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MT1-MMP collagenolytic activity is regulated through association with tetraspanin CD151 in primary endothelial cells.
Abstract
MT1-MMP plays a key role in endothelial function, as underscored by the angiogenic defects found in MT1-MMP deficient mice. We have studied the molecular interactions that underlie the functional regulation of MT1-MMP. At lateral endothelial cell junctions, MT1-MMP colocalizes with tetraspanin CD151 (Tspan 24) and its associated partner α3β1 integrin. Biochemical and FRET analyses show that MT1-MMP, through its hemopexin domain, associates tightly with CD151, thus forming α3β1 integrin/CD151/MT1-MMP ternary complexes. siRNA knockdown of HUVEC CD151 expression enhanced MT1-MMP-mediated activation of MMP2, and the same activation was seen in ex vivo lung endothelial cells isolated from CD151-deficient mice. However, analysis of collagen degradation in these experimental models revealed a diminished MT1-MMP enzymatic activity in confined areas around the cell periphery. CD151 knockdown affected both MT1-MMP subcellular localization and its inclusion into detergent-resistant membrane domains, and prevented biochemical association of the metalloproteinase with the integrin α3β1. These data provide evidence for a novel regulatory role of tetraspanin microdomains on the collagenolytic activity of MT1-MMP and indicate that CD151 is a key regulator of MT1-MMP in endothelial homeostasis.
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Exosites outside the catalytic core domain of MMPs are less conserved and contribute to substrate selection and binding.
“exosites that are regions outside the catalytic core domain of MMPs are less conserved and contribute to substrate selection and binding (27–29).”
From Identification of amino acid residues in the MT-loop of MT1-MMP critical for its ability to cleave low-density lipoprotein receptor (2022) · cites this paper as [28]
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Research works printed but not linked: 41
- Sabeh, 2004, Tumor cell traffic through the extracellular matrix is controlled by the membrane-anchored collagenase MT1-MMP., J Cell Biol, 167, 769, 10.1083/jcb.200408028 · DOI
- Holmbeck, 1999, MT1-MMP-deficient mice develop dwarfism, osteopenia, arthritis, and connective tissue disease due to inadequate collagen turnover., Cell, 99, 81, 10.1016/S0092-8674(00)80064-1 · DOI · Paper page
- Oh, 2004, Mutations in two matrix metalloproteinase genes, MMP-2 and MT1-MMP, are synthetic lethal in mice., Oncogene, 23, 5041, 10.1038/sj.onc.1207688 · DOI
- Osenkowski, 2004, Processing, shedding, and endocytosis of membrane type 1-matrix metalloproteinase (MT1-MMP)., J Cell Physiol, 200, 2, 10.1002/jcp.20064 · DOI
- Itoh, 2006, MT1-MMP: a potent modifier of pericellular microenvironment., J Cell Physiol, 206, 1, 10.1002/jcp.20431 · DOI
- Itoh, 2004, MT1-MMP: an enzyme with multidimensional regulation., Trends Biochem Sci, 29, 285, 10.1016/j.tibs.2004.04.001 · DOI
- Lehti, 1998, Proteolytic processing of membrane-type-1 matrix metalloproteinase is associated with gelatinase A activation at the cell surface., Biochem J, 334, 345, 10.1042/bj3340345 · DOI
- Lehti, 2002, Oligomerization through hemopexin and cytoplasmic domains regulates the activity and turnover of membrane-type 1 matrix metalloproteinase., J Biol Chem, 277, 8440, 10.1074/jbc.M109128200 · DOI
- Bravo-Cordero, 2007, MT1-MMP proinvasive activity is regulated by a novel Rab8-dependent exocytic pathway., EMBO J, 26, 1499, 10.1038/sj.emboj.7601606 · DOI
