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Volumn 61, Issue 6, 2013, Pages 444-461

Tissue- and cell-specific co-localization of intracellular gelatinolytic activity and matrix metalloproteinase

Author keywords

Gelatinolytic activity; Homeostasis; Intracellular; MMP 2

Indexed keywords

EDETIC ACID; GELATIN; GELATINASE A; METALLOPROTEINASE INHIBITOR; N [N (3 CARBOXYOXIRANE 2 CARBONYL)LEUCYL]AGMATINE;

EID: 84879473301     PISSN: 00221554     EISSN: None     Source Type: Journal    
DOI: 10.1369/0022155413484765     Document Type: Article
Times cited : (16)

References (45)
  • 2
    • 84861856192 scopus 로고    scopus 로고
    • Cardiac sarcomeric proteins: Novel intracellular targets of matrix metalloproteinase-2 in heart disease
    • Ali M.A., Fan X, Schulz R. 2011. Cardiac sarcomeric proteins: novel intracellular targets of matrix metalloproteinase-2 in heart disease. Trends Cardiovasc Med. 21:112-118.
    • (2011) Trends Cardiovasc Med. , vol.21 , pp. 112-118
    • Ali, M.A.1    Fan, X.2    Schulz, R.3
  • 3
    • 0037013250 scopus 로고    scopus 로고
    • Substrate binding of gelatinase B induces its enzymatic activity in the presence of intact propeptide
    • Bannikov G.A., Karelina TV, Collier IE, Marmer BL, Goldberg GI. 2002. Substrate binding of gelatinase B induces its enzymatic activity in the presence of intact propeptide. J BiolChem. 277:16022-16027.
    • (2002) J BiolChem. , vol.277 , pp. 16022-16027
    • Bannikov, G.A.1    Karelina, T.V.2    Collier, I.E.3    Marmer, B.L.4    Goldberg, G.I.5
  • 4
    • 0028276441 scopus 로고
    • A simple technique for preservation of fixation-sensitive antigens in paraffin-embedded tissues
    • Beckstead JH. 1994. A simple technique for preservation of fixation-sensitive antigens in paraffin-embedded tissues. J HistochemCytochem. 42:1127-1134.
    • (1994) J HistochemCytochem. , vol.42 , pp. 1127-1134
    • Beckstead, J.H.1
  • 5
    • 72749114050 scopus 로고    scopus 로고
    • Updated biological roles for matrix metalloproteinases and new "intracellular" substrates revealed by degradomics
    • Butler G.S., Overall CM. 2009. Updated biological roles for matrix metalloproteinases and new "intracellular" substrates revealed by degradomics. Biochemistry. 48:10830-10845.
    • (2009) Biochemistry. , vol.48 , pp. 10830-10845
    • Butler, G.S.1    Overall, C.M.2
  • 6
    • 77956784544 scopus 로고    scopus 로고
    • Intracellular substrate cleavage: A novel dimension in the biochemistry, biology and pathology of matrix metalloproteinases
    • Cauwe B., Opdenakker G. 2010. Intracellular substrate cleavage: a novel dimension in the biochemistry, biology and pathology of matrix metalloproteinases. Crit Rev Biochem Mol Biol. 45:351-423.
    • (2010) Crit Rev Biochem Mol Biol. , vol.45 , pp. 351-423
    • Cauwe, B.1    Opdenakker, G.2
  • 7
    • 63049095880 scopus 로고    scopus 로고
    • Live-cell imaging demonstrates extracellular matrix degradation in association with active cathepsin B in caveolae of endothelial cells during tube formation
    • Cavallo-Medved D, Rudy D, Blum G, Bogyo M, Caglic D, Sloane BF. 2009. Live-cell imaging demonstrates extracellular matrix degradation in association with active cathepsin B in caveolae of endothelial cells during tube formation. Exp Cell Res. 315:1234-1246.
    • (2009) Exp Cell Res. , vol.315 , pp. 1234-1246
    • Cavallo-Medved, D.1    Rudy, D.2    Blum, G.3    Bogyo, M.4    Caglic, D.5    Sloane, B.F.6
  • 8
    • 0031937107 scopus 로고    scopus 로고
    • Phagocytosis of cross-linked gelatin matrix by human breast carcinoma cells correlates with their invasive capacity
    • Coopman P.J., Do MT, Thompson EW, Mueller SC. 1998. Phagocytosis of cross-linked gelatin matrix by human breast carcinoma cells correlates with their invasive capacity. Clin Cancer Res. 4:507-515.
