Allopathic Medicine, Nova Southeastern University, 3301 College Avenue, Fort Lauderdale, FL 33314 *Correspondence to: Dmitriy Minond, Rumbaugh-Goodwin Institute for Cancer Research, Nova Southeastern University, 3321 College Avenue, CCR r.605, Fort Lauderdale, FL 33314, [email protected]; Short title: Selective inhibitors of meprin α Subject category: Enzymatic assays KEYWORDS: meprin α, meprin β, zinc metalloproteinase, uHTS. 1 © 2020 by the author(s). Distributed under a Creative Commons CC BY license. Preprints (www.preprints.org) | NOT PEER-REVIEWED | Posted: 14 December 2020 doi:10.20944/preprints202012.0354.v1 ABSTRACT Meprin α and β are zinc-dependent proteinases implicated in multiple diseases including cancers, fibrosis, and Alzheimer’s. However, until recently, only a few inhibitors of either meprin were reported and no inhibitors are in pre-clinical development.