ADAMTS13 and 15 Are Not Regulated by the Full Length and N‑Terminal Domain Forms of TIMP‑1, ‑2, ‑3 and ‑4
Total Page:16
File Type:pdf, Size:1020Kb
Load more
Recommended publications
-
What Are the Roles of Metalloproteinases in Cartilage and Bone Damage? G Murphy, M H Lee
iv44 Ann Rheum Dis: first published as 10.1136/ard.2005.042465 on 20 October 2005. Downloaded from REPORT What are the roles of metalloproteinases in cartilage and bone damage? G Murphy, M H Lee ............................................................................................................................... Ann Rheum Dis 2005;64:iv44–iv47. doi: 10.1136/ard.2005.042465 enzyme moiety into an upper and a lower subdomain. A A role for metalloproteinases in the pathological destruction common five stranded beta-sheet and two alpha-helices are in diseases such as rheumatoid arthritis and osteoarthritis, always found in the upper subdomain with a further C- and the irreversible nature of the ensuing cartilage and bone terminal helix in the lower subdomain. The catalytic sites of damage, have been the focus of much investigation for the metalloproteinases, especially the MMPs, have been several decades. This has led to the development of broad targeted for the development of low molecular weight spectrum metalloproteinase inhibitors as potential therapeu- synthetic inhibitors with a zinc chelating moiety. Inhibitors tics. More recently it has been appreciated that several able to fully differentiate between individual enzymes have families of zinc dependent proteinases play significant and not been identified thus far, although a reasonable level of varied roles in the biology of the resident cells in these tissues, discrimination is now being achieved in some cases.7 Each orchestrating development, remodelling, and subsequent family does, however, have other unique domains with pathological processes. They also play key roles in the numerous roles, including the determination of physiological activity of inflammatory cells. The task of elucidating the substrate specificity, ECM, or cell surface localisation (fig 1). -
And MMP-Mediated Cell–Matrix Interactions in the Tumor Microenvironment
International Journal of Molecular Sciences Review Hold on or Cut? Integrin- and MMP-Mediated Cell–Matrix Interactions in the Tumor Microenvironment Stephan Niland and Johannes A. Eble * Institute of Physiological Chemistry and Pathobiochemistry, University of Münster, 48149 Münster, Germany; [email protected] * Correspondence: [email protected] Abstract: The tumor microenvironment (TME) has become the focus of interest in cancer research and treatment. It includes the extracellular matrix (ECM) and ECM-modifying enzymes that are secreted by cancer and neighboring cells. The ECM serves both to anchor the tumor cells embedded in it and as a means of communication between the various cellular and non-cellular components of the TME. The cells of the TME modify their surrounding cancer-characteristic ECM. This in turn provides feedback to them via cellular receptors, thereby regulating, together with cytokines and exosomes, differentiation processes as well as tumor progression and spread. Matrix remodeling is accomplished by altering the repertoire of ECM components and by biophysical changes in stiffness and tension caused by ECM-crosslinking and ECM-degrading enzymes, in particular matrix metalloproteinases (MMPs). These can degrade ECM barriers or, by partial proteolysis, release soluble ECM fragments called matrikines, which influence cells inside and outside the TME. This review examines the changes in the ECM of the TME and the interaction between cells and the ECM, with a particular focus on MMPs. Keywords: tumor microenvironment; extracellular matrix; integrins; matrix metalloproteinases; matrikines Citation: Niland, S.; Eble, J.A. Hold on or Cut? Integrin- and MMP-Mediated Cell–Matrix 1. Introduction Interactions in the Tumor Microenvironment. -
Human ADAM12 Quantikine ELISA