    • (1998) Clin Cancer Res. , vol.4 , pp. 507-515
    • Coopman, P.J.1    Do, M.T.2    Thompson, E.W.3    Mueller, S.C.4
  • 9
    • 38049174649 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinases-2 binding to membrane-type 1 matrix metalloproteinase induces MAPK activation and cell growth by a non-proteolytic mechanism
    • D'Alessio S, Ferrari G, Cinnante K, Scheerer W, Galloway AC, Roses D.F., Rozanov DV, Remacle AG, Oh ES, Shiryaev SA, et al. 2008. Tissue inhibitor of metalloproteinases-2 binding to membrane-type 1 matrix metalloproteinase induces MAPK activation and cell growth by a non-proteolytic mechanism. J Biol Chem. 283:87-99.
    • (2008) J Biol Chem. , vol.283 , pp. 87-99
    • D'Alessio, S.1    Ferrari, G.2    Cinnante, K.3    Scheerer, W.4    Galloway, A.C.5    Roses, D.F.6    Rozanov, D.V.7    Remacle, A.G.8    Oh, E.S.9    Shiryaev, S.A.10
  • 11
    • 78649734507 scopus 로고    scopus 로고
    • MT1-MMP regulates VEGF-A expression through a complex with VEGFR-2 and Src
    • Eisenach P.A., Roghi C, Fogarasi M, Murphy G, English WR. 2010. MT1-MMP regulates VEGF-A expression through a complex with VEGFR-2 and Src. J Cell Sci. 123:4182-4193.
    • (2010) J Cell Sci. , vol.123 , pp. 4182-4193
    • Eisenach, P.A.1    Roghi, C.2    Fogarasi, M.3    Murphy, G.4    English, W.R.5
  • 12
    • 3042703295 scopus 로고    scopus 로고
    • Three small integrin binding ligand N-linked glycoproteins (SIBLINGs) bind and activate specific matrix metalloproteinases
    • Fedarko N.S., Jain A, Karadag A, Fisher LW. 2004. Three small integrin binding ligand N-linked glycoproteins (SIBLINGs) bind and activate specific matrix metalloproteinases. FASEB J. 18:734-736.
    • (2004) FASEB J. , vol.18 , pp. 734-736
    • Fedarko, N.S.1    Jain, A.2    Karadag, A.3    Fisher, L.W.4
  • 13
    • 70449720597 scopus 로고    scopus 로고
    • The alpha 2 chain of collagen type VI sequesters latent proforms of matrix-metalloproteinases and modulates their activation and activity
    • Freise C., Erben U, Muche M, Farndale R, Zeitz M, Somasundaram R, Ruehl M. 2009. The alpha 2 chain of collagen type VI sequesters latent proforms of matrix-metalloproteinases and modulates their activation and activity. Matrix Biol. 28:480-489.
    • (2009) Matrix Biol. , vol.28 , pp. 480-489
    • Freise, C.1    Erben, U.2    Muche, M.3    Farndale, R.4    Zeitz, M.5    Somasundaram, R.6    Ruehl, M.7
  • 14
    • 78650424066 scopus 로고    scopus 로고
    • Roles of matrix metalloproteinases in cancer progression and their pharmacological targeting 1
    • Gialeli C., Theocharis AD, Karamanos NK. 2011. Roles of matrix metalloproteinases in cancer progression and their pharmacological targeting 1. FEBS J. 278:16-27.
    • (2011) FEBS J. , vol.278 , pp. 16-27
    • Gialeli, C.1    Theocharis, A.D.2    Karamanos, N.K.3
  • 15
    • 0030758034 scopus 로고    scopus 로고
    • Urokinase plasminogen activator and gelatinases are associated with membrane vesicles shed by human HT1080 fibrosarcoma cells 2
    • Ginestra A., Monea S, Seghezzi G, Dolo V, Nagase H, Mignatti P, Vittorelli ML. 1997. Urokinase plasminogen activator and gelatinases are associated with membrane vesicles shed by human HT1080 fibrosarcoma cells 2. J Biol Chem. 272:17216-17222.
