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Volumn 223, Issue 1, 2010, Pages 260-269

Regulation of ATPase activity of transglutaminase 2 by MT1-MMP: Implications for mineralization of MC3T3-E1 osteoblast cultures

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; MATRIX METALLOPROTEINASE 14; PHOSPHATE; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE 2;

EID: 75749134894     PISSN: 00219541     EISSN: 10974652     Source Type: Journal    
DOI: 10.1002/jcp.22034     Document Type: Article
Times cited : (23)

References (93)
  • 1
    • 0023644524 scopus 로고
    • Identification of a guanosine triphosphate-binding site on guinea pig liver transglutaminase. Role of GTP and calcium ions in modulating activity
    • Achyuthan KE, Greenberg CS. 1987. Identification of a guanosine triphosphate-binding site on guinea pig liver transglutaminase. Role of GTP and calcium ions in modulating activity. J Biol Chem 262:1901-1906.
    • (1987) J Biol Chem , vol.262 , pp. 1901-1906
    • Achyuthan, K.E.1    Greenberg, C.S.2
  • 2
    • 34447538396 scopus 로고    scopus 로고
    • Pyrophosphate inhibits mineralization of osteoblast cultures by binding tomineral, up-regulating osteopontin, and inhibiting alkaline phosphatase activity
    • Addison WN, Azari F, Sorensen ES, Kaartinen MT, McKee MD. 2007. Pyrophosphate inhibits mineralization of osteoblast cultures by binding tomineral, up-regulating osteopontin, and inhibiting alkaline phosphatase activity. J Biol Chem 282:15872-15883.
    • (2007) J Biol Chem , vol.282 , pp. 15872-15883
    • Addison, W.N.1    Azari, F.2    Sorensen, E.S.3    Kaartinen, M.T.4    McKee, M.D.5
  • 3
    • 21244446693 scopus 로고    scopus 로고
    • Proteolysis of cell-surface tissue transglutaminase by matrix metalloproteinase-2 contributes to the adhesive defect andmatrix abnormalities in thrombospondin-2-null fibroblasts and mice
    • Agah A, Kyriakides TR, Bornstein P. 2005. Proteolysis of cell-surface tissue transglutaminase by matrix metalloproteinase-2 contributes to the adhesive defect andmatrix abnormalities in thrombospondin-2-null fibroblasts and mice. Am J Pathol 167:81-88.
    • (2005) Am J Pathol , vol.167 , pp. 81-88
    • Agah, A.1    Kyriakides, T.R.2    Bornstein, P.3
  • 4
    • 33645396457 scopus 로고    scopus 로고
    • Transglutaminase activity regulates osteoblast differentiation and matrix mineralization in MC3T3-E1 osteoblast cultures
    • Al-Jallad HF, Nakano Y, Chen JL, McMillan E, Lefebvre C, Kaartinen MT. 2006. Transglutaminase activity regulates osteoblast differentiation and matrix mineralization in MC3T3-E1 osteoblast cultures. Matrix Biol 25:135-148.
    • (2006) Matrix Biol , vol.25 , pp. 135-148
    • Al-Jallad, H.F.1    Nakano, Y.2    Chen, J.L.3    McMillan, E.4    Lefebvre, C.5    Kaartinen, M.T.6
  • 5
    • 34547906086 scopus 로고    scopus 로고
    • The role of matrix vesicles in physiological and pathological calcification
    • Anderson HC. 2007. The role of matrix vesicles in physiological and pathological calcification. Curr Opin Orthop 18:428-433.
    • (2007) Curr Opin Orthop , vol.18 , pp. 428-433
    • Anderson, H.C.1
  • 6
    • 0030696783 scopus 로고    scopus 로고
    • Matrix vesicles in osteomalacic hypophosphatasia bone contain apatite-like mineral crystals
    • Anderson HC, Hsu HH, Morris DC, Fedde KN, Whyte MP. 1997. Matrix vesicles in osteomalacic hypophosphatasia bone contain apatite-like mineral crystals. Am J Pathol 151:1555-1561.
    • (1997) Am J Pathol , vol.151 , pp. 1555-1561
    • Anderson, H.C.1    Hsu, H.H.2    Morris, D.C.3    Fedde, K.N.4    Whyte, M.P.5
  • 7
    • 1242316272 scopus 로고    scopus 로고
    • Impaired calcification around matrix vesicles of growth plate and bone in alkaline phosphatase-deficient mice
    • Anderson HC, Sipe JB, Hessle L, Dhanyamraju R, Atti E, Camacho NP, Millan JL. 2004. Impaired calcification around matrix vesicles of growth plate and bone in alkaline phosphatase-deficient mice. Am J Pathol 164:841-847.
    • (2004) Am J Pathol , vol.164 , pp. 841-847
    • Anderson, H.C.1    Sipe, J.B.2    Hessle, L.3    Dhanyamraju, R.4    Atti, E.5    Camacho, N.P.6    Millan, J.L.7
  • 8
    • 1942442183 scopus 로고    scopus 로고
    • Stromal cell-derived factor-1a promotes melanoma cell invasion across basement membranes involving stimulation of membrane-type 1 matrix metalloproteinase and rho GTPase activities
    • Bartolome RA, Galvez BG, Longo N, Baleux F, van Muijen GNP, Sanchez-Mateos P, Arroyo AG, Teixido J. 2004. Stromal cell-derived factor-1a promotes melanoma cell invasion across basement membranes involving stimulation of membrane-type 1 matrix metalloproteinase and rho GTPase activities. Cancer Res 64:2534-2543.
