메뉴 건너뛰기




Volumn 42, Issue 2-3, 2012, Pages 939-949

TG2, a novel extracellular protein with multiple functions

Author keywords

Cell adhesion and crosslinking; Extracellular matrix; Tissue transglutaminase

Indexed keywords

ANTINEOPLASTIC AGENT; BETA INTEGRIN; CARMUSTINE; COLLAGEN TYPE 1; DIHYDROISOXAZOLE DERIVATIVE; ENZYME INHIBITOR; FIBRONECTIN; G PROTEIN COUPLED RECEPTOR; G PROTEIN COUPLED RECEPTOR 56; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; METALLOPROTEINASE; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE 2; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE 2 INHIBITOR; PROTEIN KINASE C ALPHA; PROTEOHEPARAN SULFATE; SMALL INTERFERING RNA; SYNDECAN 4; UNCLASSIFIED DRUG; AMIDE; CALCIUM; MATRIX METALLOPROTEINASE; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; TISSUE TRANSGLUTAMINASE 2, HUMAN;

EID: 84859632755     PISSN: 09394451     EISSN: 14382199     Source Type: Journal    
DOI: 10.1007/s00726-011-1008-x     Document Type: Review
Times cited : (92)

References (80)
  • 1
    • 0026612802 scopus 로고
    • Identification of Gln (726) in nidogen as the amine acceptor in transglutaminasecatalyzed cross-linking of laminin-nidogen complexes
    • Aeschlimann D, Paulsson M, Mann K (1992) Identification of Gln (726) in nidogen as the amine acceptor in transglutaminasecatalyzed cross-linking of laminin-nidogen complexes. J Biol Chem 267:11316-11321
    • (1992) J Biol Chem , vol.267 , pp. 11316-11321
    • Aeschlimann, D.1    Paulsson, M.2    Mann, K.3
  • 3
    • 0035469864 scopus 로고    scopus 로고
    • Cell surface tissue transglutaminase is involved in adhesion and migration of monocytic cells on fibronectin
    • Akimov SS, Belkin AM (2001) Cell surface tissue transglutaminase is involved in adhesion and migration of monocytic cells on fibronectin. Blood 98:1567-1576
    • (2001) Blood , vol.98 , pp. 1567-1576
    • Akimov, S.S.1    Belkin, A.M.2
  • 4
    • 0034695929 scopus 로고    scopus 로고
    • Tissue transglutaminase is an integrin-binding adhesion coreceptor for fibronectin
    • Akimov SS, Krylov D, Fleischman LF, Belkin AM (2000) Tissue transglutaminase is an integrin-binding adhesion coreceptor for fibronectin. J Cell Biol 148:825-838
    • (2000) J Cell Biol , vol.148 , pp. 825-838
    • Akimov, S.S.1    Krylov, D.2    Fleischman, L.F.3    Belkin, A.M.4
  • 5
    • 33645396457 scopus 로고    scopus 로고
    • Transglutaminase activity regulates osteoblast differentiation and matrix mineralization in MOT3-E1 osteoblast cultures
    • Al-Jallad HF, Nakano Y, Chen JL Y, McMillan E, Lefebvre C, Kaartinen MT (2006) Transglutaminase activity regulates osteoblast differentiation and matrix mineralization in MOT3-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.Y.3    McMillan, E.4    Lefebvre, C.5    Kaartinen, M.T.6
  • 6
    • 67650538098 scopus 로고    scopus 로고
    • Tissue transglutaminase is an essential participant in the epidermal growth factor-stimulated signaling pathway leading to cancer cell migration and invasion
    • Antonyak MA, Li B, Regan AD, Feng Q, Dusaban SS, Cerione RA (2009) Tissue transglutaminase is an essential participant in the epidermal growth factor-stimulated signaling pathway leading to cancer cell migration and invasion. J Biol Chem 284:17914-17925
    • (2009) J Biol Chem , vol.284 , pp. 17914-17925
    • Antonyak, M.A.1    Li, B.2    Regan, A.D.3    Feng, Q.4    Dusaban, S.S.5    Cerione, R.A.6
  • 7
    • 0037053359 scopus 로고    scopus 로고
