Are matrix metalloproteinases and their inhibitors reliable diagnosis biomarkers and attractive therapeutic targets in endometriosis? Patrick Henriet, Khin Su Mon, Etienne Marbaix De Duve Institute, Université catholique de Louvain, Brussels, Belgium Abstract: Matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs) are expressed in the human endometrium during the menstrual cycle, in particular to induce substantial extracellular matrix breakdown underlying menstruation. Endometriosis (EM) is characterized by the presence of endometrial tissue at ectopic locations. Because EM is thought to often develop from retrograde menstruation followed by implantation of menstrual tissue fragments at ectopic sites, endometrial MMPs and TIMPs were rapidly suspected as contributors to EM development and progression, generating hope for their use as biomarkers to facilitate EM diagnosis and as potential targets for developing new therapies against EM. Here, we not only summarize a
Matrix metalloproteinases in impaired wound healing Fabio Sabino, Ulrich auf dem Keller Institute of Molecular Health Sciences, Eidgenössische Technische Hochschule (ETH) Zürich, Zürich, Switzerland Abstract: Cutaneous wound healing is a complex tissue response that requires a coordinated interplay of multiple cells in orchestrated biological processes to finally re-establish the skin's barrier function upon injury. Proteolytic enzymes and in particular matrix metalloproteinases (MMPs) contribute to all phases of the healing process by regulating immune cell influx, facilitating migration of fibroblasts and keratinocytes, and remodeling of the scar tissue. As a result of these pleiotropic functions in the healing skin wound, uncontrolled activities of MMPs are associated with impaired wound healing, a growing health problem in Western countries due to increased life expectancies and rising rates of underlying diseases, such as diabetes. However, detailed mechanisms have been only
The key findings of this study are that stress-related biobehavioral factors were associated with both stromal and tumor expression of factors supporting angiogenesis and invasion in the tumor microenvironment of ovarian cancer patients. Specifically, depressed patients and patients reporting higher levels of chronic stress, current stress, and negative affect showed higher MMP-9 expression in TAMs. In contrast, patients with higher levels of social support had lower levels of VEGF and MMP-9 expression in tumor cells. MMP-2 expression by macrophages or tumor cells was not significantly associated with any of the biobehavioral factors examined. To the best of our knowledge, this is the first clinical study to show significant associations between biobehavioral factors and stromal macrophage production of MMPs.. These findings extend previous experiments showing that chronic stress and social isolation increase expression of VEGF and MMP-9 by human ovarian tumors implanted orthotopically in mice ...
Matrix metalloproteinases (MMPs) are a group of structurally related proteolytic enzymes containing a zinc ion in the active site. They are secreted from cells or bound to the plasma membrane and hydrolyze extracellular matrix (ECM) and cell surface-bound molecules. They therefore play key roles in morphogenesis, wound healing, tissue repair and remodeling in diseases such as cancer and arthritis. Although the cell anchored membrane-type MMPs (MT-MMPs) function pericellularly, the secreted MMPs have been considered to act within the ECM, away from the cells from which they are synthesized. However, recent studies have shown that secreted MMPs bind to specific cell surface receptors, membrane-anchored proteins or cell-associated ECM molecules and function pericellularly at focussed locations. This minireview describes examples of cell surface and pericellular partners of MMPs, as well as how they alter enzyme function and cellular behaviour.
Background: Pressure-overload causes left ventricular (LV) remodeling with one of the structural milestones of this process being extracellular matrix remodeling and fibrosis. While the regulation of matrix metalloproteinases (MMPs) likely plays a role in this process, the induction and mechanistic role of specific MMPs is poorly understood. Recent in-vivo studies have suggested that the transmembrane MMP, MT1-MMP can actually induce a profibrotic process and thereby effect matrix remodeling and fibrosis in PO. This study tested the hypothesis that in-vivo induction of MT1-promoter activity and expression occurs with PO.. Methods: MT1-MMP promoter activity (MT1-PROM act) was measured by generating a transgenic mouse (FVB; full length human MT1-MMP promoter ligated to the firefly luciferase gene). MT1-MMP PROM reporter mice underwent PO (4 weeks transverse aortic constriction n = 13) and were compared to non-banded controls (n = 10). In-vivo MT1-PROM act was quantified by luciferase mRNA ...
