Gelatinase-A (MMP-2), Gelatinase-B (MMP-9) and Membrane Type Matrix
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MATRIX METALLOPROTEINASE REQUIREMENTS for NEUROMUSCULAR SYNAPTOGENESIS by Mary Lynn Dear Dissertation Submitted to the Faculty O
MATRIX METALLOPROTEINASE REQUIREMENTS FOR NEUROMUSCULAR SYNAPTOGENESIS By Mary Lynn Dear Dissertation Submitted to the Faculty of the Graduate School of Vanderbilt University in partial fulfillment of the requirements for the degree of DOCTOR OF PHILOSOPHY in Biological Sciences January 31, 2018 Nashville, Tennessee Approved: Todd Graham, Ph.D. Kendal Broadie, Ph.D. Katherine Friedman, Ph.D. Barbara Fingleton, Ph.D. Jared Nordman, Ph.D. Copyright © 2018 by Mary Lynn Dear All Rights Reserved ACKNOWLEDGEMENTS I would like to acknowledge my advisor, Kendal Broadie, and the entire Broadie laboratory, both past and present, for their endless support, engaging conversations, thoughtful suggestions and constant encouragement. I would also like to thank my committee members both past and present for playing such a pivotal role in my graduate career and growth as a scientist. I thank the Department of Biological Sciences for fostering my graduate education. I thank the entire protease community for their continued support, helpful suggestions and collaborative efforts that helped my project move forward. I would like to acknowledge Dr. Andrea Page-McCaw and her entire laboratory for helpful suggestions, being engaged in my studies and providing many tools that were invaluable to my project. I thank my parents, Leisa Justus and Raymond Dear, my brother Jake Dear and my best friend Jenna Kaufman. Words cannot describe how grateful I am for your support and encouragement. Most importantly, I would like to thank my husband, Jeffrey Thomas, for always believing in me, your unwavering support and for helping me endure all the ups and downs that come with graduate school. -
Proteases, Mucus, and Mucosal Immunity in Chronic Lung Disease
International Journal of Molecular Sciences Review Proteases, Mucus, and Mucosal Immunity in Chronic Lung Disease Michael C. McKelvey 1 , Ryan Brown 1, Sinéad Ryan 1, Marcus A. Mall 2,3,4 , Sinéad Weldon 1 and Clifford C. Taggart 1,* 1 Airway Innate Immunity Research (AiiR) Group, Wellcome-Wolfson Institute for Experimental Medicine, Queen’s University Belfast, Belfast BT9 7BL, UK; [email protected] (M.C.M.); [email protected] (R.B.); [email protected] (S.R.); [email protected] (S.W.) 2 Department of Pediatric Respiratory Medicine, Immunology and Critical Care Medicine, Charité—Universitätsmedizin Berlin, 13353 Berlin, Germany; [email protected] 3 Berlin Institute of Health (BIH), 10178 Berlin, Germany 4 German Center for Lung Research (DZL), 35392 Gießen, Germany * Correspondence: [email protected]; Tel.: +44-289097-6383 Abstract: Dysregulated protease activity has long been implicated in the pathogenesis of chronic lung diseases and especially in conditions that display mucus obstruction, such as chronic obstructive pulmonary disease, cystic fibrosis, and non-cystic fibrosis bronchiectasis. However, our appreciation of the roles of proteases in various aspects of such diseases continues to grow. Patients with muco- obstructive lung disease experience progressive spirals of inflammation, mucostasis, airway infection and lung function decline. Some therapies exist for the treatment of these symptoms, but they are unable to halt disease progression and patients may benefit from novel adjunct therapies. In this review, we highlight how proteases act as multifunctional enzymes that are vital for normal Citation: McKelvey, M.C.; Brown, R.; airway homeostasis but, when their activity becomes immoderate, also directly contribute to airway Ryan, S.; Mall, M.A.; Weldon, S.; dysfunction, and impair the processes that could resolve disease. -
Metalloproteinase-9 and Chemotaxis Inflammatory Cell Production of Matrix AQARSAASKVKVSMKF, Induces 5, Α a Site on Laminin
