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MMP2 (Human) Recombinant protein (< 1 EU/ug). Protein Activity: MMP-2 activity was measured by its ability to cleave a chromogenic peptide MMP-2 substrate at room Catalog Number: P6073 temperature. At an MMP-2 concentration of 2.5 ug/ml, Regulation Status: For research use only (RUO) 50% cleavage was achieved at an incubation time of approximately 25 minutes. Product Description: Human MMP2 (P08253) partial recombinant protein expressed in Escherichia coli. Recommend Usage: Activity assay SDS-PAGE Sequence: The optimal working dilution should be determined by MYNFFPRKPKWDKNQITYRIIGYTPDLDPETVDDAFAR the end user. AFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYP FDGKDGLLAHAFAPGTGVGGDSHFDDDELWTLGEGQ Storage Buffer: Lyophilized from 0.4x PBS, pH 7.4. VVRVKYGNADGEYCKFPFLFNGKEYNSCTDTGRSDG Storage Instruction: Store at -20°C. FLWCSTTYNFEKDGKYGFCPHEALFTMGGNAEGQPC Reconstitute in water to a concentration of 0.1-1.0 KFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDK mg/mL. Do not vortex. KYGFCPETAMSTVGGNSEGAPCVFPFTFLGNKYESCT For extended storage, it is recommended to further dilute SAGRSDGKMWCATTANYDDDRKWGFCPDQGYSLFL in buffer containing carrier protein (e.g. 0.1% BSA) and VAAHEFGHAMGLEHSQDPGALMAPIYTYTKNFRLSQD store in aliquots at -20°C to -80°C is recommended. DIKGIQELYGASPDIDLGTGPTPTLGPVTPEICKQDIVF DGIAQIRGEIFFFKDRFIWRTVTPRDKPMGPLLVATFW Entrez GeneID: 4313 PELPEKIDAVYEAPQEEKAVFFAGNEYWIYSASTLERG YPKPLTSLGLPPDVQRVDAAFNWSKNKKTYIFAGDKF Gene Symbol: MMP2 WRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQG GGHSYFFKGAYYLKLENQSLKSVKFGSIKSDWLGC Gene Alias: CLG4, CLG4A, MMP-II, MONA, TBE-1 Host: Escherichia coli Gene Summary: Proteins of the matrix metalloproteinase (MMP) family are involved in the Theoretical MW (kDa): 62.0 breakdown of extracellular matrix in normal physiological processes, such as embryonic development, Reactivity: Human reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Applications: Func, SDS-PAGE Most MMP's are secreted as inactive proproteins which (See our web site product page for detailed applications are activated when cleaved by extracellular proteinases. information) This gene encodes an enzyme which degrades type IV Protocols: See our web site at collagen, the major structural component of basement http://www.abnova.com/support/protocols.asp or product membranes. The enzyme plays a role in endometrial page for detailed protocols menstrual breakdown, regulation of vascularization and the inflammatory response. Mutations in this gene have Form: Lyophlized been associated with Winchester syndrome and Nodulosis-Arthropathy-Osteolysis (NAO) syndrome. Two Preparation Method: Escherichia coli expression transcript variants encoding different isoforms have been system found for this gene. [provided by RefSeq] Purity: 90% Endotoxin Level: Endotoxin level is < 0.1 ng/ug of Page 1/1 Powered by TCPDF (www.tcpdf.org).

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Gene Polymorphisms and Circulating Levels of MMP-2 and MMP-9
ANTICANCER RESEARCH 40 : 3619-3631 (2020) doi:10.21873/anticanres.14351 Review Gene Polymorphisms and Circulating Levels of MMP-2 and MMP-9: A Review of Their Role in Breast Cancer Risk SUÉLÈNE GEORGINA DOFARA 1,2,3 , SUE-LING CHANG 1,2 and CAROLINE DIORIO 1,2,3 1Division of Oncology, CHU de Québec-Université Laval Research Center, Quebec City, QC, Canada; 2Cancer Research Center – Laval University, Quebec City, QC, Canada; 3Department of Social and Preventive Medicine, Faculty of Medicine, Laval University, Quebec City, QC, Canada Abstract. MMP-2 and MMP-9 genes have been suggested to (4), as well as other extracellular matrix components, thus play a role in breast cancer. Their functions have been promoting extracellular matrix remodeling and consequently associated with invasion and metastasis of breast cancer; play a key role in several physiological processes, such as however, their involvement in the development of the disease is tissue repair, wound healing, and cell differentiation (5, 6). not well-established. Herein, we reviewed the literature Gelatinases could be involved in carcinogenesis processes, investigating the association between circulating levels and including cell proliferation, angiogenesis, and tumor metastasis polymorphisms of MMP-2 and MMP-9 and breast cancer risk. through their proteolytic function (7). Indeed, the literature Various studies report conflicting results regarding the suggests their involvement in several pathological processes relationship of polymorphisms in MMP-2 and MMP-9 and critical for cancer development, including inflammation, breast cancer risk. Nevertheless, it appears that the T allele in angiogenesis, and cell proliferation, as well as in tumor rs243865 and rs2285053 in MMP-2 are associated with progression (8, 9).