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MMPs degrade the extracellular matrix of proteins, cleave cell surface receptors, release apoptotic ligands, and support activity of chemokine/cytokines.
Sigma-Aldrich offers abstracts and full-text articles by [Eyal Zcharia, Juan Jia, Xiao Zhang, Lea Baraz, Ulf Lindahl, Tamar Peretz, Israel Vlodavsky, Jin-Ping Li].
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The EU Joint Programme - Neurodegenerative Disease Research (JPND) is the largest global research initiative aimed at tackling the challenge of neurodegenerative diseases, in particular, Alzheimers. Join Us ...
We focus on the epithelial-specific integrin αvβ6 as therapeutic target for carcinoma because it is not expressed by most normal tissues but is upregulated on many carcinomas including breast, colon, lung, pancreas and cervix making it a novel therapeutic target. We have been the first to show that αvβ6 promoted invasion, in part, by regulating matrix-metalloproteinases (MMPs). Strong expression of αvβ6 correlates with very poor prognosis from breast cancer. The BCI αvβ6-specific peptide (A20FMDV2) is being developed for radio-imaging of human cancers ...
Background: Glioblastomas (GBM), the most frequent malignant brain tumors in adults, are characterized by an aggressive local growth pattern and highly invasive tumor cells. This invasion is facilitated by expression of matrix metalloproteinases (MMPs), a family of zinc-dependent endopeptidases. They mediate the degradation of protein components of the extracellular matrix. Twenty-three family members are known. Elevated levels of several of them have been reported in GBM. GBM cell-lines are used for in vitro studies of cell migration and invasion. Therefore, it is essential to know their MMP expression patterns. Only limited data for some of the cell-lines are published, yet. To fill the gaps in our knowledge would help to choose suitable model systems for analysis of regulation and function of MMPs during GBM tumorigenesis, cell migration and invasion. Findings: We analysed MMP-1, -8, -9, -10, -11, -13, -17, -19, -20, -21, -23, -24, -26, -27, and MMP-28 expression in seven GBM cell-lines ...
Secreted active proteases, from families of enzymes such as matrix metalloproteinases (MMPs) and ADAMs (a disintegrin and metalloproteinases), participate in diverse pathological processes. To simultaneously measure multiple specific protease activities, a series of parallel enzyme reactions combined with a
2. Matrix Metalloproteinases (MMP) - are responsible for breaking down proteins. They are found throughout the body but in skin their role is to breakdown and recycle the skin matrix of the dermis, specifically collagen and elastin. Typically, this is a bad thing because it weakns the matrix and leads to wrinkles; however, this is a good thing if the enzymes are breaking down damaged or worn out structural proteins, facilitating wound healing, or clearing a way for white blood cells to move into infected areas. Some skin care ingredients are designed to inhibit these enzymes ...
I have set logic so that depending on what is selected from a drop down, the user is taken to a specific matrix, which are all on different pages. After they an...
Matrix metalloproteinases (MMPs) are a family of endoproteases that require zinc and calcium for expressing catalytic activity. These enzymes
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TY - JOUR. T1 - Extracellular matrix metalloproteinase inducer (CD147) confers resistance of breast cancer cells to anoikis through inhibition of bim. AU - Yang, Jin Ming. AU - ONeill, Peter. AU - Jin, Wei. AU - Foty, Ramsey. AU - Medina, Daniel J.. AU - Xu, Zude. AU - Lomas, Mehnaaz. AU - Arndt, Greg M.. AU - Tang, Yi. AU - Nakada, Marian. AU - Yan, Li. AU - Hait, William N.. PY - 2006/4/7. Y1 - 2006/4/7. N2 - Overexpression of extracellular matrix metalloproteinase inducer (EMMPRIN or CD147), a member of the immunoglobulin family and a glycoprotein enriched on the surface of tumor cells, promotes invasion, metastasis, and growth and survival of malignant cells and confers resistance to some chemotherapeutic drugs. However, the molecular mechanisms underlying the actions of EMMPRIN are not fully understood. In this study we sought to determine whether EMMPRIN contributes to the malignant phenotype of breast cancer by inhibiting anoikis, a form of apoptosis induced by loss or alteration of ...