A Site on Laminin α5, AQARSAASKVKVSMKF, Induces Inflammatory Cell Production of Matrix Metalloproteinase-9 and Chemotaxis This information is current as of September 25, 2021. Tracy L. Adair-Kirk, Jeffrey J. Atkinson, Thomas J. Broekelmann, Masayuki Doi, Karl Tryggvason, Jeffrey H. Miner, Robert P. Mecham and Robert M. Senior J Immunol 2003; 171:398-406; ; doi: 10.4049/jimmunol.171.1.398 Downloaded from http://www.jimmunol.org/content/171/1/398 References This article cites 64 articles, 24 of which you can access for free at: http://www.jimmunol.org/ http://www.jimmunol.org/content/171/1/398.full#ref-list-1 Why The JI? Submit online. • Rapid Reviews! 30 days* from submission to initial decision • No Triage! Every submission reviewed by practicing scientists by guest on September 25, 2021 • 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 © 2003 by The American Association of Immunologists All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. The Journal of Immunology A Site on Laminin ␣5, AQARSAASKVKVSMKF, Induces Inflammatory Cell Production of Matrix Metalloproteinase-9 and Chemotaxis1 Tracy L. Adair-Kirk,* Jeffrey J. Atkinson,* Thomas J. -
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). -
High Serum Levels of Matrix Metalloproteinase-9 and Matrix
Imaging, Diagnosis, Prognosis High Serum Levels of Matrix Metalloproteinase-9 and Matrix Metalloproteinase-1Are Associated with Rapid Progression in Patients with Metastatic Melanoma Johanna Nikkola,1, 3 PiaVihinen,1, 3 Meri-SiskoVuoristo,4 Pirkko Kellokumpu-Lehtinen,4 Veli-Matti Ka« ha« ri,2 and Seppo Pyrho« nen1, 3 Abstract Purpose: Matrixmetalloproteinases (MMP) are proteolytic enzymes that play an important role in various aspects of cancer progression. In the present work, we have studied the prognostic significance of serum levels of gelatinase B (MMP-9), collagenase-1 (MMP-1), and collagenase- 3 (MMP-13) in patients with advanced melanoma. Experimental Design:Total pretreatment serum levels of MMP-9 in 71patients and MMP-1and MMP-13 in 48 patients were determined by an assay system based on ELISA. Total MMP levels were also assessed in eight healthy controls. The active and latent forms of MMPs were defined by usingWestern blot analysis and gelatin zymography. Results: Patients with high serum levels of MMP-9 (z376.6 ng/mL; n = 19) had significantly poorer overall survival (OS) than patients with lower serum MMP-9 levels (n =52;medianOS, 29.1versus 45.2 months; P = 0.033). High MMP-9 levels were also associated with visceral or bone metastasis (P = 0.027), elevated serum alkaline phosphatase level (P = 0.0009), and presence of liver metastases (P =0.032).SerumlevelsofMMP-1andMMP-13didnotcorrelate with OS. MMP-1and MMP-9 were found mainly in latent forms in serum, whereas the majority of MMP-13 in serum was active (48 kDa) form. MMP-13 was found more often in active form in patients (mean, 99% of the total MMP-13 level) than in controls (mean, 84% of the total MMP-13 level; P < 0.0001). -
Cloning of a Salivary Gland Metalloprotease And
University of Rhode Island DigitalCommons@URI Past Departments Faculty Publications (CELS) College of the Environment and Life Sciences 2003 Cloning of a salivary gland metalloprotease and characterization of gelatinase and fibrin(ogen)lytic activities in the saliva of the Lyme disease tick vector Ixodes scapularis Ivo M.B. Francischetti Thomas N. Mather University of Rhode Island, [email protected] José M.C. Ribeiro Follow this and additional works at: https://digitalcommons.uri.edu/cels_past_depts_facpubs Citation/Publisher Attribution Francischetti, I. M.B., Mather, T. N., & Ribeiro, J. M.C. (2003). Cloning of a salivary gland metalloprotease and characterization of gelatinase and fibrin(ogen)lytic activities in the saliva of the Lyme disease tick vector Ixodes scapularis. Biochemical and Biophysical Research Communications, 305(4), 869-875. doi: 10.1016/S0006-291X(03)00857-X Available at: https://doi.org/10.1016/S0006-291X(03)00857-X This Article is brought to you for free and open access by the College of the Environment and Life Sciences at DigitalCommons@URI. It has been accepted for inclusion in Past Departments Faculty Publications (CELS) by an authorized administrator of DigitalCommons@URI. For more information, please contact [email protected]. NIH Public Access Author Manuscript Biochem Biophys Res Commun. Author manuscript; available in PMC 2010 July 14. NIH-PA Author ManuscriptPublished NIH-PA Author Manuscript in final edited NIH-PA Author Manuscript form as: Biochem Biophys Res Commun. 2003 June 13; 305(4): 869±875. Cloning of a salivary gland metalloprotease and characterization of gelatinase and fibrin(ogen)lytic activities in the saliva of the Lyme Disease tick vector Ixodes scapularis Ivo M. -
ADAM17 Targets MMP-2 and MMP-9 Via EGFR-MEK-ERK Pathway Activation to Promote Prostate Cancer Cell Invasion
1714 INTERNATIONAL JOURNAL OF ONCOLOGY 40: 1714-1724, 2012 ADAM17 targets MMP-2 and MMP-9 via EGFR-MEK-ERK pathway activation to promote prostate cancer cell invasion LI-JIE XIAO1,2*, PING LIN1*, FENG LIN1*, XIN LIU1, WEI QIN1, HAI-FENG ZOU1, LIANG GUO1, WEI LIU1, SHU-JUAN WANG1 and XIAO-GUANG YU1 1Department of Biochemistry and Molecular Biology, College of Basic Medical Science, Harbin Medical University, 194 Xuefu Road, Harbin 150081, Heilongjiang; 2College of Life Science and Technology, Heilongjiang Bayi Agricultural University, 2 Xinyang Road, Daqing 163319, Heilongjiang, P.R. China Received September 8, 2011; Accepted November 18, 2011 DOI: 10.3892/ijo.2011.1320 Abstract. ADAM17, also known as tumor necrosis factor-α released and down-regulation of MMP-2, MMP-9. However, converting enzyme (TACE), is involved in proteolytic ectodo- these effects could be reversed by simultaneous addition of main shedding of cell surface molecules and cytokines. TGF-α. These data demonstrated that ADAM17 contributes to Although aberrant expression of ADAM17 has been shown androgen-independent prostate cancer cell invasion by shed- in various malignancies, the function of ADAM17 in prostate ding of EGFR ligand TGF-α, which subsequently activates the cancer has not been clarified. In the present study, we sought EGFR-MEK-ERK signaling pathway, leading finally to over- to elucidate whether ADAM17 contributes to prostate cancer expression of MMP-2 and MMP-9. This study suggests that the cell invasion, as well as the mechanism involved in the process. ADAM17 expression level may be a new predictive biomarker The expression pattern of ADAM17 was investigated in human of invasion and metastasis of prostate cancer, and ADAM17 prostate cancer cells. -
Serine Proteases with Altered Sensitivity to Activity-Modulating
(19) & (11) EP 2 045 321 A2 (12) EUROPEAN PATENT APPLICATION (43) Date of publication: (51) Int Cl.: 08.04.2009 Bulletin 2009/15 C12N 9/00 (2006.01) C12N 15/00 (2006.01) C12Q 1/37 (2006.01) (21) Application number: 09150549.5 (22) Date of filing: 26.05.2006 (84) Designated Contracting States: • Haupts, Ulrich AT BE BG CH CY CZ DE DK EE ES FI FR GB GR 51519 Odenthal (DE) HU IE IS IT LI LT LU LV MC NL PL PT RO SE SI • Coco, Wayne SK TR 50737 Köln (DE) •Tebbe, Jan (30) Priority: 27.05.2005 EP 05104543 50733 Köln (DE) • Votsmeier, Christian (62) Document number(s) of the earlier application(s) in 50259 Pulheim (DE) accordance with Art. 76 EPC: • Scheidig, Andreas 06763303.2 / 1 883 696 50823 Köln (DE) (71) Applicant: Direvo Biotech AG (74) Representative: von Kreisler Selting Werner 50829 Köln (DE) Patentanwälte P.O. Box 10 22 41 (72) Inventors: 50462 Köln (DE) • Koltermann, André 82057 Icking (DE) Remarks: • Kettling, Ulrich This application was filed on 14-01-2009 as a 81477 München (DE) divisional application to the application mentioned under INID code 62. (54) Serine proteases with altered sensitivity to activity-modulating substances (57) The present invention provides variants of ser- screening of the library in the presence of one or several ine proteases of the S1 class with altered sensitivity to activity-modulating substances, selection of variants with one or more activity-modulating substances. A method altered sensitivity to one or several activity-modulating for the generation of such proteases is disclosed, com- substances and isolation of those polynucleotide se- prising the provision of a protease library encoding poly- quences that encode for the selected variants. -