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Proteomic Identification of in Vivo Substrates for Matrix
Proteomic Identification of In Vivo Substrates for Matrix Metalloproteinases 2 and 9 Reveals a Mechanism for Resolution of Inflammation This information is current as of September 23, 2021. Kendra J. Greenlee, David B. Corry, David A. Engler, Risë K. Matsunami, Philippe Tessier, Richard G. Cook, Zena Werb and Farrah Kheradmand J Immunol 2006; 177:7312-7321; ; doi: 10.4049/jimmunol.177.10.7312 Downloaded from http://www.jimmunol.org/content/177/10/7312 References This article cites 48 articles, 14 of which you can access for free at: http://www.jimmunol.org/ http://www.jimmunol.org/content/177/10/7312.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 23, 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 © 2006 by The American Association of Immunologists All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. The Journal of Immunology Proteomic Identiﬁcation of In Vivo Substrates for Matrix Metalloproteinases 2 and 9 Reveals a Mechanism for Resolution of Inﬂammation1 Kendra J. Greenlee,* David B.
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A Therapeutic Role for MMP Inhibitors in Lung Diseases?
ERJ Express. Published on June 9, 2011 as doi: 10.1183/09031936.00027411 A therapeutic role for MMP inhibitors in lung diseases? Roosmarijn E. Vandenbroucke1,2, Eline Dejonckheere1,2 and Claude Libert1,2,* 1Department for Molecular Biomedical Research, VIB, Ghent, Belgium 2Department of Biomedical Molecular Biology, Ghent University, Ghent, Belgium *Corresponding author. Mailing address: DBMR, VIB & Ghent University Technologiepark 927 B-9052 Ghent (Zwijnaarde) Belgium Phone: +32-9-3313700 Fax: +32-9-3313609 E-mail: [email protected] 1 Copyright 2011 by the European Respiratory Society. A therapeutic role for MMP inhibitors in lung diseases? Abstract Disruption of the balance between matrix metalloproteinases and their endogenous inhibitors is considered a key event in the development of pulmonary diseases such as chronic obstructive pulmonary disease, asthma, interstitial lung diseases and lung cancer. This imbalance often results in elevated net MMP activity, making MMP inhibition an attractive therapeutic strategy. Although promising results have been obtained, the lack of selective MMP inhibitors together with the limited knowledge about the exact functions of a particular MMP hampers the clinical application. This review discusses the involvement of different MMPs in lung disorders and future opportunities and limitations of therapeutic MMP inhibition. 1. Introduction The family of matrix metalloproteinases (MMPs) is a protein family of zinc dependent endopeptidases. They can be classified into subgroups based on structure (Figure 1), subcellular location and/or function [1, 2]. Although it was originally believed that they are mainly involved in extracellular matrix (ECM) cleavage, MMPs have a much wider substrate repertoire, and their specific processing of bioactive molecules is their most important in vivo role [3, 4].