Tumor necrosis factor-alpha is released from cells by a proteolytic cleavage. Previous work suggested that a specific, non-matrix metalloproteinase carries out this cleavage, but matrix metalloproteinases have also been implicated. In this paper, we report that none of the matrix metalloproteinases tested cleaved peptide substrates as specifically as the non-matrix metalloproteinase. A matrix metalloproteinase did process tumor necrosis factor-alpha extracted from COS cells, but neither tissue inhibitor of metalloproteinases-1 nor -2 blocked tumor necrosis factor-alpha processing by human monocytes. Moreover, tissue inhibitor of metalloproteinases-1 had at most a partial effect on the in vivo release of the cytokine in mice. We conclude that a non-matrix metalloproteinase is the major physiological tumor necrosis factor-alpha convertase.
The irreversible destruction of the tissues that comprise synovial joints is the hallmark of both rheumatoid arthritis and osteoarthritis. In both diseases, inflammatory cytokines, such as interleukin-1β, stimulate the production of matrix metalloproteinases (MMPs), a family of enzymes that collectively degrade all components of the extra-cellular matrix. The collagenases, a subgroup of the MMP family, have the unique ability to cleave the collagen fibrils that comprise cartilage, tendon, and bone, and thereby provide the rate-limiting step in the degradation of many joint structures. In the arthritides, MMP-1 and MMP-13 (collagenase-1 and collagenase-3, respectively) are key mediators of joint destruction, and therefore represent potential therapeutic targets. In this thesis, we identified the rexinoid LG100268 (LG268), a ligand for the nuclear hormone receptor (NHR) RXR, as a novel, selective inhibitor of MMP-1 and -13 expression, and investigated the molecular mechanisms behind its ...
The irreversible destruction of the tissues that comprise synovial joints is the hallmark of both rheumatoid arthritis and osteoarthritis. In both diseases, inflammatory cytokines, such as interleukin-1β, stimulate the production of matrix metalloproteinases (MMPs), a family of enzymes that collectively degrade all components of the extra-cellular matrix. The collagenases, a subgroup of the MMP family, have the unique ability to cleave the collagen fibrils that comprise cartilage, tendon, and bone, and thereby provide the rate-limiting step in the degradation of many joint structures. In the arthritides, MMP-1 and MMP-13 (collagenase-1 and collagenase-3, respectively) are key mediators of joint destruction, and therefore represent potential therapeutic targets. In this thesis, we identified the rexinoid LG100268 (LG268), a ligand for the nuclear hormone receptor (NHR) RXR, as a novel, selective inhibitor of MMP-1 and -13 expression, and investigated the molecular mechanisms behind its ...
TY - JOUR. T1 - Progression of mycosis fungoides is associated with changes in angiogenesis and expression of the matrix metalloproteinases 2 and 9. AU - Vacca, A.. AU - Moretti, S.. AU - Ribatti, D.. AU - Pellegrino, A.. AU - Pimpinelli, N.. AU - Bianchi, B.. AU - Bonifazi, E.. AU - Ria, R.. AU - Serio, G.. AU - Dammacco, F.. PY - 1997/9. Y1 - 1997/9. N2 - Changes in angiogenesis and expression of extracellular matrix-degrading enzymes have been substantiated during progression of solid tumours, whereas information on haematological tumours remains circumstantial. In this study, 57 biopsies of mycosis fungoides (MF), a haematological tumour of T-cell lineage, were investigated immunohistochemically for the extent of angiogenesis, and by in situ hybridisation for the expression of matrix metalloproteinases 2 (MMP-2, collagenase A) and 9 (MMP-9, collagenase B). The biopsies we grouped according to the stage of progression: patch → plaque → nodular (most advanced). The extent of angiogenesis, ...
Read "Enhanced matrix metalloproteinase expression by Tisseel in mesothelial cells, normal peritoneal fibroblasts, and adhesion fibroblasts, European Journal of Plastic Surgery" on DeepDyve, the largest online rental service for scholarly research with thousands of academic publications available at your fingertips.