    • (2004) Cancer Res , vol.64 , pp. 2534-2543
    • Bartolome, R.A.1    Galvez, B.G.2    Longo, N.3    Baleux, F.4    van Muijen, G.N.P.5    Sanchez-Mateos, P.6    Arroyo, A.G.7    Teixido, J.8
  • 9
    • 0033278045 scopus 로고    scopus 로고
    • Root development in mice lacking functional tissue non-specific alkaline phosphatase gene: Inhibition of acellular cementum formation
    • Beertsen W, Vanden Bos T, Everts V. 1999. Root development in mice lacking functional tissue non-specific alkaline phosphatase gene: inhibition of acellular cementum formation. J Dent Res 78:1221-1229.
    • (1999) J Dent Res , vol.78 , pp. 1221-1229
    • Beertsen, W.1    Vanden Bos, T.2    Everts, V.3
  • 11
    • 33744950386 scopus 로고    scopus 로고
    • Mutation of a critical arginine in the GTP-binding site of transglutaminase 2 disinhibits intracellular crosslinking activity
    • Begg GE, Holman SR, Stokes PH, Matthews JM, Graham RM, Iismaa SE. 2006b. Mutation of a critical arginine in the GTP-binding site of transglutaminase 2 disinhibits intracellular crosslinking activity. J Biol Chem 281:12603-12609.
    • (2006) J Biol Chem , vol.281 , pp. 12603-12609
    • Begg, G.E.1    Holman, S.R.2    Stokes, P.H.3    Matthews, J.M.4    Graham, R.M.5    Iismaa, S.E.6
  • 12
    • 0035947675 scopus 로고    scopus 로고
    • Matrixdependent proteolysis of surface transglutaminase by membrane-type metalloproteinase regulates cancer cell adhesion and locomotion
    • Belkin AM, Akimov SS, Zaritskaya LS, Ratnikov BI, Deryugina EI, Strongin AY. 2001. Matrixdependent proteolysis of surface transglutaminase by membrane-type metalloproteinase regulates cancer cell adhesion and locomotion. J Biol Chem 276:18415-18422.
    • (2001) J Biol Chem , vol.276 , pp. 18415-18422
    • Belkin, A.M.1    Akimov, S.S.2    Zaritskaya, L.S.3    Ratnikov, B.I.4    Deryugina, E.I.5    Strongin, A.Y.6
  • 14
    • 0026559372 scopus 로고
    • Inorganic phosphate added exogenously or released from beta-glycerophosphate initiates mineralization of osteoid nodules in vitro
    • Bellows CG, Heersche JN, Aubin JE. 1992. Inorganic phosphate added exogenously or released from beta-glycerophosphate initiates mineralization of osteoid nodules in vitro. Bone Miner 17:15-29.
    • (1992) Bone Miner , vol.17 , pp. 15-29
    • Bellows, C.G.1    Heersche, J.N.2    Aubin, J.E.3
  • 15
    • 0023733194 scopus 로고
    • GTP modulates calcium binding and cation-induced conformational changes in erythrocyte transglutaminase
    • Bergamini CM. 1988. GTP modulates calcium binding and cation-induced conformational changes in erythrocyte transglutaminase. FEBS Lett 239:255-258.
    • (1988) FEBS Lett , vol.239 , pp. 255-258
    • Bergamini, C.M.1
  • 16
    • 0027405469 scopus 로고
    • Studies on tissue transglutaminases: Interaction of erythrocyte type-2 transglutaminase with GTP
    • Bergamini CM, Signorini M. 1993. Studies on tissue transglutaminases: interaction of erythrocyte type-2 transglutaminase with GTP. Biochem J 291:37-39.
    • (1993) Biochem J , vol.291 , pp. 37-39
    • Bergamini, C.M.1    Signorini, M.2
  • 17
    • 0014132665 scopus 로고
    • Fine structure of early cartilage calcification
    • Bonucci E. 1967. Fine structure of early cartilage calcification. J Ultrastruct Res 20:33-50.
    • (1967) J Ultrastruct Res , vol.20 , pp. 33-50
    • Bonucci, E.1
  • 18
    • 0026523307 scopus 로고
    • Extracellular alkaline phosphatase activity in mineralizing matrices of cartilage and bone: Ultrastructural localization using a ceriumbased method
    • Bonucci E, Silvestrini G, Bianco P. 1992. Extracellular alkaline phosphatase activity in mineralizing matrices of cartilage and bone: ultrastructural localization using a ceriumbased method. Histochemistry 97:323-327.
    • (1992) Histochemistry , vol.97 , pp. 323-327
    • Bonucci, E.1    Silvestrini, G.2    Bianco, P.3
  • 20
    • 0021020015 scopus 로고
    • Pyrophosphate, phosphate ion interaction: Effects on calcium pyrophosphate and calcium hydroxyapatite crystal formation in aqueous solutions
    • Cheng PT, Pritzker KP. 1983. Pyrophosphate, phosphate ion interaction: effects on calcium pyrophosphate and calcium hydroxyapatite crystal formation in aqueous solutions. J Rheumatol 10:769-777.
    • (1983) J Rheumatol , vol.10 , pp. 769-777
    • Cheng, P.T.1    Pritzker, K.P.2
  • 21
    • 42049108832 scopus 로고    scopus 로고
    • Extracellular transglutaminase 2 activates [beta]-catenin signaling in calcifying vascular smooth muscle cells
    • Faverman L, Mikhaylova L, Malmquist J, Nurminskaya M. 2008. Extracellular transglutaminase 2 activates [beta]-catenin signaling in calcifying vascular smooth muscle cells. FEBS Lett 582:1552-1557.