Quantikine® ELISA Human ADAM12 Immunoassay Catalog Number DAD120 For the quantitative determination of A Disintegrin And Metalloproteinase domain- containing protein 12 (ADAM12) concentrations in cell culture supernates, serum, plasma, and urine. This package insert must be read in its entirety before using this product. For research use only. Not for use in diagnostic procedures. TABLE OF CONTENTS SECTION PAGE INTRODUCTION .....................................................................................................................................................................1 PRINCIPLE OF THE ASSAY ...................................................................................................................................................2 LIMITATIONS OF THE PROCEDURE .................................................................................................................................2 TECHNICAL HINTS .................................................................................................................................................................2 MATERIALS PROVIDED & STORAGE CONDITIONS ...................................................................................................3 OTHER SUPPLIES REQUIRED .............................................................................................................................................3 PRECAUTIONS .........................................................................................................................................................................4 -
Quantikine® ELISA
Quantikine® ELISA Human ADAMTS13 Immunoassay Catalog Number DADT130 For the quantitative determination of human A Disintegrin And Metalloproteinase with Thombospondin type 1 motif, 13 (ADAMTS13) concentrations in cell culture supernates, serum, and plasma. This package insert must be read in its entirety before using this product. For research use only. Not for use in diagnostic procedures. TABLE OF CONTENTS SECTION PAGE INTRODUCTION .....................................................................................................................................................................1 PRINCIPLE OF THE ASSAY ...................................................................................................................................................2 LIMITATIONS OF THE PROCEDURE .................................................................................................................................2 TECHNICAL HINTS .................................................................................................................................................................2 MATERIALS PROVIDED & STORAGE CONDITIONS ...................................................................................................3 OTHER SUPPLIES REQUIRED .............................................................................................................................................4 PRECAUTIONS .........................................................................................................................................................................4 -
Crystal Structures of the Noncatalytic Domains of ADAMTS13 Reveal Multiple Discontinuous Exosites for Von Willebrand Factor
Crystal structures of the noncatalytic domains of ADAMTS13 reveal multiple discontinuous exosites for von Willebrand factor Masashi Akiyamaa,1, Soichi Takedaa,1,2, Koichi Kokamea, Junichi Takagib, and Toshiyuki Miyataa,2 aNational Cardiovascular Center Research Institute, Suita, Osaka 565-8565, Japan; and bLaboratory of Protein Synthesis and Expression, Institute for Protein Research, Osaka University, Suita, Osaka 565-0871, Japan Edited by Philip W. Majerus, Washington University Medical School, St. Louis, MO, and approved September 16, 2009 (received for review August 27, 2009) ADAMTS13 specifically cleaves plasma von Willebrand factor (VWF) distribution of VWF multimers is important for normal hemo- and thereby controls VWF-mediated platelet thrombus formation. stasis, as large multimers are hemostatically more active than Severe deficiencies in ADAMTS13 can cause life-threatening throm- small multimers (3). Deficiencies in ADAMTS13 activity, caused botic thrombocytopenic purpura. Here, we determined 2 crystal either by genetic mutations in the ADAMTS13 gene or by structures of ADAMTS13-DTCS (residues 287–685), an exosite- acquired inhibitory autoantibodies directed against the AD- containing human ADAMTS13 fragment, at 2.6-Å and 2.8-Å reso- AMTS13 protein, results in the accumulation of UL-VWF in the lution. The structures revealed folding similarities between the plasma (8–11). The UL-VWF accumulation leads to the forma- disintegrin-like (D) domain and the N-terminal portion of the tion of disseminated platelet-rich microthrombi in the micro- cysteine-rich domain (designated the CA domain). The spacer (S) vasculature, which results in the life-threatening disease, throm- domain forms a globular functional unit with a 10-stranded botic thrombocytopenic purpura (TTP). -