Sex steroids are inevitable in women. However, long-term exposure to sex steroids increases the risk of breast cancer. A complete understanding of sex steroid control of the breast and how it relates to breast cancer risk is still lacking. Angiogenesis and proteolytic enzyme activity are crucial for the process by which tumors evolve into a vascularized, invasive phenotype. Matrix metalloproteinases are potent matrixdegrading enzymes that affect several steps in tumor progression including angiogenesis. In the female reproductive organs, sex steroids regulate angiogenesis and MMP activity, yet little is known how sex steroids affect these crucial events in normal and malignant breast tissue.. This thesis elucidates a link between sex steroids, MMP activity, and angiogenesis. It is shown that estradiol down-regulates while tamoxifen up-regulates the protein expression and activity of MMP-2 and MMP-9 in human breast cancer cells in vitro and in human breast cancer xenografts in vivo. The results ...
Abstract. Background: Colorectal cancer metastasis is a multistep process involving degradation of extracellular matrix components by proteolytic enzymes. Among them, matrix metalloproteinases (MMPs) are the principal degrading enzymes and their expressions/activities are also correlated with survival. Much research has showed the associations between genetic polymorphisms in MMPs and risk of colorectal cancer; however, their prognostic significance has not been well determined.. Methods: We selected and genotyped 4 cancer-associated single nucleotide polymorphisms (SNPs) in a cohort of 282 colorectal cancer patients. The associations of these SNPs with distant metastasis-free survival and overall survival were evaluated by Kaplan-Meier analysis, Cox regression model, and survival tree analysis.. Results: The relative risks of developing distant metastasis after curative surgery were higher in individuals with minor homozygote AA genotype than in those with GG/GA genotypes at MMP2 rs243866 (P = ...
Paper I: Furenes EB, Seljeflot I, Solheim S, Hjerkinn EM, Arnesen H. Long-term influence of diet and/or omega-3 fatty acids on matrix metalloproteinase-9 and pregnancy-associated plasma protein-A in men at high risk of coronary heart disease. Scand J Clin Lab Invest 2008; 68: 177-184. The paper is removed from the thesis in DUO due to publisher restrictions. The published version is available at: https://doi.org/10.1080/00365510701663350 ...
BIOZYME, INC. BioZyme, Inc. is the only company to offer both selective and sensitive fluorescence substrates (FRET) for the Matrix Metalloproteinase (MMP) and A Disintegrin and Metalloproteinase (ADAM) Family members. We also have the most competitive pricing for fluorescence substrates (FRET) for the Matrix Metalloproteinase (MMP) and A Disintegrin and Metalloproteinase (ADAM) Family members as well as recombinant human ADAM8 enzyme.. See our online catalog or our individual Product Sheets located on this website.. Many of Biozyme, Inc. ADAM and MMP fluorescent substrates have been used successfully to screen biological samples of all kinds. All of our ADAM substrates and MMP substrates have been used in a technique called proteolytic matrix analysis or PrAMA to decipher the contributions of different metalloproteinase activities in a biological sample even though the substrates are not completely selective. With this technique, the MMP substrates and ADAM substrates have helped quantify MMP9, ...
Published in Trends in Cardiovascular Medicine, Volume 14, Issue 3, 2004, pages 105-111. © Trends in Cardiovascular Medicine, 2004, Elsevier Publishing. Lessner, S.M., Galis, Z.S. (2004). Matrix Metalloproteinases and Vascular Endothelium-Mononuclear Cell Close Encounters. Trends in Cardiovascular Medicine, 14(3), 105-111.. http://dx.doi.org/10.1016/j.tcm.2003.12.009. ...