- Remacle, 2003, Membrane type I-matrix metalloproteinase (MT1-MMP) is internalised by two different pathways and is recycled to the cell surface., J Cell Sci, 116, 3905, 10.1242/jcs.00710 · DOI
- Galvez, 2004, Caveolae are a novel pathway for membrane-type 1 matrix metalloproteinase traffic in human endothelial cells., Mol Biol Cell, 15, 678, 10.1091/mbc.e03-07-0516 · DOI
- Rozanov, 2004, Aberrant, persistent inclusion into lipid rafts limits the tumorigenic function of membrane type-1 matrix metalloproteinase in malignant cells., Exp Cell Res, 293, 81, 10.1016/j.yexcr.2003.10.006 · DOI · Paper page
- Hemler, 2003, Tetraspanin proteins mediate cellular penetration, invasion, and fusion events and define a novel type of membrane microdomain., Annu Rev Cell Dev Biol, 19, 397, 10.1146/annurev.cellbio.19.111301.153609 · DOI
- Shiomi, 2005, Pericellular activation of proMMP-7 (promatrilysin-1) through interaction with CD151., Lab Invest, 85, 1489, 10.1038/labinvest.3700351 · DOI
- Takino, 2003, Tetraspanin CD63 promotes targeting and lysosomal proteolysis of membrane-type 1 matrix metalloproteinase., Biochem Biophys Res Commun, 304, 160, 10.1016/S0006-291X(03)00544-8 · DOI
- Yan, 2002, The metalloprotease Kuzbanian (ADAM10) mediates the transactivation of EGF receptor by G protein-coupled receptors., J Cell Biol, 158, 221, 10.1083/jcb.200112026 · DOI
- Andre, 2006, Proteomic analysis of the tetraspanin web using LC-ESI-MS/MS and MALDI-FTICR-MS., Proteomics, 6, 1437, 10.1002/pmic.200500180 · DOI
- Yáñez-Mó, 1998, Regulation of endothelial cell motility by complexes of tetraspan molecules CD81/TAPA-1 and CD151/PETA-3 with alpha3 beta1 integrin localized at endothelial lateral junctions., J Cell Biol, 141, 791, 10.1083/jcb.141.3.791 · DOI
- Karamatic Crew, 2004, CD151, the first member of the tetraspanin (TM4) superfamily detected on erythrocytes, is essential for the correct assembly of human basement membranes in kidney and skin., Blood, 104, 2217, 10.1182/blood-2004-04-1512 · DOI
- Wright, 2004, Characterization of mice lacking the tetraspanin superfamily member CD151., Mol Cell Biol, 24, 5978, 10.1128/MCB.24.13.5978-5988.2004 · DOI
- Sachs, 2006, Kidney failure in mice lacking the tetra-spanin CD151., J Cell Biol, 175, 33, 10.1083/jcb.200603073 · DOI
- Takeda, 2007, Deletion of tetraspanin CD151 results in decreased pathologic angiogenesis in vivo and in vitro., Blood, 109, 1524, 10.1182/blood-2006-08-041970 · DOI
- Oblander, 2005, Distinctive functions of membrane type 1 matrix-metalloprotease (MT1-MMP or MMP-14) in lung and submandibular gland development are independent of its role in pro-MMP-2 activation., Dev Biol, 277, 255, 10.1016/j.ydbio.2004.09.033 · DOI
- Galvez, 2001, Membrane type 1-matrix metalloproteinase is activated during migration of human endothelial cells and modulates endothelial motility and matrix remodeling., J Biol Chem, 276, 37491, 10.1074/jbc.M104094200 · DOI
- Lehti, 2000, Regulation of membrane-type-1 matrix metalloproteinase activity by its cytoplasmic domain., J Biol Chem, 275, 15006, 10.1074/jbc.M910220199 · DOI · Paper page
- Barreiro, 2002, Dynamic interaction of VCAM-1 and ICAM-1 with moesin and ezrin in a novel endothelial docking structure for adherent leukocytes., J Cell Biol, 157, 1233, 10.1083/jcb.200112126 · DOI
- Nishiuchi, 2005, Potentiation of the ligand-binding activity of integrin alpha3beta1 via association with tetraspanin CD151., Proc Natl Acad Sci U S A, 102, 1939, 10.1073/pnas.0409493102 · DOI
- Serru, 1999, Selective tetraspan-integrin complexes (CD81/alpha4beta1, CD151/alpha3beta1, CD151/alpha6beta1) under conditions disrupting tetraspan interactions., Biochem J, 340, 103, 10.1042/bj3400103 · DOI