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Prognostic Significance of Abnormal Matrix Collagen Remodeling in Colorectal Cancer Based on Histologic and Bioinformatics Analysis
ONCOLOGY REPORTS 44: 1671-1685, 2020 Prognostic significance of abnormal matrix collagen remodeling in colorectal cancer based on histologic and bioinformatics analysis YUQI LIANG1,2, ZHIHAO LV3, GUOHANG HUANG4, JINGCHUN QIN1,2, HUIXUAN LI1,2, FEIFEI NONG1,2 and BIN WEN1,2 1Department of Science and Technology Innovation Center, Guangzhou University of Chinese Medicine; 2Department of PI-WEI Institute of Guangzhou University of Chinese Medicine, Guangzhou, Guangdong 510000; 3Department of Anorectal Surgery, Zhongshan Hospital Affiliated to Guangzhou University of Chinese Medicine, Zhongshan, Guangdong 528400; 4Department of Rehabilitation Sciences, The Hong Kong Polytechnic University, Hong Kong, SAR 999077, P.R. China Received February 25, 2020; Accepted July 20, 2020 DOI: 10.3892/or.2020.7729 Abstract. As the major component of the tumor matrix, CRC. Furthermore, the results of Gene Ontology (GO) and collagen greatly influences tumor invasion and prognosis. Kyoto Encyclopedia of Genes and Genomes (KEGG) analysis The present study compared the remodeling of collagen and suggest that collagen may promote tumor development by collagenase in 56 patients with colorectal cancer (CRC) using activating platelets. Collectively, the abnormal collagen Sirius red stain and immunohistochemistry, exploring the remodeling, including associated protein and coding genes is relationship between collagen remodeling and the prognosis associated with the tumorigenesis and metastasis, affecting the of CRC. Weak or strong changes in collagen fiber arrange- prognosis of patients with CRC. ment in birefringence were observed. With the exception of a higher density, weak changes equated to a similar Introduction arrangement in normal collagen, while strong changes facilitated cross-linking into bundles. Compared with normal Colorectal cancer (CRC) has a high global incidence and tissues, collagen I (COL I) and III (COL III) deposition was mortality rate (1).
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Expression of Matrix Metalloproteinase (MMP)-2 and MMP-9 in Breast Cancer with a Special Reference to Activator Protein-2, HER2, and Prognosis
Vol. 10, 7621–7628, November 15, 2004 Clinical Cancer Research 7621 Expression of Matrix Metalloproteinase (MMP)-2 and MMP-9 in Breast Cancer with a Special Reference to Activator Protein-2, HER2, and Prognosis Johanna M. Pellikainen,1,2,3 Kirsi M. Ropponen,2 positive disease. In the univariate survival analysis, positive Vesa V. Kataja,3 Jari K. Kellokoski,4 stromal MMP-9 predicted shorter recurrence-free survival and breast cancer-related survival (0.0389 ؍ RFS; P) 1,2,3,6 5 ؉ ؍ Matti J. Eskelinen, and Veli-Matti Kosma 1 (BCRS; P 0.0081) in ER disease, especially in the sub- ؍ > Department of Pathology and Forensic Medicine, University of ؉ 2 3 group of ER tumors of 2 cm in diameter (T1; P 0.0031 ؍ ,Kuopio, Kuopio, Finland; Departments of Pathology, Oncology 4Otorhinolaryngology, Oral and Maxillofacial Unit, and 5Surgery, for RFS, and P 0.0089 for BCRS). High MMP-9 expres- in the (0.0351 ؍ Kuopio University Hospital, Kuopio, Finland; and 6Department of sion in cancer cells predicted longer RFS (P Pathology, Centre for Laboratory Medicine, University of Tampere whole patient group. In the multivariate analysis of the and Tampere University Hospital, Tampere, Finland whole patient group, the independent predictors of shorter RFS were reduced MMP-9 expression in carcinoma cells ؍ ؍ ABSTRACT (P 0.0248), HER2 overexpression (P 0.0001), and ad- -Shorter BCRS was pre .(0.0002 ؍ vanced-stage disease (P Purpose: In the present study, we investigated the ex- dicted by advanced-stage disease (P < 0.0001). pression and prognostic value of matrix metalloproteinase Conclusions: Expression of MMP-2 and MMP-9 in (MMP)-2 and MMP-9 in breast cancer as well as their breast cancer seems to be partly related to expression of relation to transcription factor activator protein (AP)-2 AP-2 and HER2.