Matrix Metalloproteinases in Angiogenesis: a Moving Target for Therapeutic Intervention
Matrix metalloproteinases in angiogenesis: a moving target for therapeutic intervention William G. Stetler-Stevenson J Clin Invest. 1999;103(9):1237-1241. https://doi.org/10.1172/JCI6870. Perspective Angiogenesis is the process in which new vessels emerge from existing endothelial lined vessels. This is distinct from the process of vasculogenesis in that the endothelial cells arise by proliferation from existing vessels rather than differentiating from stem cells. Angiogenesis is an invasive process that requires proteolysis of the extracellular matrix and, proliferation and migration of endothelial cells, as well as synthesis of new matrix components. During embryonic development, both vasculogenesis and angiogenesis contribute to formation of the circulatory system. In the adult, with the single exception of the reproductive cycle in women, angiogenesis is initiated only in response to a pathologic condition, such as inflammation or hypoxia. The angiogenic response is critical for progression of wound healing and rheumatoid arthritis. Angiogenesis is also a prerequisite for tumor growth and metastasis formation. Therefore, understanding the cellular events involved in angiogenesis and the molecular regulation of these events has enormous clinical implications. This understanding is providing novel therapeutic targets for the treatment of a variety of diseases, including cancer. Whatever the pathologic condition, an initiating stimulus results in the formation of a migrating solid column of endothelial cells called the vascular sprout. The advancing front of this endothelial cell column presumably focuses proteolytic activity to create a defect in the extracellular matrix, through which the advancing and proliferating column of endothelial […] Find the latest version: https://jci.me/6870/pdf Matrix metalloproteinases in angiogenesis: Perspective a moving target for therapeutic intervention SERIES Topics in angiogenesis David A. -
Gent Forms of Metalloproteinases in Hydra
Cell Research (2002); 12(3-4):163-176 http://www.cell-research.com REVIEW Structure, expression, and developmental function of early diver- gent forms of metalloproteinases in Hydra 1 2 3 4 MICHAEL P SARRAS JR , LI YAN , ALEXEY LEONTOVICH , JIN SONG ZHANG 1 Department of Anatomy and Cell Biology University of Kansas Medical Center Kansas City, Kansas 66160- 7400, USA 2 Centocor, Malvern, PA 19355, USA 3 Department of Experimental Pathology, Mayo Clinic, Rochester, MN 55904, USA 4 Pharmaceutical Chemistry, University of Kansas, Lawrence, KS 66047, USA ABSTRACT Metalloproteinases have a critical role in a broad spectrum of cellular processes ranging from the breakdown of extracellular matrix to the processing of signal transduction-related proteins. These hydro- lytic functions underlie a variety of mechanisms related to developmental processes as well as disease states. Structural analysis of metalloproteinases from both invertebrate and vertebrate species indicates that these enzymes are highly conserved and arose early during metazoan evolution. In this regard, studies from various laboratories have reported that a number of classes of metalloproteinases are found in hydra, a member of Cnidaria, the second oldest of existing animal phyla. These studies demonstrate that the hydra genome contains at least three classes of metalloproteinases to include members of the 1) astacin class, 2) matrix metalloproteinase class, and 3) neprilysin class. Functional studies indicate that these metalloproteinases play diverse and important roles in hydra morphogenesis and cell differentiation as well as specialized functions in adult polyps. This article will review the structure, expression, and function of these metalloproteinases in hydra. Key words: Hydra, metalloproteinases, development, astacin, matrix metalloproteinases, endothelin. -