    • (2008) FEBS Lett , vol.582 , pp. 1552-1557
    • Faverman, L.1    Mikhaylova, L.2    Malmquist, J.3    Nurminskaya, M.4
  • 23
    • 0033791732 scopus 로고    scopus 로고
    • The expression ofmetalloproteinase-2, -9, and -14 and of tissue inhibitors-1 and -2 is developmentally modulated during osteogenesis;1; in vitro, the mature osteoblastic phenotype expressing metalloproteinase-14
    • Filanti C, Dickson GR, Di Martino D, Ulivi V, Sanguineti C, Romano P, Palermo C, Manduca P. 2000. The expression ofmetalloproteinase-2, -9, and -14 and of tissue inhibitors-1 and -2 is developmentally modulated during osteogenesis;1; in vitro, the mature osteoblastic phenotype expressing metalloproteinase-14. J Bone Miner Res 15:2154-2168.
    • (2000) J Bone Miner Res , vol.15 , pp. 2154-2168
    • Filanti, C.1    Dickson, G.R.2    Di Martino, D.3    Ulivi, V.4    Sanguineti, C.5    Romano, P.6    Palermo, C.7    Manduca, P.8
  • 24
    • 0037064589 scopus 로고    scopus 로고
    • ECM regulates MT1-MMP localization with beta1 or alphavbeta3 integrins at distinct cell compartments modulating its internalization and activity on human endothelial cells
    • Galvez BG, Matias-Roman S, Yanez-Mo M, Sanchez-Madrid F, Arroyo AG. 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 159:509-521.
    • (2002) J Cell Biol , vol.159 , pp. 509-521
    • Galvez, B.G.1    Matias-Roman, S.2    Yanez-Mo, M.3    Sanchez-Madrid, F.4    Arroyo, A.G.5
  • 25
    • 33749363239 scopus 로고    scopus 로고
    • Nature of phosphate substrate as a major determinant of mineral type formed in matrix vesicle-mediated in vitro mineralization: An FTIR imaging study
    • Garimella R, Bi X, Anderson HC, Camacho NP. 2006. Nature of phosphate substrate as a major determinant of mineral type formed in matrix vesicle-mediated in vitro mineralization: an FTIR imaging study. Bone 38:811-817.
    • (2006) Bone , vol.38 , pp. 811-817
    • Garimella, R.1    Bi, X.2    Anderson, H.C.3    Camacho, N.P.4
  • 27
    • 0031885056 scopus 로고    scopus 로고
    • Ectophosphodiesterase/pyrophosphatase of lymphocytes and non-lymphoid cells: Structure and function of the PC-1 family
    • Goding JW, Terkeltaub R, Maurice M, Deterre P, Sali A, Belli SI. 1998. Ectophosphodiesterase/pyrophosphatase of lymphocytes and non-lymphoid cells: structure and function of the PC-1 family. Immunol Rev 161:11-26.
    • (1998) Immunol Rev , vol.161 , pp. 11-26
    • Goding, J.W.1    Terkeltaub, R.2    Maurice, M.3    Deterre, P.4    Sali, A.5    Belli, S.I.6
  • 28
    • 0021733794 scopus 로고
    • Hereditary joint disorder in progressive ankylosis (ank/ank) mice. I. Association of calcium hydroxyapatite deposition with inflammatory arthropathy
    • Hakim FT, Cranley R, Brown KS, Eanes ED, Harne L, Oppenheim JJ. 1984. Hereditary joint disorder in progressive ankylosis (ank/ank) mice. I. Association of calcium hydroxyapatite deposition with inflammatory arthropathy. Arthritis Rheum 27:1411-1420.
    • (1984) Arthritis Rheum , vol.27 , pp. 1411-1420
    • Hakim, F.T.1    Cranley, R.2    Brown, K.S.3    Eanes, E.D.4    Harne, L.5    Oppenheim, J.J.6
  • 29
    • 17644417961 scopus 로고    scopus 로고
    • Transglutaminase contributes to CPPD crystal formation in osteoarthritis
    • Heinkel D, Gohr CM, Uzuki M, Rosenthal AK. 2004. Transglutaminase contributes to CPPD crystal formation in osteoarthritis. Front Biosci 9:3257-3261.
    • (2004) Front Biosci , vol.9 , pp. 3257-3261
    • Heinkel, D.1    Gohr, C.M.2    Uzuki, M.3    Rosenthal, A.K.4
  • 30
  • 31
    • 0034647482 scopus 로고    scopus 로고
    • Role of the mouse ank gene in control of tissue calcification and arthritis
    • Ho AM, Johnson MD, Kingsley DM. 2000. Role of the mouse ank gene in control of tissue calcification and arthritis. Science 289:265-270.
    • (2000) Science , vol.289 , pp. 265-270
    • Ho, A.M.1    Johnson, M.D.2    Kingsley, D.M.3
  • 34
    • 0034674770 scopus 로고    scopus 로고
    • GTP binding and signaling by Gh/transglutaminase II involves distinct residues in a unique GTP-binding pocket
    • Iismaa SE, Wu MJ, Nanda N, Church WB, Graham RM. 2000.GTP binding and signaling by Gh/transglutaminase II involves distinct residues in a unique GTP-binding pocket. J Biol Chem 275:18259-18265.
    • (2000) J Biol Chem , vol.275 , pp. 18259-18265
    • Iismaa, S.E.1    Wu, M.J.2    Nanda, N.3    Church, W.B.4    Graham, R.M.5
  • 35
    • 67651071286 scopus 로고    scopus 로고
    • Transglutaminases and disease: Lessons from genetically engineered mouse models and inherited disorders
    • Iismaa SE, Mearns BM, Lorand L, Graham RM. 2009. Transglutaminases and disease: lessons from genetically engineered mouse models and inherited disorders. Physiol Rev 89:991-1023.