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Polymorphisms in Matrix Metalloproteinases 2, 3, and 8 Increase Recurrence and Mortality Risk by Regulating Enzyme Activity in Gastric Adenocarcinoma
www.impactjournals.com/oncotarget/ Oncotarget, 2017, Vol. 8, (No. 62), pp: 105971-105983 Research Paper Polymorphisms in matrix metalloproteinases 2, 3, and 8 increase recurrence and mortality risk by regulating enzyme activity in gastric adenocarcinoma Youdong Lin1, Jinsheng Liu2, Long Jin3 and Yun Jiang4 1Fujian Shengli Clinical Medical College of Fujian Medical University and Department of Clinical Laboratory Medicine, Fujian Provincial Hospital, Fuzhou, Fujian 350001, China 2Department of Gastrointestinal Surgery, Fujian Provincial Hospital, Fuzhou, Fujian 350001, China 3Department of Pathology, Fujian Provincial Hospital, Fuzhou, Fujian 350001, China 4Department of VIP Clinic, Fujian Provincial Hospital, Fuzhou, Fujian 350001, China Correspondence to: Youdong Lin, email: [email protected] Keywords: matrix metalloproteinases; polymorphisms; enzyme activity; gastric adenocarcinoma; clinical outcomes Received: September 26, 2016 Accepted: October 29, 2017 Published: November 20, 2017 Copyright: Lin et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License 3.0 (CC BY 3.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. ABSTRACT The association of polymorphisms in matrix metalloproteinases (MMPs) with clinical outcomes of gastric adenocarcinoma has not been examined. Ten polymorphisms in MMP1, 2, 3, 7, 8, 9, 12, and 13 were genotyped and investigated, and patients were followed for an average of 58 months. The activities of MMP2, 3, and 8 were measured. Recurrence risk increased in patients with the MMP2 rs2285053 CC genotype (hazard ratio [HR], 1.85), MMP3 rs679620 AA genotype (HR, 2.15), and MMP8 rs1940475 TT genotype (HR, 2.22) on recurrence free survival (RFS).
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Biochemical Characterization and Zinc Binding Group (Zbgs) Inhibition Studies on the Catalytic Domains of Mmp7 (Cdmmp7) and Mmp16 (Cdmmp16)
MIAMI UNIVERSITY The Graduate School Certificate for Approving the Dissertation We hereby approve the Dissertation of Fan Meng Candidate for the Degree DOCTOR OF PHILOSOPHY ______________________________________ Director Dr. Michael W. Crowder ______________________________________ Dr. David L. Tierney ______________________________________ Dr. Carole Dabney-Smith ______________________________________ Dr. Christopher A. Makaroff ______________________________________ Graduate School Representative Dr. Hai-Fei Shi ABSTRACT BIOCHEMICAL CHARACTERIZATION AND ZINC BINDING GROUP (ZBGS) INHIBITION STUDIES ON THE CATALYTIC DOMAINS OF MMP7 (CDMMP7) AND MMP16 (CDMMP16) by Fan Meng Matrix metalloproteinase 7 (MMP7/matrilysin-1) and membrane type matrix metalloproteinase 16 (MMP16/MT3-MMP) have been implicated in the progression of pathological events, such as cancer and inflammatory diseases; therefore, these two MMPs are considered as viable drug targets. In this work, we (a) provide a review of the role(s) of MMPs in biology and of the previous efforts to target MMPs as therapeutics (Chapter 1), (b) describe our efforts at over-expression, purification, and characterization of the catalytic domains of MMP7 (cdMMP7) and MMP16 (cdMMP16) (Chapters 2 and 3), (c) present our efforts at the preparation and initial spectroscopic characterization of Co(II)-substituted analogs of cdMMP7 and cdMMP16 (Chapters 2 and 3), (d) present inhibition data on cdMMP7 and cdMMP16 using zinc binding groups (ZBG) as potential scaffolds for future inhibitors (Chapter 3), and (e) summarize our data in the context of previous results and suggest future directions (Chapter 4). The work described in this dissertation integrates biochemical (kinetic assays, inhibition studies, limited computational methods), spectroscopic (CD, UV-Vis, 1H-NMR, fluorescence, and EXAFS), and analytical (MALDI-TOF mass spectrometry, isothermal calorimetry) methods to provide a detailed structural and mechanistic view of these MMPs.
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Towards Third Generation Matrix Metalloproteinase Inhibitors for Cancer Therapy
British Journal of Cancer (2006) 94, 941 – 946 & 2006 Cancer Research UK All rights reserved 0007 – 0920/06 $30.00 www.bjcancer.com Minireview Towards third generation matrix metalloproteinase inhibitors for cancer therapy ,1 1 CM Overall* and O Kleifeld 1CBCRA Program in Breast Cancer Metastasis, Departments of Oral Biological & Medical Sciences, Biochemistry & Molecular Biology, The UBC Centre for Blood Research, University of British Columbia, Vancouver, BC, Canada V6T 1Z3 The failure of matrix metalloproteinase (MMP) inhibitor drug clinical trials in cancer was partly due to the inadvertent inhibition of MMP antitargets that counterbalanced the benefits of MMP target inhibition. We explore how MMP inhibitor drugs might be developed to achieve potent selectivity for validated MMP targets yet therapeutically spare MMP antitargets that are critical in host protection. British Journal of Cancer (2006) 94, 941–946. doi:10.1038/sj.bjc.6603043 www.bjcancer.com Published online 14 March 2006 & 2006 Cancer Research UK Keywords: target validation; antiproteolytic drug; cancer therapy; drug design; zinc chelation Twenty five years ago, the therapeutic strategy of controlling avenues for the therapeutic control of cancer. Conversely, stromal cancer by broadly targeting collagenase (matrix metalloproteinase cells harness the beneficial actions of MMPs in tissue homeostasis (MMP)1), stromelysin-1 (MMP3), and gelatinase A (MMP2), the and innate immunity for host resistance against cancer (Overall three then known MMPs, was founded on reducing degradation of and Kleifeld, 2006). All MMPs exhibit some of these functions, basement membrane and extracellular matrix proteins by cancer but MMPs -3, -8 and -9 have activities so important that when cells in metastasis and angiogenesis (Liotta et al, 1980; Hodgson, genetically knocked out, this leads to enhanced tumorigenesis and 1995).