9/Gelatinase B Reduce NK Cell-Mediated Cytotoxicity
in vivo 22 : 593-598 (2008) A High Concentration of MMP-2/ Gelatinase A and MMP- 9/ Gelatinase B Reduce NK Cell-mediated Cytotoxicity against an Oral Squamous Cell Carcinoma Cell Line BU-KYU LEE 1, MI-JUNG KIM 2, HA-SOON JANG 1, HEE-RAN LEE 2, KANG-MIN AHN 1, JONG-HO LEE 3, PILL-HOON CHOUNG 3 and MYUNG-JIN KIM 3 Departments of 1Oral and Maxillofacial Surgery and 2Cell Biology, Asan Institute for Life Sciences, Asan Medical Center, College of Medicine, Ulsan University, Songpa-ku, 138-040, Seoul; 3Department of Oral and Maxillofacial Surgery, College of Dentistry, Seoul National University, Jongno-ku, 110-768, Seoul, Korea Abstract. Background: Recent studies have shown that advanced state of the disease had generally reduced host matrix metalloproteinases (MMPs) from tumors influence the immune function (3, 4). Nevertheless, the exact role of host immune system to reduce antitumor activity. The aim of immune cells, and of the immune system in general, in the this study was to examine the influence of MMP-2 and development of OSCC and in tumor progression remains MMP-9 on the natural killer (NK) cell. Materials and ambiguous. While the initiation of the process of Methods: NK cells were pretreated with either MMP-2 or tumorigenesis is clearly linked to carcinogens ( i.e. tobacco MMP-9 in the experimental group but not in the control or alcohol), its progression through a series of discrete group. NK cell cytotoxicity against oral squamous cell genetic changes results in the emergence of a tumor that is carcinoma cells (OSCC) were examined using the [Cr 51 ] resistant to immune effector cells (5, 6). -
Signal Transduction, Quorum-Sensing, and Extracellular Protease Activity in Enterococcus Faecalis Biofilm Formation
Signal Transduction, Quorum-Sensing, and Extracellular Protease Activity in Enterococcus faecalis Biofilm Formation The Harvard community has made this article openly available. Please share how this access benefits you. Your story matters Citation Carniol, K., and M. S. Gilmore. 2004. Signal Transduction, Quorum- Sensing, and Extracellular Protease Activity in Enterococcus Faecalis Biofilm Formation. Journal of Bacteriology 186, no. 24: 8161–8163. doi:10.1128/jb.186.24.8161-8163.2004. Published Version doi:10.1128/JB.186.24.8161-8163.2004 Citable link http://nrs.harvard.edu/urn-3:HUL.InstRepos:33867369 Terms of Use This article was downloaded from Harvard University’s DASH repository, and is made available under the terms and conditions applicable to Other Posted Material, as set forth at http:// nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of- use#LAA JOURNAL OF BACTERIOLOGY, Dec. 2004, p. 8161–8163 Vol. 186, No. 24 0021-9193/04/$08.00ϩ0 DOI: 10.1128/JB.186.24.8161–8163.2004 Copyright © 2004, American Society for Microbiology. All Rights Reserved. GUEST COMMENTARY Signal Transduction, Quorum-Sensing, and Extracellular Protease Activity in Enterococcus faecalis Biofilm Formation Karen Carniol1,2 and Michael S. Gilmore1,2* Department of Ophthalmology, Harvard Medical School,1 and The Schepens Eye Research Institute,2 Boston, Massachusetts Biofilms are surface-attached communities of bacteria, en- sponse regulator proteins (10). Only one of the mutants gen- cased in an extracellular matrix of secreted proteins, carbohy- erated, fsrA, impaired the ability of E. faecalis strain V583A to drates, and/or DNA, that assume phenotypes distinct from form biofilms in vitro.