ProMMP1 has several activators including plasmin (Eeckhout & Vaes 1977, Werb et al. 1977, Santala et al. 1999), trypsin (Grant et al. 1987, Saunders et al. 2005), plasma kallikrein (Nagase et al. 1982, Saunders et al. 2005), chymase (Saarinen et al. 1994, Suzuki et al. 1995, Saunders et al. 2005), tryptase (Gruber et al. 1989, Suzuki et al. 1995, Saunders et al. 2005), neutrophil elastase, cathepsin G (Saunders et al. 2005) and trypsin-2 (Moilanen et al. 2003). Concanavalin A (ConA) was the first cellular treatment that yielded active MMPs in culture, inducing the cellular activation of MMP1 likely through MMP14 activity (Overall and Sodek 1990).Trypsin-like serine proteinases are believed to remove 34-36 residues from the N-terminus of the secreted pro-enzyme, equivalent to positions 53-55 of the UniProt cannonical sequence which includes a signal peptide. Removal of this region is sufficient to destabilize the Cys92-Zn2+ stabilizing bond (numbered according to the Uniprot canonical sequence, ...
PubMed comprises more than 30 million citations for biomedical literature from MEDLINE, life science journals, and online books. Citations may include links to full-text content from PubMed Central and publisher web sites.
Tissue inhibitors of metalloproteinases (TIMPs) are a family of closely related proteins that inhibit matrix metalloproteinases (MMPs). In the central nervous system (CNS), TIMPs 2, 3, and 4 are constitutively expressed at high levels, whereas TIMP1 can be induced by various stimuli. Here, we studied the effects of constitutive expression of TIMP1 in the CNS in transgenic mice. Transgene expression started prenatally and persisted throughout lifetime at high levels. Since MMP activity has been implicated in CNS development, in proper function of the adult CNS, and in inflammatory disorders, we investigated Timp1-induced CNS alterations. Despite sufficient MMP inhibition, high expressor transgenic mice had a normal phenotype. The absence of compensatory up-regulation of MMP genes in the CNS of Timp1 transgenic mice indicates that development, learning, and memory functions do not require the entire MMP arsenal. To elucidate the effects of strong Timp1 expression in CNS inflammation, we induced ...
Extracellular matrix provides the microenvironment for the cells and serves as a tissue scaffold, guiding cell migration during embryonic development and wound repair. Beyond that, it also functions as the repository and modulator of growth factors and cytokines, and therefore is responsible for transmitting environmental signals to the cells.. Among proteases, the matrix metalloproteinases (MMPs) and a disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS) family are often associated with ECM degradation and remodeling. The inhibitors of MMPs are called tissue inhibitors of metalloproteinases (TIMPs), which are comprised of TIMP-1, TIMP-2, TIMP-3, and TIMP-4. The interactions between these proteases and their inhibitors play important roles in cell morphogenesis, angiogenesis, tissue remodeling, tissue repair, tumor metastasis, cirrhosis, and arthritis. The features of the ECM are determined both by the cells that produce the matrix and by the cells growing in it. QIAGENs ...
(2010) Mishra et al. Reproductive Biology and Endocrinology. Background: Extracellular matrix metalloproteinase inducer (EMMPRIN) regulates several biological functions involving the modulation of cell behaviors via cell-cell and cell-matrix interactions. According to its diverse functions, we hy...
2974 Matrix metalloproteinases (MMPs) are a family of zinc dependent proteins that selectively degrade components of the extracellular matrix (ECM). MMPs can be categorized based on their substrate specificity and sequence characteristics. Our previous study identified elevated expression of 12 MMPs in African American cell lines when compared to their Caucasian counterparts. This study investigates the expression of the 12 potential biomarkers and their regulation by RECK, (reversion inducing cysteine-rich protein with Kazal motifs), in metastatic cell lines. RECK is a membrane-anchored glycoprotein that negatively regulates matrix metalloproteinases and inhibits tumor metastasis and angiogenesis. Metastatic breast cell lines derived from African American and Caucasian patients were assayed to demonstrate alterations in the transcription of the identified biomarkers. Total RNA was isolated from tissue and cell lines. The steady state levels of mRNAs were measured by RT-PCR analysis. An aliquot ...
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Matrix metalloproteases (MMPs) are a collection of enzymes capable of cleaving extracellular matrix components, growth factors, and cell-surface receptors. MMPs modulate most aspects of tumorigenesis and are highly expressed in cancer compared with normal tissues. Preclinical studies have demonstrat …
Sigma-Aldrich offers abstracts and full-text articles by [Samuel B Adams, Lori A Setton, Richard D Bell, Mark E Easley, Janet L Huebner, Thomas Stabler, Virginia B Kraus, Elizabeth M Leimer, Steven A Olson, Dana L Nettles].