    • Analysis of tissue transglutaminase function in the migration of Swiss 3T3 fibroblasts. The active-state conformation of the enzyme does not affect cell motility but is important for its secretion
    • DOI 10.1074/jbc.M109836200
    • Balklava Z, Verderio E, Collighan R, Gross S, Adams J, Griffin M (2002) Analysis of tissue transglutaminase function in the migration of Swiss 3T3 fibroblasts: the active-state conformation of the enzyme does not affect cell motility but is important for its secretion. J Biol Chem 277:16567-16575 (Pubitemid 34967673)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.19 , pp. 16567-16575
    • Balklava, Z.1    Verderio, E.2    Collighan, R.3    Gross, S.4    Adams, J.5    Griffin, M.6
  • 8
    • 0035947675 scopus 로고    scopus 로고
    • Matrix-dependent 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) Matrix-dependent 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
  • 9
    • 22544438722 scopus 로고    scopus 로고
    • The cellular response to transglutaminase-cross-linked collagen
    • DOI 10.1016/j.biomaterials.2005.04.017, PII S0142961205003273
    • Chau DYS, Collighan RJ, Verderio EAM, Addy VL, Griffin M (2005) The cellular response to transglutaminase-cross-linked collagen. Biomaterials 26:6518-6529 (Pubitemid 41021746)
    • (2005) Biomaterials , vol.26 , Issue.33 , pp. 6518-6529
    • Chau, D.Y.S.1    Collighan, R.J.2    Verderio, E.A.M.3    Addy, V.L.4    Griffin, M.5
  • 10
    • 78650255565 scopus 로고    scopus 로고
    • Up-regulation of fibronectin and tissue transglutaminase promotes cell invasion involving increased association with integrin and MMP expression in A431 cells
    • Chen SH, Lin CY, Lee LT, Chang GD, Lee PP, Hung CC, Kao WT, Tsai PH, Schally AV, Hwang JJ, Lee MT (2010) Up-regulation of fibronectin and tissue transglutaminase promotes cell invasion involving increased association with integrin and MMP expression in A431 cells. Anticancer Res 30:4177-4186
    • (2010) Anticancer Res , vol.30 , pp. 4177-4186
    • Chen, S.H.1    Lin, C.Y.2    Lee, L.T.3    Chang, G.D.4    Lee, P.P.5    Hung, C.C.6    Kao, W.T.7    Tsai, P.H.8    Schally, A.V.9    Hwang, J.J.10    Lee, M.T.11
  • 11
    • 62949217561 scopus 로고    scopus 로고
    • Transglutaminase 2 cross-linking of matrix proteins: Biological significance and medical applications
    • Collighan RJ, Griffin M (2009) Transglutaminase 2 cross-linking of matrix proteins: biological significance and medical applications. Amino Acids 36:659-670
    • (2009) Amino Acids , vol.36 , pp. 659-670
    • Collighan, R.J.1    Griffin, M.2
  • 12
    • 33747891469 scopus 로고    scopus 로고
    • Complex formation between tissue transglutaminase II (tTG) and vascular endothelial growth factor receptor 2 (VEGFR-2): Proposed mechanism for modulation of endothelial cell response to VEGF
    • DOI 10.1016/j.yexcr.2006.05.019, PII S0014482706001947
    • Dardik R, Inbal A (2006) Complex formation between tissue transglutaminase II (tTG) and vascular endothelial growth factor receptor 2 (VEGFR-2): proposed mechanism for modulation of endothelial cell response to VEGF. Exp Cell Res 312: 2973-2982 (Pubitemid 44292656)
    • (2006) Experimental Cell Research , vol.312 , Issue.16 , pp. 2973-2982
    • Dardik, R.1    Inbal, A.2
  • 13
    • 62949131510 scopus 로고    scopus 로고
    • Enhanced osteoblast adhesion on transglutaminase 2-crosslinked fibronectin