Inhibition of Tumor Growth by Antibody to ADAMTS1 in Mouse Xenografts of Breast Cancer
ANTICANCER RESEARCH 31: 3839-3842 (2011) Inhibition of Tumor Growth by Antibody to ADAMTS1 in Mouse Xenografts of Breast Cancer TOMOHIRO HIRANO1, KUNITAKA HIROSE2, KENICHI SAKURAI1, MAKOTO MAKISHIMA3, KENJI SASAKI4† and SADAO AMANO1 1Division of Breast and Endocrine Surgery, Department of Surgery, 3Division of Biochemistry, Department of Biomedical Sciences and 4Division of Plastic and Reconstructive Surgery, Department of Plastic and Reconstructive Surgery, Nihon University School of Medicine, Itabashi-ku, Tokyo, Japan; 2Biomedical Research Laboratory, Kureha Chemical Industry Co., Ltd., Shinjuku-ku, Tokyo, Japan Abstract. Background: A disintegrin and metalloproteinase carcinoma and Lewis lung carcinoma cells (4). ADAMTS1 and with thrombospondin motifs-1 (ADAMTS1), a member of the matrix metalloproteinase-1 synergistically promote bone ADAMTS family of proteases, is involved in the shedding of metastasis of breast cancer cells by shedding epidermal growth epidermal growth factor (EGF)-like ligands such as factor (EGF)-like ligands, including heparin-binding EGF (HB- amphiregulin, which activate the EGF receptor. Since EGF), amphiregulin, and transforming growth factor α, from ADAMTS1 has been implicated in aggressive breast tumor cells, and subsequent activation of the EGF receptor carcinogenesis, we examined potential antitumor effects of (EGFR) (5). In human breast samples, ADAMTS1 mRNA is antibody to ADAMTS1 in a mouse model of breast cancer. expressed in non-neoplastic mammary tissues, predominantly in Materials and Methods: BALB/c female mice were inoculated stromal fibroblasts, and is significantly down-regulated in breast with syngenic 4T1 breast cancer cells and treated with anti- carcinomas (6). The erythroblastic leukemia viral oncogene ADAMTS1 antibody or control IgG. Tumor volume and weight homolog (ERBB) family of receptor tyrosine kinases, were evaluated. -
Association of ADAM12 Gene Polymorphisms with Knee Osteoarthritis Susceptibility
www.impactjournals.com/oncotarget/ Oncotarget, Supplementary Materials 2017 Association of ADAM12 gene polymorphisms with knee osteoarthritis susceptibility SUPPLEMENTARY MATERIALS REFERENCES candidate genes for the prevalence and progression of knee osteoarthritis. Arthritis Rheum. 2004;50:2497-2507. 1. Poonpet T, Tammachote R, Tammachote N, Kanitnate S, 11. Kerna I, Kisand K, Laitinen P, Tamm A, Tamm A. Honsawek S. Association between ADAM12 polymorphism Association of metallopeptidase domain 12 (ADAM12) and knee osteoarthritis in Thai population. Knee. gene polymorphisms and ADAM12 protein with the 2016;23:357-361. development of knee osteoarthritis. Osteoarthritis Cartilage. 2. Wang L, Guo L, Tian F, Hao R, Yang T. Analysis of single 2010;18. nucleotide polymorphisms within ADAM12 and risk of 12. Stark K, Straub RH, Blažičková S, Hengstenberg C, knee osteoarthritis in a Chinese Han population. Biomed Rovenský J. Genetics in neuroendocrine immunology: Res Int. 2015;2015:518643. implications for rheumatoid arthritis and osteoarthritis. Ann 3. Lou S, Zhao Z, Qian J, Zhao K, Wang R. Association N Y Acad Sci. 2010;1193. of single nucleotide polymorphisms in ADAM12 gene 13. Limer KL, Tosh K, Bujac SR, McConnell R, Doherty S, with susceptibility to kneeosteoarthritis: a case-control Nyberg F, Zhang W, Doherty M, Muir KR, Maciewicz study in a Chinese Han population. Int J Clin Exp Pathol. RA. Attempt to replicate published genetic associations 2014;7:5154-5159. in a large, well-defined osteoarthritis case-control 4. Kerna I, Kisand K, Tamm AE, Kumm J, Tamm AO. population (the GOAL study). Osteoarthritis Cartilage. Two single-nucleotide polymorphisms in ADAM12 2009;17:782-789. gene are associated with early and late radiographic 14. -
Comparative Transcriptome Analysis of Embryo Invasion in the Mink Uterus