    • (2009) Physiol Rev , vol.89 , pp. 991-1023
    • Iismaa, S.E.1    Mearns, B.M.2    Lorand, L.3    Graham, R.M.4
  • 36
    • 0025065288 scopus 로고
    • A novel guanine nucleotide-binding protein coupled to the alpha 1-adrenergic receptor. I. Identification by photolabeling or membrane and ternary complex preparation
    • Im MJ, Graham RM. 1990. A novel guanine nucleotide-binding protein coupled to the alpha 1-adrenergic receptor. I. Identification by photolabeling or membrane and ternary complex preparation. J Biol Chem 265:18944-18951.
    • (1990) J Biol Chem , vol.265 , pp. 18944-18951
    • Im, M.J.1    Graham, R.M.2
  • 37
    • 0030725001 scopus 로고    scopus 로고
    • Transglutaminase II: A new class of GTP-binding proteinwith new biological functions
    • Im MJ, Russell MA, Feng JF. 1997. Transglutaminase II: a new class of GTP-binding proteinwith new biological functions. Cell Signal 9:477-482.
    • (1997) Cell Signal , vol.9 , pp. 477-482
    • Im, M.J.1    Russell, M.A.2    Feng, J.F.3
  • 38
    • 0030010940 scopus 로고    scopus 로고
    • Membrane-type matrix metalloproteinase 1 is a gelatinolytic enzyme and is secreted in a complex with tissue inhibitor of metalloproteinases 2
    • Imai K, Ohuchi E, Aoki T, Nomura H, Fujii Y, Sato H, Seiki M, Okada Y. 1996. Membrane-type matrix metalloproteinase 1 is a gelatinolytic enzyme and is secreted in a complex with tissue inhibitor of metalloproteinases 2. Cancer Res 56:2707-2710.
    • (1996) Cancer Res , vol.56 , pp. 2707-2710
    • Imai, K.1    Ohuchi, E.2    Aoki, T.3    Nomura, H.4    Fujii, Y.5    Sato, H.6    Seiki, M.7    Okada, Y.8
  • 39
    • 17644372415 scopus 로고    scopus 로고
    • External GTP-bound transglutaminase 2 is a molecular switch for chondrocyte hypertrophic differentiation and calcification
    • Johnson KA, Terkeltaub RA. 2005. External GTP-bound transglutaminase 2 is a molecular switch for chondrocyte hypertrophic differentiation and calcification. J Biol Chem 280:15004-15012.
    • (2005) J Biol Chem , vol.280 , pp. 15004-15012
    • Johnson, K.A.1    Terkeltaub, R.A.2
  • 40
    • 0032983541 scopus 로고    scopus 로고
    • Matrix vesicle plasma cell membrane glycoprotein-1 regulates mineralization by murine osteoblastic MC3T3 cells
    • Johnson K, Moffa A, Chen Y, Pritzker K, Goding J, Terkeltaub R. 1999. Matrix vesicle plasma cell membrane glycoprotein-1 regulates mineralization by murine osteoblastic MC3T3 cells. J Bone Miner Res 14:883-892.
    • (1999) J Bone Miner Res , vol.14 , pp. 883-892
    • Johnson, K.1    Moffa, A.2    Chen, Y.3    Pritzker, K.4    Goding, J.5    Terkeltaub, R.6
  • 41
    • 48049093713 scopus 로고    scopus 로고
    • Factor XIIIA mobilizes transglutaminase 2 to induce chondrocyte hypertrophic differentiation
    • Johnson KA, Rose DM, Terkeltaub RA. 2008. Factor XIIIA mobilizes transglutaminase 2 to induce chondrocyte hypertrophic differentiation. J Cell Sci 121:2256-2264.
    • (2008) J Cell Sci , vol.121 , pp. 2256-2264
    • Johnson, K.A.1    Rose, D.M.2    Terkeltaub, R.A.3
  • 42
    • 0038820036 scopus 로고    scopus 로고
    • Distinct transglutaminase 2-independent and transglutaminase 2-dependent pathways mediate articular chondrocyte hypertrophy
    • Johnson KA, van Etten D, Nanda N, Graham RM, Terkeltaub RA. 2003. Distinct transglutaminase 2-independent and transglutaminase 2-dependent pathways mediate articular chondrocyte hypertrophy. J Biol Chem 278:18824-18832.
    • (2003) J Biol Chem , vol.278 , pp. 18824-18832
    • Johnson, K.A.1    van Etten, D.2    Nanda, N.3    Graham, R.M.4    Terkeltaub, R.A.5
  • 44
    • 23944448662 scopus 로고    scopus 로고
    • Transglutaminase crosslinking of SIBLING proteins in teeth
    • Kaartinen MT, Sun W, Kaipatur N, McKee MD. 2005. Transglutaminase crosslinking of SIBLING proteins in teeth. J Dent Res 84:607-612.
    • (2005) J Dent Res , vol.84 , pp. 607-612
    • Kaartinen, M.T.1    Sun, W.2    Kaipatur, N.3    McKee, M.D.4
  • 45
    • 33947598333 scopus 로고    scopus 로고
    • Osteopontin upregulation and polymerization by transglutaminase 2 in calcified arteries of Matrix Gla protein-deficient mice
    • Kaartinen MT, Murshed M, Karsenty G, McKee MD. 2007. Osteopontin upregulation and polymerization by transglutaminase 2 in calcified arteries of Matrix Gla protein-deficient mice. J Histochem Cytochem 55:375-386.