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Trophoblast Survival Signaling During Human Placentation Requires HSP70 Activation of MMP2-Mediated HBEGF Shedding
Cell Death and Differentiation (2017) 24, 1772–1783 & 2017 Macmillan Publishers Limited, part of Springer Nature. All rights reserved 1350-9047/17 www.nature.com/cdd Trophoblast survival signaling during human placentation requires HSP70 activation of MMP2-mediated HBEGF shedding Chandni V Jain1,2, Philip Jessmon2,3, Charbel T Barrak2, Alan D Bolnick2, Brian A Kilburn2, Michael Hertz2 and D Randall Armant*,2,3 Survival of trophoblast cells in the low oxygen environment of human placentation requires metalloproteinase-mediated shedding of HBEGF and downstream signaling. A matrix metalloproteinase (MMP) antibody array and quantitative RT-PCR revealed upregulation of MMP2 post-transcriptionally in human first trimester HTR-8/SVneo trophoblast cells and placental villous explants exposed to 2% O2. Specific MMP inhibitors established the requirement for MMP2 in HBEGF shedding and upregulation. Because α-amanitin inhibited the upregulation of HBEGF, differentially expressed genes were identified by next-generation sequencing of RNA from trophoblast cells cultured at 2% O2 for 0, 1, 2 and 4 h. Nine genes, all containing HIF-response elements, were upregulated at 1 h, but only HSPA6 (HSP70B’) remained elevated at 2–4 h. The HSP70 chaperone inhibitor VER 155008 blocked upregulation of both MMP2 and HBEGF at 2% O2, and increased apoptosis. However, both HBEGF upregulation and apoptosis were rescued by exogenous MMP2. Proximity ligation assays demonstrated interactions between HSP70 and MMP2, and between MMP2 and HBEGF, supporting the concept that MMP2-mediated shedding of HBEGF, initiated by HSP70, contributes to trophoblast survival at the low O2 concentrations encountered during the first trimester, and is essential for successful pregnancy outcomes.
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Polymorphisms of Genes Involved in Extracellular Matrix Remodeling And
CORE Metadata, citation and similar papers at core.ac.uk Provided by Florence Research BASIC RESEARCH STUDIES Polymorphisms of genes involved in extracellular matrix remodeling and abdominal aortic aneurysm Claudia Saracini, PhD,a Paola Bolli, PhD,a Elena Sticchi, PhD,a,b Giovanni Pratesi, MD,c Raffaele Pulli, MD,d Francesco Sofi, PhD,a Carlo Pratesi, MD,d Gian Franco Gensini, MD,a,b Rosanna Abbate, MD,a and Betti Giusti, PhD,a Florence and Rome, Italy Background: Abdominal aortic aneurysm (AAA) has a multifactorial etiology and the relevance of genetic factors is getting increasing interest, in particular those related to the destructive remodeling of extracellular matrix. Methods: We performed a candidate gene association study of polymorphisms in genes coding matrix metalloproteinases (MMPs), tissue inhibitors of MMPs (TIMPs), and elastin (ELN) in AAA. DNA samples from 423 AAA patients and 423 ;controls were genotyped for 12 polymorphisms in 10 genes: MMP1 (؊1607G/GG), MMP2 (؊735C/T; ؊1306C/T ,(؊1575 G/A), MMP3 (5A/6A), MMP9 (؊1562C/T), MMP10 (A180G), MMP-12 (؊82A/G), MMP-13 (؊77A/G .(TIMP1 (C434T), TIMP3 (؊1296T/C), and ELN (G1355A Results: Genotype distribution was significantly different between patients and controls for the following polymorphisms: ؊1306C/T MMP2; 5A/6A MMP3; ؊77A/G MMP-13; G1355A ELN; and C434T TIMP1. In a multivariable logistic regression analysis adjusted for traditional cardiovascular risk factors and chronic obstructive pulmonary disease, confidence interval, CI .34-.85], P < .007) and G1355A ELN %95] 0.55 ؍ [؊1306C/T MMP2 (odds ratios [OR polymorphisms resulted in independent protective factors for abdominal aortic (046.