Matrix metalloproteinases (MMPs) are now acknowledged as key players in the regulation of both cell-cell and cell-extracellular matrix interactions. They are involved in modifying matrix structure, growth factor availability and the function of cell surface signalling systems, with consequent effects on cellular differentiation, proliferation and apoptosis. They play central roles in morphogenesis, wound healing, tissue repair and remodelling in response to injury and in the progression of diseases such as arthritis, cancer and cardiovascular disease. Because of their wide spectrum of activities and expression sites, the elucidation of their potential as drug targets in disease or as important features of the repair process will be dependent upon careful analysis of their role in different cellular locations and at different disease stages. Novel approaches to the specific regulation of individual MMPs in different contexts are also being developed.
Background VEGF proteolysis by plasmin or matrix metalloproteinases (MMPs) is believed to play an important role in regulating vascular patterning in vivo by releasing VEGF from the extracellular matrix (ECM). However, a quantitative understanding of the kinetics of VEGF cleavage and the efficiency of cell-mediated VEGF release is currently lacking. To address these uncertainties, we develop a molecular-detailed quantitative model of VEGF proteolysis, used here in the context of an endothelial sprout. Methodology and Findings To study a cells ability to cleave VEGF, the model captures MMP secretion, VEGF-ECM binding, VEGF proteolysis from VEGF165 to VEGF114 (the expected MMP cleavage product of VEGF165) and VEGF receptor-mediated recapture. Using experimental data, we estimated the effective bimolecular rate constant of VEGF165 cleavage by plasmin to be 328 M−1s−1 at 25°C, which is relatively slow compared to typical MMP-ECM proteolysis reactions. While previous studies have implicated cellular
IntroductionThe tissue inhibitors of metalloproteinases (TIMPs) are naturally occurring proteins that specifically inhibit matrix metalloproteinases…
Substrate cleavage by metalloproteinases involves nucleophilic attack on the scissile peptide bond by a water molecule that is polarized by a catalytic metal, usually a zinc ion, and a general base, usually the carboxyl group of a glutamic acid side chain
Matrix metalloproteinases (MMPs) are a family of Zinc- dependent endopeptidases that degrade extracellular matrix proteins. MMP-9 serum is quantitated using an ELISA (Enzyme Linked Immunosorbent Assay) procedure. It is a two-step sandwich-type immunoassay using two antibodies to MMP-9 Learn more.
Increased inflammation delays wound healing in mice deficient in collagenase-2 (MMP-8).: Matrix metalloproteinases (MMPs) have been implicated in numerous tissu
Matrix metalloproteinases (MMPs) have been identified as biomarkers for cancer, offering prognostic potential; however, non-invasive detection protocols are currently lacking. Herein, we describe the synthesis of a DOTA-containing peptide sequence that can be radiolabelled easily with 68Gallium or can be incorporat
This gene belongs to the TIMP gene family. The proteins encoded by this gene family are inhibitors of the matrix metalloproteinases, a group of peptidases involved in deg
Vranka, Janice A., "The characterization of gelatinase inhibition and the involvement of the matrix metalloproteinases and their inhibitors in glaucoma and a retinal degeneration" (1997). Scholar Archive. 2639 ...
CD147 Antigens: A widely distributed cell surface transmembrane glycoprotein that stimulates the synthesis of MATRIX METALLOPROTEINASES. It is found at high levels on the surface of malignant NEOPLASMS and may play a role as a mediator of malignant cell behavior.
J:105134 Perez SE, Cano DA, Dao-Pick T, Rougier JP, Werb Z, Hebrok M, Matrix metalloproteinases 2 and 9 are dispensable for pancreatic islet formation and function in vivo. Diabetes. 2005 Mar;54(3):694-701 ...
Cell-permeable. A broad spectrum matrix metalloprotease (MMP) inhibitor with Ki values of 0.4 nM, 0.5 nM, 27 nM, 3.7 nM, 0.1 nM, 0.2 nM, 3.6 nM, 13.4 nM, 0.36 nM for MMPs
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