Placenta 75 (2019) 16–22 Contents lists available at ScienceDirect Placenta journal homepage: www.elsevier.com/locate/placenta Comparative transcriptome analysis of embryo invasion in the mink uterus T ∗ Xinyan Caoa,b, , Chao Xua,b, Yufei Zhanga,b, Haijun Weia,b, Yong Liuc, Junguo Caoa,b, Weigang Zhaoa,b, Kun Baoa,b, Qiong Wua,b a Institute of Special Animal and Plant Sciences, Chinese Academy of Agricultural Sciences, Changchun, China b State Key Laboratory for Molecular Biology of Special Economic Animal and Plant Science, Chinese Academy of Agricultural Sciences, Changchun, China c Key Laboratory of Embryo Development and Reproductive Regulation of Anhui Province, College of Biological and Food Engineering, Fuyang Teachers College, Fuyang, China ABSTRACT Introduction: In mink, as many as 65% of embryos die during gestation. The causes and the mechanisms of embryonic mortality remain unclear. The purpose of our study was to examine global gene expression changes during embryo invasion in mink, and thereby to identify potential signaling pathways involved in implantation failure and early pregnancy loss. Methods: Illumina's next-generation sequencing technology (RNA-Seq) was used to analyze the differentially expressed genes (DEGs) in implantation (IMs) and inter- implantation sites (inter-IMs) of uterine tissue. Results: We identified a total of 606 DEGs, including 420 up- and 186 down-regulated genes in IMs compared to inter-IMs. Gene annotation analysis indicated multiple biological pathways to be significantly enriched for DEGs, including immune response, ECM complex, cytokine activity, chemokine activity andprotein binding. The KEGG pathway including cytokine-cytokine receptor interaction, Jak-STAT, TNF and the chemokine signaling pathway were the most enriched. -
ADAMTS Proteases in Vascular Biology
Review MATBIO-1141; No. of pages: 8; 4C: 3, 6 ADAMTS proteases in vascular biology Juan Carlos Rodríguez-Manzaneque 1, Rubén Fernández-Rodríguez 1, Francisco Javier Rodríguez-Baena 1 and M. Luisa Iruela-Arispe 2 1 - GENYO, Centre for Genomics and Oncological Research, Pfizer, Universidad de Granada, Junta de Andalucía, 18016 Granada, Spain 2 - Department of Molecular, Cell, and Developmental Biology, Molecular Biology Institute, University of California, Los Angeles, Los Angeles, CA 90095, USA Correspondence to Juan Carlos Rodríguez-Manzaneque and M. Luisa Iruela-Arispe: J.C Rodríguez-Manzaneque is to be contacted at: GENYO, 15 PTS Granada - Avda. de la Ilustración 114, Granada 18016, Spain; M.L. Iruela-Arispe, Department of Molecular, Cell and Developmental Biology, UCLA, 615 Charles Young Drive East, Los Angeles, CA 90095, USA. [email protected]; [email protected] http://dx.doi.org/10.1016/j.matbio.2015.02.004 Edited by W.C. Parks and S. Apte Abstract ADAMTS (a disintegrin and metalloprotease with thrombospondin motifs) proteases comprise the most recently discovered branch of the extracellular metalloenzymes. Research during the last 15 years, uncovered their association with a variety of physiological and pathological processes including blood coagulation, tissue repair, fertility, arthritis and cancer. Importantly, a frequent feature of ADAMTS enzymes relates to their effects on vascular-related phenomena, including angiogenesis. Their specific roles in vascular biology have been clarified by information on their expression profiles and substrate specificity. Through their catalytic activity, ADAMTS proteases modify rather than degrade extracellular proteins. They predominantly target proteoglycans and glycoproteins abundant in the basement membrane, therefore their broad contributions to the vasculature should not come as a surprise. -
Pancancer Progression Human Vjune2017
Gene Symbol Accession Alias/Prev Symbol Official Full Name AAMP NM_001087.3 - angio-associated, migratory cell protein ABI3BP NM_015429.3 NESHBP|TARSH ABI family, member 3 (NESH) binding protein ACHE NM_000665.3 ACEE|ARACHE|N-ACHE|YT acetylcholinesterase ACTG2 NM_001615.3 ACT|ACTA3|ACTE|ACTL3|ACTSG actin, gamma 2, smooth muscle, enteric ACVR1 NM_001105.2 ACTRI|ACVR1A|ACVRLK2|ALK2|FOP|SKR1|TSRI activin A receptor, type I ACVR1C NM_145259.2 ACVRLK7|ALK7 activin A receptor, type IC ACVRL1 NM_000020.1 ACVRLK1|ALK-1|ALK1|HHT|HHT2|ORW2|SKR3|TSR-I activin A receptor type II-like 1 ADAM15 NM_207195.1 MDC15 ADAM metallopeptidase domain 15 ADAM17 NM_003183.4 ADAM18|CD156B|CSVP|NISBD|TACE ADAM metallopeptidase domain 17 ADAM28 NM_014265.4 ADAM 28|ADAM23|MDC-L|MDC-Lm|MDC-Ls|MDCL|eMDC II|eMDCII ADAM metallopeptidase domain 28 ADAM8 NM_001109.4 