    • Forsprecher J, Wang Z, Nelea V, Kaartinen MT (2009) Enhanced osteoblast adhesion on transglutaminase 2-crosslinked fibronectin. Amino Acids 36:747-753
    • (2009) Amino Acids , vol.36 , pp. 747-753
    • Forsprecher, J.1    Wang, Z.2    Nelea, V.3    Kaartinen, M.T.4
  • 14
    • 0032747129 scopus 로고    scopus 로고
    • Cell surface localization of tissue transglutaminase is dependent on a fibronectin-binding site in its N-terminal betasandwich domain
    • Gaudry CA, Verderio E, Aeschlimann D, Cox A, Smith C, Griffin M (1999a) Cell surface localization of tissue transglutaminase is dependent on a fibronectin-binding site in its N-terminal betasandwich domain. J Biol Chem 274:30707-30714
    • (1999) J Biol Chem , vol.274 , pp. 30707-30714
    • Gaudry, C.A.1    Verderio, E.2    Aeschlimann, D.3    Cox, A.4    Smith, C.5    Griffin, M.6
  • 15
    • 0033544020 scopus 로고    scopus 로고
    • 1 integrin
    • DOI 10.1006/excr.1999.4633
    • Gaudry CA, Verderio E, Jones RA, Smith C, Griffin M (1999b) Tissue transglutaminase is an important player at the surface of human endothelial cells: evidence for its externalization and its colocalization with the beta(1) integrin. Exp Cell Res 252:104-113 (Pubitemid 29485130)
    • (1999) Experimental Cell Research , vol.252 , Issue.1 , pp. 104-113
    • Gaudry, C.A.1    Verderio, E.2    Jones, R.A.3    Smith, C.4    Griffin, M.5
  • 16
    • 0028332036 scopus 로고
    • Differential recognition of target genes by nuclear receptor monomers, dimers, and heterodimers
    • DOI 10.1210/er.15.3.391
    • Glass CK (1994) Differential recognition of target genes by nuclear receptor monomers, dimers, and heterodimers. Endocr Rev 15:391-407 (Pubitemid 24180795)
    • (1994) Endocrine Reviews , vol.15 , Issue.3 , pp. 391-407
    • Glass, C.K.1
  • 17
    • 0036901574 scopus 로고    scopus 로고
    • Transglutaminases: Nature's biological glues
    • DOI 10.1042/BJ20021234
    • Griffin M, Casadio R, Bergamini CM (2002) Transglutaminases: nature's biological glues. Biochem J 368:377-396 (Pubitemid 35454517)
    • (2002) Biochemical Journal , vol.368 , Issue.2 , pp. 377-396
    • Griffin, M.1    Casadio, R.2    Bergamini, C.M.3
  • 19
    • 77954143820 scopus 로고    scopus 로고
    • Crystal structure of human transglutaminase 2 in complex with adenosine triphosphate
    • Han BJ, Cho JW, Cho YD, Jeong CK, Kim SY, Lee BI (2010) Crystal structure of human transglutaminase 2 in complex with adenosine triphosphate. Int J Biol Macromol 47:190-195
    • (2010) Int J Biol Macromol , vol.47 , pp. 190-195
    • Han, B.J.1    Cho, J.W.2    Cho, Y.D.3    Jeong, C.K.4    Kim, S.Y.5    Lee, B.I.6
  • 20
    • 0022330157 scopus 로고
    • Activation of transglutaminase at calcium levels consistent with a role for this enzyme as a calcium receptor protein
    • Hand D, Bungay PJ, Elliott BM, Griffin M (1985) Activation of transglutaminase at calcium levels consistent with a role for this enzyme as a calcium receptor protein. Biosci Rep 5:1079-1086 (Pubitemid 16141515)
    • (1985) Bioscience Reports , vol.5 , Issue.12 , pp. 1079-1086
    • Hand, D.1    Bungay, P.J.2    Elliott, B.M.3    Griffin, M.4
  • 22
    • 0037086740 scopus 로고    scopus 로고
    • Involvement of tissue transglutaminase in the stabilisation of biomaterial/tissue interfaces important in medical devices
    • DOI 10.1016/S0142-9612(01)00282-4, PII S0142961201002824
    • Heath DJ, Christian P, Griffin M (2002) Involvement of tissue trans glutaminase in the stabilisation of biomaterial/tissue interfaces important in medical devices. Biomaterials 23:1519-1526 (Pubitemid 34037088)