    • (1997) J Biol Chem. , vol.272 , pp. 17216-17222
    • Ginestra, A.1    Monea, S.2    Seghezzi, G.3    Dolo, V.4    Nagase, H.5    Mignatti, P.6    Vittorelli, M.L.7
  • 20
    • 0036191352 scopus 로고    scopus 로고
    • Serum is a rich source of ligands for the scavenger receptor of hepatic sinusoidal endothelial cells
    • Hansen B., Melkko J, Smedsrod B. 2002. Serum is a rich source of ligands for the scavenger receptor of hepatic sinusoidal endothelial cells. Mol Cell Biochem. 229:63-72.
    • (2002) Mol Cell Biochem. , vol.229 , pp. 63-72
    • Hansen, B.1    Melkko, J.2    Smedsrod, B.3
  • 21
    • 84864770380 scopus 로고    scopus 로고
    • Intranuclear matrix metalloproteinases promote DNA damage and apoptosis induced by oxygen-glucose deprivation in neurons
    • Hill J.W., Poddar R, Thompson JF, Rosenberg GA, Yang Y. 2012. Intranuclear matrix metalloproteinases promote DNA damage and apoptosis induced by oxygen-glucose deprivation in neurons. Neuroscience. 220:277-290.
    • (2012) Neuroscience. , vol.220 , pp. 277-290
    • Hill, J.W.1    Poddar, R.2    Thompson, J.F.3    Rosenberg, G.A.4    Yang, Y.5
  • 22
    • 33947152499 scopus 로고    scopus 로고
    • Atypical localization of membrane type 1-matrix metalloproteinase in the nucleus is associated with aggressive features of hepatocellular carcinoma
    • Ip Y.C., Cheung ST, Fan ST. 2007. Atypical localization of membrane type 1-matrix metalloproteinase in the nucleus is associated with aggressive features of hepatocellular carcinoma. Mol Carcinog. 46:225-230.
    • (2007) Mol Carcinog. , vol.46 , pp. 225-230
    • Ip, Y.C.1    Cheung, S.T.2    Fan, S.T.3
  • 23
    • 52249098010 scopus 로고    scopus 로고
    • Structural requirements for bone sialoprotein binding and modulation of matrix metalloproteinase-2
    • Jain A., Karadag A, Fisher LW, Fedarko NS. 2008. Structural requirements for bone sialoprotein binding and modulation of matrix metalloproteinase-2. Biochemistry. 47:10162-10170.
    • (2008) Biochemistry. , vol.47 , pp. 10162-10170
    • Jain, A.1    Karadag, A.2    Fisher, L.W.3    Fedarko, N.S.4
  • 24
    • 0031846148 scopus 로고    scopus 로고
    • Differential regulation of MMP-2 and MMP-9 gelatinases in cultured human keratinocytes
    • Kobayashi T., Hattori S, Nagai Y, Tajima S, Nishikawa T. 1998. Differential regulation of MMP-2 and MMP-9 gelatinases in cultured human keratinocytes. Dermatology. 197:1-5.
    • (1998) Dermatology. , vol.197 , pp. 1-5
    • Kobayashi, T.1    Hattori, S.2    Nagai, Y.3    Tajima, S.4    Nishikawa, T.5
  • 25
    • 84863300391 scopus 로고    scopus 로고
    • Dimerization of matrix metalloproteinase-2 (MMP-2): Functional implication in MMP-2 activation
    • Koo B.H., Kim YH, Han JH, Kim DS. 2012. Dimerization of matrix metalloproteinase-2 (MMP-2): functional implication in MMP-2 activation. J Biol Chem. 287:22643-22653.
    • (2012) J Biol Chem. , vol.287 , pp. 22643-22653
    • Koo, B.H.1    Kim, Y.H.2    Han, J.H.3    Kim, D.S.4
  • 26
    • 3042745695 scopus 로고    scopus 로고
    • Matrix metalloproteinase-2 (MMP-2) is present in the nucleus of cardiac myocytes and is capable of cleaving poly (ADP-ribose) polymerase (PARP) in vitro
    • Kwan J.A., Schulze CJ, Wang W, Leon H, Sariahmetoglu M, Sung M, Sawicka J, Sims DE, Sawicki G, Schulz R. 2004. Matrix metalloproteinase-2 (MMP-2) is present in the nucleus of cardiac myocytes and is capable of cleaving poly (ADP-ribose) polymerase (PARP) in vitro. FASEB J. 18:690-692.