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Matrix Metalloproteinases As Potential Biomarkers and Therapeutic Targets in Liver Diseases
cells Review Matrix Metalloproteinases as Potential Biomarkers and Therapeutic Targets in Liver Diseases Eline Geervliet and Ruchi Bansal * Translational Liver Research, Department of Medical Cell BioPhysics, Technical Medical Centre, Faculty of Science and Technology, University of Twente, 7522 NB Enschede, The Netherlands; [email protected] * Correspondence: [email protected]; Tel.: +31-53-489-3115 Received: 6 April 2020; Accepted: 13 May 2020; Published: 13 May 2020 Abstract: Chronic liver diseases, characterized by an excessive accumulation of extracellular matrix (ECM) resulting in scar tissue formation, are a growing health problem causing increasing morbidity and mortality worldwide. Currently, therapeutic options for tissue fibrosis are severely limited, and organ transplantation is the only treatment for the end-stage liver diseases. During liver damage, injured hepatocytes release proinflammatory factors resulting in the recruitment and activation of immune cells that activate quiescent hepatic stellate cells (HSCs). Upon activation, HSCs transdifferentiate into highly proliferative, migratory, contractile and ECM-producing myofibroblasts. The disrupted balance between ECM deposition and degradation leads to the formation of scar tissue referred to as fibrosis. This balance can be restored either by reducing ECM deposition (by inhibition of HSCs activation and proliferation) or enhancing ECM degradation (by increased expression of matrix metalloproteinases (MMPs)). MMPs play an important role in ECM remodeling and represent an interesting target for therapeutic drug discovery. In this review, we present the current knowledge about ECM remodeling and role of the different MMPs in liver diseases. MMP expression patterns in different stages of liver diseases have also been reviewed to determine their role as biomarkers.
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Expression of MT-1 MMP, MMP2, MMP9 and TIMP2 Mrnas in Ductal Carcinoma in Situ and Invasive Ductal Carcinoma of the Breast
Yonsei Medical Journal Vol. 47, No. 3, pp. 333 - 342, 2006 Expression of MT-1 MMP, MMP2, MMP9 and TIMP2 mRNAs in Ductal Carcinoma in Situ and Invasive Ductal Carcinoma of the Breast Hee Jung Kim,1 Chan-il Park,2 Byeong Woo Park,3 Hy-de Lee,3 and Woo Hee Jung2 1Department of Pathology, MizMedi Breast Center, MizMedi Hospital, Seoul, Korea; 2Department of Pathology, 3Surgery, Yonsei University College of Medicine, Seoul, Korea. We investigated the expression of membrane type-1 (MT1)- in tumor growth, as well as the utility of CD44std as a pro- MMP, MMP2, MMP9 and TIMP2 mRNAs and their roles in gnostic indicator of breast cancer. ductal carcinoma in situ (DCIS) and T1 and T2 invasive ductal Key Words: Carcinoma, ductal, breast, MT1-MMP, MMP2, carcinoma of the breast. We further compared these two types MMP9, TIMP2, prognosis of carcinomas for differences in microvessel density, and expres- sion of angiogenic factors and CD44std. MT1-MMP, MMP2, MMP9 and TIMP2 mRNA were expressed in both DCIS and invasive ductal carcinomas. Expression rates of MT1-MMP, INTRODUCTION MMP2, MMP9 and TIMP2 mRNAs were not statistically dif- ferent between DCIS and invasive ductal carcinomas, nor did Degradation of basement membranes and ex- they differ statistically when grouped by tumor size, histologic grade or nuclear grade of invasive ductal carcinoma. Microvessel tracellular matrix is an essential process in inva- density and expression of VEGF and TGF-β1 were not statisti- sion and metastasis in malignant tumors. MMP, cally different between DCIS and invasive ductal carcinoma. potent proteolytic enzymes are known to play key CD44std expression was significantly increased in DCIS roles in this process.
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