    • (2007) J Histochem Cytochem , vol.55 , pp. 375-386
    • Kaartinen, M.T.1    Murshed, M.2    Karsenty, G.3    McKee, M.D.4
  • 46
    • 33646703312 scopus 로고    scopus 로고
    • Determinants of pathological mineralization
    • Kirsch T. 2006. Determinants of pathological mineralization. Curr Opin Rheumatol 18:174-180.
    • (2006) Curr Opin Rheumatol , vol.18 , pp. 174-180
    • Kirsch, T.1
  • 47
    • 34547907393 scopus 로고    scopus 로고
    • Physiological and pathological mineralization: A complex multifactorial process
    • Kirsch T. 2007. Physiological and pathological mineralization: a complex multifactorial process. Curr Opin Orthop 18:425-427.
    • (2007) Curr Opin Orthop , vol.18 , pp. 425-427
    • Kirsch, T.1
  • 49
    • 0029856983 scopus 로고    scopus 로고
    • C-terminal deletion of human tissue transglutaminase enhances magnesium-dependent GTP/ATPase activity
    • Lai TS, Slaughter TF, Koropchak CM, Haroon ZA, Greenberg CS. 1996. C-terminal deletion of human tissue transglutaminase enhances magnesium-dependent GTP/ATPase activity. J Biol Chem 271:31191-31195.
    • (1996) J Biol Chem , vol.271 , pp. 31191-31195
    • Lai, T.S.1    Slaughter, T.F.2    Koropchak, C.M.3    Haroon, Z.A.4    Greenberg, C.S.5
  • 50
    • 0031890194 scopus 로고    scopus 로고
    • Regulation of human tissue transglutaminase function by magnesium-nucleotide complexes. Identification of distinct binding sites for Mg-GTP and Mg-ATP
    • Lai TS, Slaughter TF, Peoples KA, Hettasch JM, Greenberg CS. 1998. Regulation of human tissue transglutaminase function by magnesium-nucleotide complexes. Identification of distinct binding sites for Mg-GTP and Mg-ATP. J Biol Chem 273:1776-1781.
    • (1998) J Biol Chem , vol.273 , pp. 1776-1781
    • Lai, T.S.1    Slaughter, T.F.2    Peoples, K.A.3    Hettasch, J.M.4    Greenberg, C.S.5
  • 52
    • 0034685778 scopus 로고    scopus 로고
    • Regulation ofmembrane-type-1 matrix metalloproteinase activity by its cytoplasmic domain
    • Lehti K, Valtanen H, Wickstrom SA, Lohi J, Keski-Oja J. 2000. Regulation ofmembrane-type-1 matrix metalloproteinase activity by its cytoplasmic domain. J Biol Chem 275:15006-15013.
    • (2000) J Biol Chem , vol.275 , pp. 15006-15013
    • Lehti, K.1    Valtanen, H.2    Wickstrom, S.A.3    Lohi, J.4    Keski-Oja, J.5
  • 53
    • 0037022619 scopus 로고    scopus 로고
    • Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity
    • Liu S, Cerione RA, Clardy J. 2002. Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity. Proc Natl Acad Sci USA 99:2743-2747.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 2743-2747
    • Liu, S.1    Cerione, R.A.2    Clardy, J.3
  • 54
    • 0037317032 scopus 로고    scopus 로고
    • Transglutaminases: Crosslinking enzymes with pleiotropic functions
    • Lorand L, Graham RM. 2003. Transglutaminases: crosslinking enzymes with pleiotropic functions. Nat Rev Mol Cell Biol 4:140-156.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 140-156
    • Lorand, L.1    Graham, R.M.2
  • 56
    • 0015176398 scopus 로고
    • Phosphatases of epiphyseal cartilage studied by electron microscopic cytochemical methods
    • Matsuzawa T, Anderson HC. 1971. Phosphatases of epiphyseal cartilage studied by electron microscopic cytochemical methods. J Histochem Cytochem 19:801-808.
    • (1971) J Histochem Cytochem , vol.19 , pp. 801-808
    • Matsuzawa, T.1    Anderson, H.C.2
  • 57
    • 33646007642 scopus 로고    scopus 로고
    • Hierarchies of extracellular matrix and mineral organization in bone of the craniofacial complex and skeleton
    • McKee MD, Addison WN, Kaartinen MT. 2005. Hierarchies of extracellular matrix and mineral organization in bone of the craniofacial complex and skeleton. Cells Tissues Organs 181:176-188.
    • (2005) Cells Tissues Organs , vol.181 , pp. 176-188
    • McKee, M.D.1    Addison, W.N.2    Kaartinen, M.T.3
  • 58
    • 0034783355 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinases during ascorbate-induced differentiation of osteoblastic MC3T3-E1 cells
    • Mizutani A, Sugiyama I, Kuno E, Matsunaga S, Tsukagoshi N. 2001. Expression of matrix metalloproteinases during ascorbate-induced differentiation of osteoblastic MC3T3-E1 cells. J Bone Miner Res 16:2043-2049.
    • (2001) J Bone Miner Res , vol.16 , pp. 2043-2049
    • Mizutani, A.1    Sugiyama, I.2    Kuno, E.3    Matsunaga, S.4    Tsukagoshi, N.5
  • 60
    • 18244392685 scopus 로고    scopus 로고
    • Unique coexpression in osteoblasts of broadly expressed genes accounts for the spatial restriction of ECM mineralization to bone
    • Murshed M, Harmey D, Millan JL, McKee MD, Karsenty G. 2005. Unique coexpression in osteoblasts of broadly expressed genes accounts for the spatial restriction of ECM mineralization to bone. Genes Dev 19:1093-1104.