    • (2004) FASEB J. , vol.18 , pp. 690-692
    • Kwan, J.A.1    Schulze, C.J.2    Wang, W.3    Leon, H.4    Sariahmetoglu, M.5    Sung, M.6    Sawicka, J.7    Sims, D.E.8    Sawicki, G.9    Schulz, R.10
  • 27
    • 84859229746 scopus 로고    scopus 로고
    • A novel intracellular isoform of matrix metalloproteinase-2 induced by oxidative stress activates innate immunity
    • Lovett D.H., Mahimkar R, Raffai RL, Cape L, Maklashina E, Cecchini G., Karliner JS. 2012. A novel intracellular isoform of matrix metalloproteinase-2 induced by oxidative stress activates innate immunity. PloS One. 7:e34177.
    • (2012) PloS One. , vol.7
    • Lovett, D.H.1    Mahimkar, R.2    Raffai, R.L.3    Cape, L.4    Maklashina, E.5    Cecchini, G.6    Karliner, J.S.7
  • 28
    • 46649089205 scopus 로고    scopus 로고
    • Interaction of pro-matrix metalloproteinase-9/proteoglycan heteromer with gelatin and collagen
    • Malla N., Berg E, Uhlin-Hansen L, Winberg JO. 2008. Interaction of pro-matrix metalloproteinase-9/proteoglycan heteromer with gelatin and collagen. J Biol Chem. 283:13652-13665.
    • (2008) J Biol Chem. , vol.283 , pp. 13652-13665
    • Malla, N.1    Berg, E.2    Uhlin-Hansen, L.3    Winberg, J.O.4
  • 30
    • 70349283085 scopus 로고    scopus 로고
    • Self-organization of engineered epithelial tubules by differential cellular motility
    • Mori H., Gjorevski N, Inman JL, Bissell MJ, Nelson CM. 2009. Self-organization of engineered epithelial tubules by differential cellular motility. Proc Natl Acad Sci U S A. 106:14890-14895.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 14890-14895
    • Mori, H.1    Gjorevski, N.2    Inman, J.L.3    Bissell, M.J.4    Nelson, C.M.5
  • 31
    • 82755189495 scopus 로고    scopus 로고
    • Calpains: An elaborate proteolytic system
    • Ono Y., Sorimachi H. 2012. Calpains: an elaborate proteolytic system. Biochim Biophys Acta. 1824:224-236.
    • (2012) Biochim Biophys Acta. , vol.1824 , pp. 224-236
    • Ono, Y.1    Sorimachi, H.2
  • 32
    • 2642546699 scopus 로고    scopus 로고
    • Processing, shedding, and endocytosis of membrane type 1-matrix metalloproteinase (MT1-MMP)
    • Osenkowski P., Toth M, Fridman R. 2004. Processing, shedding, and endocytosis of membrane type 1-matrix metalloproteinase (MT1-MMP). J Cell Physiol. 200:2-10.
    • (2004) J Cell Physiol. , vol.200 , pp. 2-10
    • Osenkowski, P.1    Toth, M.2    Fridman, R.3
  • 33
    • 60749132264 scopus 로고    scopus 로고
    • Nuclear localization of active matrix metalloproteinase-2 in cigarette smoke-exposed apoptotic endothelial cells
    • Ruta A., Mark B, Edward B, Jawaharlal P, Jianliang Z. 2009. Nuclear localization of active matrix metalloproteinase-2 in cigarette smoke-exposed apoptotic endothelial cells. Exp Lung Res. 35:59-75.
    • (2009) Exp Lung Res. , vol.35 , pp. 59-75
    • Ruta, A.1    Mark, B.2    Edward, B.3    Jawaharlal, P.4    Jianliang, Z.5
  • 35
    • 77149171184 scopus 로고    scopus 로고
    • Structural and functional bases for allosteric control of MMP activities: Can it pave the path for selective inhibition?
    • Sela-Passwell N, Rosenblum G, Shoham T, Sagi I. 2010. Structural and functional bases for allosteric control of MMP activities: can it pave the path for selective inhibition? Biochim Biophys Acta. 1803:29-38.