- Uekita, 2001, Cytoplasmic tail-dependent internalization of membrane-type 1 matrix metalloproteinase is important for its invasion-promoting activity., J Cell Biol, 155, 1345, 10.1083/jcb.200108112 · DOI
- Barreiro, 2005, Endothelial tetraspanin microdomains regulate leukocyte firm adhesion during extravasation., Blood, 105, 2852, 10.1182/blood-2004-09-3606 · DOI
- Galvez, 2002, ECM regulates MT1-MMP localization with beta1 or alphavbeta3 integrins at distinct cell compartments modulating its internalization and activity on human endothelial cells., J Cell Biol, 159, 509, 10.1083/jcb.200205026 · DOI
- Claas, 2001, Evaluation of prototype transmembrane 4 superfamily protein complexes and their relation to lipid rafts., J Biol Chem, 276, 7974, 10.1074/jbc.M008650200 · DOI
- Odintsova, 2003, Tetraspanin CD82 regulates compartmentalisation and ligand-induced dimerization of EGFR., J Cell Sci, 116, 4557, 10.1242/jcs.00793 · DOI
- Sugiura, 1999, Function of alpha3beta1-tetraspanin protein complexes in tumor cell invasion: evidence for the role of the complexes in production of matrix metalloproteinase 2 (MMP-2)., J Cell Biol, 146, 1375, 10.1083/jcb.146.6.1375 · DOI
- Sincock, 1999, PETA-3/CD151, a member of the transmembrane 4 superfamily, is localised to the plasma membrane and endocytic system of endothelial cells, associates with multiple integrins and modulates cell function., J Cell Sci, 112, 833, 10.1242/jcs.112.6.833 · DOI
- Wang, 2004, Co-recycling of MT1-MMP and MT3-MMP through the trans-Golgi network: identification of DKV582 as a recycling signal., J Biol Chem, 279, 9331, 10.1074/jbc.M312369200 · DOI
- Charrin, 2002, Differential stability of tetraspanin/tetraspanin interactions: role of palmitoylation., FEBS Lett, 516, 139, 10.1016/S0014-5793(02)02522-X · DOI
- Anilkumar, 2005, Palmitoylation at Cys574 is essential for MT1-MMP to promote cell migration., FASEB J, 19, 1326, 10.1096/fj.04-3651fje · DOI
- Yamada, 2008, Probing the interaction of tetraspanin CD151 with integrin α3β1 using a panel of monoclonal antibodies with distinct reactivities toward the CD151-integrin α3β1 complex., Biochem J, 10.1042/BJ20071625 · DOI
- Kazes, 2000, Platelet release of trimolecular complex components MT1-MMP/TIMP2/MMP2: involvement in MMP2 activation and platelet aggregation., Blood, 96, 3064, 10.1182/blood.V96.9.3064 · DOI
- Takeda, 2003, Tetraspanins CD9 and CD81 function to prevent the fusion of mononuclear phagocytes., J Cell Biol, 161, 945, 10.1083/jcb.200212031 · DOI
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Metadata
- Authors
- Yañez-Mó, M., Barreiro, O., Gonzalo, P., Batista, A., Megías, D., Genís, L., Sachs, N., Sala-Valdés, M., Alonso, M. A., Montoya, M. C., Sonnenberg, A., Arroyo, A. G., & Sánchez-Madrid, F.
- Affiliations
- Servicio de Inmunología, Hospital de la Princesa, Universidad Autónoma de Madrid, Madrid, Spain;
- Centro Nacional de Investigaciones Cardiovasculares, Madrid, Spain;
- Centro de Biología Molecular Severo Ochoa, Universidad Autónoma de Madrid, Consejo Superior de Investigaciones Científicas, Madrid, Spain;
- Centro Nacional de Investigaciones Oncológicas, Madrid, Spain; and
- Division of Cell Biology, The Netherlands Cancer Institute, Amsterdam, The Netherlands
- Venue
- Blood
- Publisher
- American Society of Hematology
- Published
- 2008-10-15
- Volume
- 112
- Issue
- 8
- Pages
- 3217-3226
- ISSN
- 0006-4971
- 1528-0020
- Cited by
- 101
- References
- 0
- Language
- en
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