CD156|MS2 ADAM metallopeptidase domain 8 ADAM9 NM_001005845.1 CORD9|MCMP|MDC9|Mltng ADAM metallopeptidase domain 9 ADAMTS1 NM_006988.3 C3-C5|METH1 ADAM metallopeptidase with thrombospondin type 1 motif, 1 ADAMTS12 NM_030955.2 PRO4389 ADAM metallopeptidase with thrombospondin type 1 motif, 12 ADAMTS8 NM_007037.4 ADAM-TS8|METH2 ADAM metallopeptidase with thrombospondin type 1 motif, 8 ADAP1 NM_006869.2 CENTA1|GCS1L|p42IP4 ArfGAP with dual PH domains 1 ADD1 NM_001119.4 ADDA adducin 1 (alpha) ADM2 NM_001253845.1 AM2|dJ579N16.4 adrenomedullin 2 ADRA2B NM_000682.4 ADRA2L1|ADRA2RL1|ADRARL1|ALPHA2BAR|alpha-2BAR adrenoceptor alpha 2B AEBP1 NM_001129.3 ACLP AE binding protein 1 AGGF1 NM_018046.3 GPATC7|GPATCH7|HSU84971|HUS84971|VG5Q -
Effect of Inhibition of Matrix Metalloproteinases on Endometrial Decidualization and Implantation in Mated Rats M
Effect of inhibition of matrix metalloproteinases on endometrial decidualization and implantation in mated rats M. P. Rechtman, J. Zhang and L. A. Salamonsen Prince Henry's Institute ofMedical Research, PO Box 5152, Clayton, Victoria 3168, Australia Implantation of the embryo into the endometrium is a highly regulated event that is critical for establishment of pregnancy. Molecules involved in this process provide potential targets for post-coital contraception. The aims of this study were to determine whether matrix metalloproteinases (MMPs) are present at implantation sites in rats and whether administration of a broad-based inhibitor of MMPs could inhibit embryo implantation. Uterine extracts from non-pregnant rats and from rats on days 3\p=n-\9 of pregnancy were examined for the presence of MMPs. Doxycycline (5 or 15 mg day\m=-\1) was administered by gavage to rats from the day of mating (day 0) to day 7 of pregnancy and the uterus was examined for implantation sites. A number of MMPs were present in all uterine samples. MMP-2 reached a peak on day 3, whereas the highest expression of MMP-7 occurred on day 7. MMP-13 and MMP-3 were present in smaller amounts. MMP-9 was detectable only on day 9. Treatment of rats with doxycycline had no effect on the number of implantation sites or on the total uterine mass. However, in treated rats, the process of decidualization was impaired and both the width and length of the decidual zone was reduced, resulting in a decrease in total decidual area from 1.20 \m=+-\0.07 to 0.91 \m=+-\0.07 mm2 (mean \m=+-\sem, controls versus doxycycline treated, P < 0.02). -
P.D187H Mutation Impairs ADAMTS13 Activity and Secretion and Contributes to Thrombotic Thrombocytopenic Purpura in Mice
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Lirias Journal of Thrombosis and Haemostasis, 13: 283–292 DOI: 10.1111/jth.12804 ORIGINAL ARTICLE The novel ADAMTS13-p.D187H mutation impairs ADAMTS13 activity and secretion and contributes to thrombotic thrombocytopenic purpura in mice E. DE COCK,* C. HERMANS,† J. DE RAEYMAECKER,‡ K. DE CEUNYNCK,* B. DE MAEYER,* N. VANDEPUTTE,* A. VANDENBULCKE,* H. DECKMYN,* H. ROTTENSTEINER,§ M. DE MAEYER,‡ S. F. DE MEYER* andK. VANHOORELBEKE* *Laboratory for Thrombosis Research, KU Leuven Kulak, Kortrijk; †Division of Haematology, Haemostasis and Thrombosis Unit, Saint-Luc University Hospital, Brussels; ‡Biochemistry, Molecular and Structural Biology Section, Department of Chemistry, Laboratory of Biomolecular Modeling, KU Leuven, Leuven, Belgium; and §Baxter Innovations GmbH, Vienna, Austria To cite this article: De Cock E, Hermans C, De Raeymaecker J, De Ceunynck K, De Maeyer B, Vandeputte N, Vandenbulcke A, Deckmyn H, Rottensteiner H, De Maeyer M, De Meyer SF, Vanhoorelbeke K. The novel ADAMTS13-p.D187H mutation impairs ADAMTS13 activity and secretion and contributes to thrombotic thrombocytopenic purpura in mice. J Thromb Haemost 2015; 13: 283–92. of ADAMTS13. The homozygous p.D187H mutation Summary. Background: Congenital thrombotic thrombo- down-regulated ADAMTS13 activity in vitro. Impaired cytopenic purpura (TTP) is characterized by mutations in proteolytic activity was linked to unstable Ca2+ binding the ADAMTS13 gene, which either impair protein secre- as visualized using a molecular dynamics simulation. In tion or influence ADAMTS13 (A Disintegrin-like And addition, the p.D187H mutation affects protein secretion Metalloprotease domain with ThromboSpondin type-1 in vitro.InAdamts13–/– mice, the homozygous p.D187H motif, member 13) activity.