    • (2005) Genes Dev , vol.19 , pp. 1093-1104
    • Murshed, M.1    Harmey, D.2    Millan, J.L.3    McKee, M.D.4    Karsenty, G.5
  • 61
    • 34548525045 scopus 로고    scopus 로고
    • ATP-mediated mineralization of MC3T3-E1 osteoblast cultures
    • Nakano Y, Addison WN, Kaartinen MT. 2007a. ATP-mediated mineralization of MC3T3-E1 osteoblast cultures. Bone 41:549-561.
    • (2007) Bone , vol.41 , pp. 549-561
    • Nakano, Y.1    Addison, W.N.2    Kaartinen, M.T.3
  • 62
    • 34250816844 scopus 로고    scopus 로고
    • Expression and localization of plasma transglutaminase factor XIIIA in bone
    • Nakano Y, Al-Jallad HF, Mousa A, Kaartinen MT. 2007b. Expression and localization of plasma transglutaminase factor XIIIA in bone. J Histochem Cytochem 55:675-685.
    • (2007) J Histochem Cytochem , vol.55 , pp. 675-685
    • Nakano, Y.1    Al-Jallad, H.F.2    Mousa, A.3    Kaartinen, M.T.4
  • 63
    • 1842409589 scopus 로고    scopus 로고
    • Inactivation of two mouse alkaline phosphatase genes and establishment of a model of infantile hypophosphatasia
    • Narisawa S, Frohlander N, Millan JL. 1997. Inactivation of two mouse alkaline phosphatase genes and establishment of a model of infantile hypophosphatasia. Dev Dyn 208:432-446.
    • (1997) Dev Dyn , vol.208 , pp. 432-446
    • Narisawa, S.1    Frohlander, N.2    Millan, J.L.3
  • 64
    • 32844467767 scopus 로고    scopus 로고
    • Transglutaminases in mineralized tissues
    • Nurminskaya M, Kaartinen MT. 2006. Transglutaminases in mineralized tissues. Front Biosci 11:1591-1606.
    • (2006) Front Biosci , vol.11 , pp. 1591-1606
    • Nurminskaya, M.1    Kaartinen, M.T.2
  • 65
    • 0036235139 scopus 로고    scopus 로고
    • Immunohistological analysis of transglutaminase factor XIIIA expression in mouse embryonic growth plate
    • Nurminskaya MV, Linsenmayer TF. 2002. Immunohistological analysis of transglutaminase factor XIIIA expression in mouse embryonic growth plate. J Orthop Res 20:575-578.
    • (2002) J Orthop Res , vol.20 , pp. 575-578
    • Nurminskaya, M.V.1    Linsenmayer, T.F.2
  • 66
    • 0142106382 scopus 로고    scopus 로고
    • Chondrocyte-derived transglutaminase promotes maturation of preosteoblasts in periosteal bone
    • Nurminskaya M, Magee C, Faverman L, Linsenmayer TF. 2003. Chondrocyte-derived transglutaminase promotes maturation of preosteoblasts in periosteal bone. Dev Biol 263:139-152.
    • (2003) Dev Biol , vol.263 , pp. 139-152
    • Nurminskaya, M.1    Magee, C.2    Faverman, L.3    Linsenmayer, T.F.4
  • 67
    • 62949175253 scopus 로고    scopus 로고
    • Transglutaminase-2 differently regulates cartilage destruction and osteophyte formation in a surgical model of osteoarthritis
    • Orlandi A, Oliva F, Taurisano G, Candi E, Di Lascio A, Melino G, Spagnoli LG, Tarantino U. 2009. Transglutaminase-2 differently regulates cartilage destruction and osteophyte formation in a surgical model of osteoarthritis. Amino Acids 36:755-763.
    • (2009) Amino Acids , vol.36 , pp. 755-763
    • Orlandi, A.1    Oliva, F.2    Taurisano, G.3    Candi, E.4    Di Lascio, A.5    Melino, G.6    Spagnoli, L.G.7    Tarantino, U.8
  • 68
    • 0033605561 scopus 로고    scopus 로고
    • Identification and characterization of the fifth membrane-type matrix metalloproteinase MT5-MMP
    • Pei D. 1999a. Identification and characterization of the fifth membrane-type matrix metalloproteinase MT5-MMP. J Biol Chem 274:8925-8932.
    • (1999) J Biol Chem , vol.274 , pp. 8925-8932
    • Pei, D.1
  • 69
    • 0033256294 scopus 로고    scopus 로고
    • Leukolysin/MMP25/MT6-MMP: A novel matrix metalloproteinase specifically expressed in the leukocyte lineage
    • Pei D. 1999b. Leukolysin/MMP25/MT6-MMP: a novel matrix metalloproteinase specifically expressed in the leukocyte lineage. Cell Res 9:291-303.
    • (1999) Cell Res , vol.9 , pp. 291-303
    • Pei, D.1
  • 70
    • 38549156658 scopus 로고    scopus 로고
    • Transglutaminase 2 undergoes a large conformational change upon activation
    • Pinkas DM, Strop P, Brunger AT, Khosla C. 2007. Transglutaminase 2 undergoes a large conformational change upon activation. PLoS Biol 5:e327.
    • (2007) PLoS Biol , vol.5
    • Pinkas, D.M.1    Strop, P.2    Brunger, A.T.3    Khosla, C.4
  • 71
    • 0030022539 scopus 로고    scopus 로고
    • Molecular cloning of a novel membrane-type matrix metalloproteinase from a human breast carcinoma
    • Puente XS, Pendas AM, Llano E, Velasco G, Lopez-Otin C. 1996. Molecular cloning of a novel membrane-type matrix metalloproteinase from a human breast carcinoma. Cancer Res 56:944-949.