    • (2002) Biomaterials , vol.23 , Issue.6 , pp. 1519-1526
    • Heath, D.J.1    Christian, P.2    Griffin, M.3
  • 23
    • 33646858986 scopus 로고    scopus 로고
    • Implications of increased tissue transglutaminase (TG2) expression in drug-resistant breast cancer (MCF-7) cells
    • DOI 10.1038/sj.onc.1209324, PII 1209324
    • Herman JF, Mangala LS, Mehta K (2006) Implications of increased tissue transglutaminase (TG2) expression in drug-resistant breast cancer (MCF-7) cells. Oncogene 25:3049-3058 (Pubitemid 43780469)
    • (2006) Oncogene , vol.25 , Issue.21 , pp. 3049-3058
    • Herman, J.F.1    Mangala, L.S.2    Mehta, K.3
  • 24
    • 38649137249 scopus 로고    scopus 로고
    • Characterization of GPR56 protein and its suppressed expression in human pancreatic cancer cells
    • DOI 10.1007/s11010-007-9621-4
    • Huang Y, Fan J, Yang J, Zhu GZ (2008) Characterization of GPR56 protein and its suppressed expression in human pancreatic cancer cells. Mol Cellular Biochem 308:133-139 (Pubitemid 351167854)
    • (2008) Molecular and Cellular Biochemistry , vol.308 , Issue.1-2 , pp. 133-139
    • Huang, Y.1    Fan, J.2    Yang, J.3    Zhu, G.-Z.4
  • 26
    • 78649497500 scopus 로고    scopus 로고
    • Do changes in transglutaminase activity alter latent transforming growth factor beta activation in experimental diabetic nephropathy?
    • Huang L, Haylor JL, Fisher M, Hau Z, El Nahas AM, Griffin M, Johnson TS (2010) Do changes in transglutaminase activity alter latent transforming growth factor beta activation in experimental diabetic nephropathy? Nephrol Dial Transplant 25:3897-3910
    • (2010) Nephrol Dial Transplant , vol.25 , pp. 3897-3910
    • Huang, L.1    Haylor, J.L.2    Fisher, M.3    Hau, Z.4    El Nahas, A.M.5    Griffin, M.6    Johnson, T.S.7
  • 27
    • 33745373374 scopus 로고    scopus 로고
    • Cell surface transglutaminase promotes RhoA activation via integrin clustering and suppression of the Src-p190RhoGAP signaling pathway
    • DOI 10.1091/mbc.E05-06-0549
    • Janiak A, Zemskov EA, Belkin AM (2006) Cell surface transglutaminase promotes RhoA activation via integrin clustering and suppression of the Src-p190RhoGAP signaling pathway. Mol Biol Cell 17:1606-1619 (Pubitemid 44017561)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.4 , pp. 1606-1619
    • Janiak, A.1    Zemskov, E.A.2    Belkin, A.M.3
  • 28
    • 17644372415 scopus 로고    scopus 로고
    • External GTP-bound transglutaminase 2 is a molecular switch for chondrocyte hypertrophic differentiation and calcification
    • DOI 10.1074/jbc.M500962200
    • Johnson KA, Terkeltaub R (2005) External GTP-bound transglutaminase 2 is a molecular switch for chondrocyte hypertrophic differentiation and calcification. J Biol Chem 280:15004-15012 (Pubitemid 40562853)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.15 , pp. 15004-15012
    • Johnson, K.A.1    Terkeltaub, R.A.2
  • 30
    • 33747060780 scopus 로고    scopus 로고
    • Matrix changes induced by transglutaminase 2 lead to inhibition of angiogenesis and tumor growth
    • DOI 10.1038/sj.cdd.4401816, PII 4401816
    • Jones RA, Kotsakis P, Johnson TS, Chau DY, Ali S, Melino G, Griffin M (2006) Matrix changes induced by transglutaminase 2 lead to inhibition of angiogenesis and tumor growth. Cell Death Differ 13:1442-1453 (Pubitemid 44210348)
    • (2006) Cell Death and Differentiation , vol.13 , Issue.9 , pp. 1442-1453