    • (2010) Biochim Biophys Acta. , vol.1803 , pp. 29-38
    • Sela-Passwell, N.1    Rosenblum, G.2    Shoham, T.3    Sagi, I.4
  • 36
    • 34548820960 scopus 로고    scopus 로고
    • Matrix metalloproteinase-2 degrades the cytoskeletal protein alpha-actinin in peroxynitrite mediated myocardial injury
    • Sung M.M., Schulz CG, Wang W, Sawicki G, Bautista-Lopez NL, Schulz R. 2007. Matrix metalloproteinase-2 degrades the cytoskeletal protein alpha-actinin in peroxynitrite mediated myocardial injury. J Mol Cell Cardiol. 43:429-436.
    • (2007) J Mol Cell Cardiol. , vol.43 , pp. 429-436
    • Sung, M.M.1    Schulz, C.G.2    Wang, W.3    Sawicki, G.4    Bautista-Lopez, N.L.5    Schulz, R.6
  • 37
    • 0036172425 scopus 로고    scopus 로고
    • Shedding of the matrix metalloproteinases MMP-2, MMP-9, and MT1-MMP as membrane vesicle-associated components by endothelial cells
    • Taraboletti G., D'Ascenzo S, Borsotti P, Giavazzi R, Pavan A, Dolo V. 2002. Shedding of the matrix metalloproteinases MMP-2, MMP-9, and MT1-MMP as membrane vesicle-associated components by endothelial cells. Am J Pathol. 160:673-680.
    • (2002) Am J Pathol. , vol.160 , pp. 673-680
    • Taraboletti, G.1    D'Ascenzo, S.2    Borsotti, P.3    Giavazzi, R.4    Pavan, A.5    Dolo, V.6
  • 38
    • 0017236298 scopus 로고
    • The role of fibroblasts in the remodeling of periodontal ligament during physiologic tooth movement
    • Ten Cate AR, Deporter DA, Freeman E. 1976. The role of fibroblasts in the remodeling of periodontal ligament during physiologic tooth movement. Am J Orthod. 69:155-168.
    • (1976) Am J Orthod. , vol.69 , pp. 155-168
    • ten Cate, A.R.1    Deporter, D.A.2    Freeman, E.3
  • 40
    • 0029098293 scopus 로고
    • Cytokines modulate phagocytosis and intracellular digestion of collagen fibrils by fibroblasts in rabbit periosteal explants: Inverse effects on procollagenase production and collagen phagocytosis
    • van der Zee E, Everts V, Hoeben K, Beertsen W. 1995. Cytokines modulate phagocytosis and intracellular digestion of collagen fibrils by fibroblasts in rabbit periosteal explants: inverse effects on procollagenase production and collagen phagocytosis. J Cell Sci. 108:3307-3315.
    • (1995) J Cell Sci. , vol.108 , pp. 3307-3315
    • van der Zee, E.1    Everts, V.2    Hoeben, K.3    Beertsen, W.4
  • 42
    • 35848947186 scopus 로고    scopus 로고
    • Cysteine cathepsin non-inhibitory binding partners: Modulating intracellular trafficking and function
    • Victor B.C., Sloane BF. 2007. Cysteine cathepsin non-inhibitory binding partners: modulating intracellular trafficking and function. Biol Chem. 388:1131-1140.
    • (2007) Biol Chem. , vol.388 , pp. 1131-1140
    • Victor, B.C.1    Sloane, B.F.2
  • 43
  • 44
    • 0037693895 scopus 로고    scopus 로고
    • Matrix metalloproteinases and tissue inhibitors of metalloproteinases: Structure, function, and biochemistry
    • Visse R., Nagase H. 2003. Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry. Circ Res. 92:827-839.
    • (2003) Circ Res. , vol.92 , pp. 827-839
    • Visse, R.1    Nagase, H.2
  • 45
    • 71649085421 scopus 로고    scopus 로고
    • Increased intranuclear matrix metalloproteinase activity in neurons interferes with oxidative DNA repair in focal cerebral ischemia
    • Yang Y., Candelario-Jalil E, Thompson JF, Cuadrado E, Estrada EY, Rosell A, Montaner J, Rosenberg GA. 2010. Increased intranuclear matrix metalloproteinase activity in neurons interferes with oxidative DNA repair in focal cerebral ischemia. J Neurochem. 112:134-149. Downloaded from jhc. sagepub. com by Michiel Schotten on June 25, 2013
    • (2010) J Neurochem , vol.112 , pp. 134-149
    • Yang, Y.1    Candelario-Jalil, E.2    Thompson, J.F.3    Cuadrado, E.4    Estrada, E.Y.5    Rosell, A.6    Montaner, J.7    Rosenberg, G.A.8


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