    • (1996) Cancer Res , vol.56 , pp. 944-949
    • Puente, X.S.1    Pendas, A.M.2    Llano, E.3    Velasco, G.4    Lopez-Otin, C.5
  • 73
    • 0036056980 scopus 로고    scopus 로고
    • MT1-MMP-dependent and -independent regulation of gelatinase A activation in long-term, ascorbate-treated fibroblast cultures: Regulation by fibrillar collagen
    • Ruangpanit N, Price JT, Holmbeck K, Birkedal-Hansen H, Guenzler V, Huang X, Chan D, Bateman JF, Thompson EW. 2002. MT1-MMP-dependent and -independent regulation of gelatinase A activation in long-term, ascorbate-treated fibroblast cultures: regulation by fibrillar collagen. Exp Cell Res 272:109-118.
    • (2002) Exp Cell Res , vol.272 , pp. 109-118
    • Ruangpanit, N.1    Price, J.T.2    Holmbeck, K.3    Birkedal-Hansen, H.4    Guenzler, V.5    Huang, X.6    Chan, D.7    Bateman, J.F.8    Thompson, E.W.9
  • 74
  • 75
    • 0033003771 scopus 로고    scopus 로고
    • Membrane-type matrix metalloproteinases
    • Seiki M. 1999. Membrane-type matrix metalloproteinases. APMIS 107:137-143.
    • (1999) APMIS , vol.107 , pp. 137-143
    • Seiki, M.1
  • 76
    • 0020411707 scopus 로고
    • A biochemical study of alkaline phosphatase isolated from rabbit incisor dentine
    • Smith AJ. 1982. A biochemical study of alkaline phosphatase isolated from rabbit incisor dentine. Arch Oral Biol 27:1081-1086.
    • (1982) Arch Oral Biol , vol.27 , pp. 1081-1086
    • Smith, A.J.1
  • 77
    • 0030020239 scopus 로고    scopus 로고
    • Expression of the nucleoside triphosphate pyrophosphohydrolase PC-1 is induced by basic fibroblast growth factor (bFGF) and modulated by activation of the protein kinase A and C pathways in osteoblastlike osteosarcoma cells
    • Solan JL, Deftos LJ, Goding JW, Terkeltaub RA. 1996. Expression of the nucleoside triphosphate pyrophosphohydrolase PC-1 is induced by basic fibroblast growth factor (bFGF) and modulated by activation of the protein kinase A and C pathways in osteoblastlike osteosarcoma cells. J Bone Miner Res 11:183-192.
    • (1996) J Bone Miner Res , vol.11 , pp. 183-192
    • Solan, J.L.1    Deftos, L.J.2    Goding, J.W.3    Terkeltaub, R.A.4
  • 78
    • 0026754093 scopus 로고
    • Putative nucleotide binding sites of guinea pig liver transglutaminase
    • Takeuchi Y, Birckbichler PJ, Patterson MK Jr, Lee KN. 1992. Putative nucleotide binding sites of guinea pig liver transglutaminase. FEBS Lett 307:177-180.
    • (1992) FEBS Lett , vol.307 , pp. 177-180
    • Takeuchi, Y.1    Birckbichler, P.J.2    Patterson Jr, M.K.3    Lee, K.N.4
  • 79
    • 0028465517 scopus 로고
    • Calmodulin regulates nucleotide hydrolysis activity of tissue transglutaminase
    • Takeuchi Y, Birckbichler PJ, Patterson MKJr, Lee KN, Carter HA. 1994. Calmodulin regulates nucleotide hydrolysis activity of tissue transglutaminase. Z Naturforsch [C] 49:453-457.
    • (1994) Z Naturforsch , vol.49 , Issue.C , pp. 453-457
    • Takeuchi, Y.1    Birckbichler, P.J.2    MKJr, P.3    Lee, K.N.4    Carter, H.A.5
  • 80
    • 0029118269 scopus 로고
    • Identification of the second membrane-type matrix metalloproteinase (MT-MMP-2) gene from a human placenta cDNA library. MTMMPs form a unique membrane-type subclass in the MMP family
    • Takino T, Sato H, Shinagawa A, Seiki M. 1995. Identification of the second membrane-type matrix metalloproteinase (MT-MMP-2) gene from a human placenta cDNA library. MTMMPs form a unique membrane-type subclass in the MMP family. J Biol Chem 270:23013-23020.
    • (1995) J Biol Chem , vol.270 , pp. 23013-23020
    • Takino, T.1    Sato, H.2    Shinagawa, A.3    Seiki, M.4
  • 81
    • 0037214203 scopus 로고    scopus 로고
    • Orientation of mineral crystallites and mineral density during skeletal development in mice deficient in tissue nonspecific alkaline phosphatase
    • Tesch W, Vandenbos T, Roschgr P, Fratzl-Zelman N, Klaushofer K, Beertsen W, Fratzl P. 2003. Orientation of mineral crystallites and mineral density during skeletal development in mice deficient in tissue nonspecific alkaline phosphatase. J Bone Miner Res 18:117-125.