    • Jones, R.A.1    Kotsakis, P.2    Johnson, T.S.3    Chau, D.Y.S.4    Ali, S.5    Melino, G.6    Griffin, M.7
  • 31
    • 4344669555 scopus 로고    scopus 로고
    • h/transglutaminase 2 inhibits cell migration through interaction with cytoplasmic tail of integrin α subunits
    • DOI 10.1074/jbc.M402084200
    • Kang SK, Yi KS, Kwon NS, Park KH, Kim UH, Baek KJ, Im MJ (2004) Alpha(1B)-adrenoceptor signaling and cell motility - GTPase function of G(h)/transglutaminase 2 inhibits cell migration through interaction with cytoplasmic tail of integrin alpha subunits. J Biol Chem 279:36593-36600 (Pubitemid 39129003)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.35 , pp. 36593-36600
    • Kang, S.K.1    Yi, K.S.2    Kwon, N.S.3    Park, K.-H.4    Kim, U.-H.5    Baek, K.J.6    Im, M.-J.7
  • 33
  • 34
    • 0028973138 scopus 로고
    • Transglutaminase-catalyzed cross-linking of fibrils of collagen V/XI in A204 rhabdomyosarcoma cells
    • Kleman JP, Aeschlimann D, Paulsson M, van der Rest M (1995) Transglutaminase-catalyzed cross-linking of fibrils of collagen V/XI in A204 rhabdomyosarcoma cells. Biochemistry 34:13768-13775
    • (1995) Biochemistry , vol.34 , pp. 13768-13775
    • Kleman, J.P.1    Aeschlimann, D.2    Paulsson, M.3    Van Der Rest, M.4
  • 35
    • 84862695997 scopus 로고    scopus 로고
    • The role of tissue transglutaminase (TG2) in regulating the tumour progression of the mouse colon carcinoma CT26
    • In press)
    • Kotsakis P, Wang Z, Collighan RJ, Griffin M (2010) The role of tissue transglutaminase (TG2) in regulating the tumour progression of the mouse colon carcinoma CT26. Amino Acids (In press)
    • (2010) Amino Acids
    • Kotsakis, P.1    Wang, Z.2    Collighan, R.J.3    Griffin, M.4
  • 36
    • 78149462058 scopus 로고    scopus 로고
    • Tissue transglutaminase promotes drug resistance and invasion by inducing mesenchymal transition in mammary epithelial cells
    • Kumar A, Xu J, Brady S, Gao H, Yu D, Reuben J, Mehta K (2010) Tissue transglutaminase promotes drug resistance and invasion by inducing mesenchymal transition in mammary epithelial cells. PLoS One 5:e13390
    • (2010) PLoS One , vol.5
    • Kumar, A.1    Xu, J.2    Brady, S.3    Gao, H.4    Yu, D.5    Reuben, J.6    Mehta, K.7
  • 37
    • 84862699536 scopus 로고    scopus 로고
    • TNFalpha modulates expression of the tissue transglutaminase gene in human HEPG2 cells
    • Kuncio GS, Tsyganskaya M, Zhu J, Liu SL, Zern MA (1996) TNFalpha modulates expression of the tissue transglutaminase gene in human HEPG2 cells. Hepatology 24: 813
    • (1996) Hepatology , vol.24 , pp. 813
    • Kuncio, G.S.1    Tsyganskaya, M.2    Zhu, J.3    Liu, S.L.4    Zern, M.A.5
  • 38
    • 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
    • DOI 10.1074/jbc.273.3.1776
    • 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 (Pubitemid 28133710)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.3 , pp. 1776-1781
    • Lai, T.-S.1    Slaughter, T.F.2    Peoples, K.A.3    Hettasch, J.M.4    Greenberg, C.S.5
  • 39
    • 0035942305 scopus 로고    scopus 로고
    • Calcium regulates S-nitrosylation, denitrosylation, and activity of tissue transglutaminase
    • DOI 10.1021/bi002321t
    • Lai TS, Hausladen A, Slaughter TF, Eu JP, Stamler JS, Greenberg CS (2001) Calcium regulates S-nitrosylation, denitrosylation, and activity of tissue transglutaminase. Biochemistry 40:4904-4910 (Pubitemid 32332535)