    • (2003) J Bone Miner Res , vol.18 , pp. 117-125
    • Tesch, W.1    Vandenbos, T.2    Roschgr, P.3    Fratzl-Zelman, N.4    Klaushofer, K.5    Beertsen, W.6    Fratzl, P.7
  • 82
    • 57349140279 scopus 로고    scopus 로고
    • Inorganic pyrophosphate as a regulator of hydroxyapatite or calcium pyrophosphate dihydrate mineral deposition bymatrix vesicles
    • Thouverey C, Bechkoff G, Pikula S, Buchet R. 2009. Inorganic pyrophosphate as a regulator of hydroxyapatite or calcium pyrophosphate dihydrate mineral deposition bymatrix vesicles. Osteoarthritis Cartilage 17:64-72.
    • (2009) Osteoarthritis Cartilage , vol.17 , pp. 64-72
    • Thouverey, C.1    Bechkoff, G.2    Pikula, S.3    Buchet, R.4
  • 85
    • 0035823493 scopus 로고    scopus 로고
    • Alterations in the sensing and transport of phosphate and calcium by differentiating chondrocytes
    • Wang D, Canaff L, Davidson D, Corluka A, Liu H, Hendy GN, Henderson JE. 2001. Alterations in the sensing and transport of phosphate and calcium by differentiating chondrocytes. J Biol Chem 276:33995-34005.
    • (2001) J Biol Chem , vol.276 , pp. 33995-34005
    • Wang, D.1    Canaff, L.2    Davidson, D.3    Corluka, A.4    Liu, H.5    Hendy, G.N.6    Henderson, J.E.7
  • 86
    • 0032983542 scopus 로고    scopus 로고
    • Isolation and characterization of MC3T3-E1 preosteoblast subclones with distinct in vitro and in vivo differentiation/mineralization potential
    • Wang D, Christensen K, Chawla K, Xiao G, Krebsbach PH, Franceschi RT. 1999. Isolation and characterization of MC3T3-E1 preosteoblast subclones with distinct in vitro and in vivo differentiation/mineralization potential. J Bone Miner Res 14:893-903.
    • (1999) J Bone Miner Res , vol.14 , pp. 893-903
    • Wang, D.1    Christensen, K.2    Chawla, K.3    Xiao, G.4    Krebsbach, P.H.5    Franceschi, R.T.6
  • 87
    • 0024389607 scopus 로고
    • Cytochemical properties of osteoblast cell membrane domains
    • Watson LP, Kang YH, Falk MC. 1989. Cytochemical properties of osteoblast cell membrane domains. J Histochem Cytochem 37:1235-1246.
    • (1989) J Histochem Cytochem , vol.37 , pp. 1235-1246
    • Watson, L.P.1    Kang, Y.H.2    Falk, M.C.3
  • 88
    • 0029115393 scopus 로고
    • Mice lacking tissue non-specific alkaline phosphatase die from seizures due to defective metabolism of vitamin B-6
    • Waymire KG, Mahuren JD, Jaje JM, Guilarte TR, Coburn SP, MacGregor GR. 1995. Mice lacking tissue non-specific alkaline phosphatase die from seizures due to defective metabolism of vitamin B-6. Nat Genet 11:45-51.
    • (1995) Nat Genet , vol.11 , pp. 45-51
    • Waymire, K.G.1    Mahuren, J.D.2    Jaje, J.M.3    Guilarte, T.R.4    Coburn, S.P.5    MacGregor, G.R.6
  • 89
    • 0027930471 scopus 로고
    • Hypophosphatasia and the role of alkaline phosphatase in skeletal mineralization
    • Whyte MP. 1994. Hypophosphatasia and the role of alkaline phosphatase in skeletal mineralization. Endocr Rev 15:439-461.
    • (1994) Endocr Rev , vol.15 , pp. 439-461
    • Whyte, M.P.1
  • 90
    • 0028914274 scopus 로고
    • Alkaline phosphatase: Placental and tissue-nonspecific isoenzymes hydrolyze phosphoethanolamine, inorganic pyrophosphate, and pyridoxal 50-phosphate. Substrate accumulation in carriers of hypophosphatasia corrects during pregnancy
    • Whyte MP, Landt M, Ryan LM, Mulivor RA, Henthorn PS, Fedde KN, Mahuren JD, Coburn SP. 1995. Alkaline phosphatase: placental and tissue-nonspecific isoenzymes hydrolyze phosphoethanolamine, inorganic pyrophosphate, and pyridoxal 50-phosphate. Substrate accumulation in carriers of hypophosphatasia corrects during pregnancy. J Clin Invest 95:1440-1445.
    • (1995) J Clin Invest , vol.95 , pp. 1440-1445
    • Whyte, M.P.1    Landt, M.2    Ryan, L.M.3    Mulivor, R.A.4    Henthorn, P.S.5    Fedde, K.N.6    Mahuren, J.D.7    Coburn, S.P.8
  • 91
    • 0029133344 scopus 로고
    • cDNA sequence and mRNA tissue distribution of a novel human matrix metalloproteinase with a potential transmembrane segment
    • Will H, Hinzmann B. 1995. cDNA sequence and mRNA tissue distribution of a novel human matrix metalloproteinase with a potential transmembrane segment. Eur J Biochem 231:602-608.
    • (1995) Eur J Biochem , vol.231 , pp. 602-608
    • Will, H.1    Hinzmann, B.2
  • 92
    • 34250197188 scopus 로고    scopus 로고
    • Osteoblast autonomous Pi regulation via Pit1 plays a role in bone mineralization
    • Yoshiko Y, Candeliere GA, Maeda N, Aubin JE. 2007. Osteoblast autonomous Pi regulation via Pit1 plays a role in bone mineralization. Mol Cell Biol 27:4465-4474.
    • (2007) Mol Cell Biol , vol.27 , pp. 4465-4474
    • Yoshiko, Y.1    Candeliere, G.A.2    Maeda, N.3    Aubin, J.E.4


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