    • (2001) Biochemistry , vol.40 , Issue.16 , pp. 4904-4910
    • Lai, T.S.1    Hausladen, A.2    Slaughter, T.F.3    Eu, J.P.4    Stamler, J.S.5    Greenberg, C.S.6
  • 40
    • 84862637165 scopus 로고
    • Affinity of human red-cell transglutaminase for a 42 k gelatinbinding fragment of human plasma fibronectin
    • Lorand L, Radek JT, Jeong JM, Murthy SNP, Ingham KC (1993) Affinity of human red-cell transglutaminase for a 42 k gelatinbinding fragment of human plasma fibronectin. Faseb J 7:A1280
    • (1993) Faseb J , vol.7
    • Lorand, L.1    Radek, J.T.2    Jeong, J.M.3    Murthy, S.N.P.4    Ingham, K.C.5
  • 41
    • 14544298333 scopus 로고    scopus 로고
    • Tissue transglutaminase (TG2) in cancer biology
    • Mangala LS, Mehta K (2005) Tissue transglutaminase (TG2) in cancer biology. Prog Exp Tumor Res 38:125-138
    • (2005) Prog Exp Tumor Res , vol.38 , pp. 125-138
    • Mangala, L.S.1    Mehta, K.2
  • 42
    • 34247153086 scopus 로고    scopus 로고
    • Tissue transglutaminase expression promotes cell attachment, invasion and survival in breast cancer cells
    • DOI 10.1038/sj.onc.1210035, PII 1210035
    • Mangala LS, Fok JY, Zorrilla-Calancha IR, Verma A, Mehta K (2007) Tissue transglutaminase expression promotes cell attachment, invasion and survival in breast cancer cells. Oncogene 26:2459-2470 (Pubitemid 46597265)
    • (2007) Oncogene , vol.26 , Issue.17 , pp. 2459-2470
    • Mangala, L.S.1    Fok, J.Y.2    Zorrilla-Calancha, I.R.3    Verma, A.4    Mehta, K.5
  • 43
    • 0030071518 scopus 로고    scopus 로고
    • Activation of retinoid receptors RARα and RXRα induces differentiation and apoptosis, respectively, in HL-60 cells
    • Mehta K, McQueen T, Neamati N, Collins S, Andreeff M (1996) Activation of retinoid receptors RAR alpha and RXR alpha induces differentiation and apoptosis, respectively, in HL-60 cells. Cell Growth Differ 7:179-186 (Pubitemid 26049826)
    • (1996) Cell Growth and Differentiation , vol.7 , Issue.2 , pp. 179-186
    • Mehta, K.1    McQueen, T.2    Neamati, N.3    Collins, S.4    Andreeff, M.5
  • 44
    • 32844467408 scopus 로고    scopus 로고
    • Tissue transglutaminase: From biological glue to cell survival cues
    • Mehta K, Fok JY, Mangala LS (2006) Tissue transglutaminase: from biological glue to cell survival cues. Front Biosci 11:173-185 (Pubitemid 43253484)
    • (2006) Frontiers in Bioscience , vol.11 , Issue.1 PART 1-446 , pp. 173-185
    • Mehta, K.1    Fok, J.Y.2    Mangala, L.S.3
  • 45
    • 78049427740 scopus 로고    scopus 로고
    • Transglutaminase 2: A multitasking protein in the complex circuitry of inflammation and cancer
    • Mehta K, Kumar A, Kim HI (2010) Transglutaminase 2: a multitasking protein in the complex circuitry of inflammation and cancer. Biochem Pharmacol 80:1921-1929
    • (2010) Biochem Pharmacol , vol.80 , pp. 1921-1929
    • Mehta, K.1    Kumar, A.2    Kim, H.I.3
  • 46
    • 2642536093 scopus 로고    scopus 로고
    • Tissue transglutaminase has intrinsic kinase activity. Identification of transglutaminase 2 as an insulin-like growth factor-binding protein-3 kinase
    • DOI 10.1074/jbc.M311919200
    • Mishra S, Murphy LJ (2004) Tissue transglutaminase has intrinsic kinase activity: identification of transglutaminase 2 as an insulinlike growth factor-binding protein-3 kinase. J Biol Chem 279:23863-23868 (Pubitemid 38725242)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.23 , pp. 23863-23868
    • Mishra, S.1    Murphy, L.J.2
  • 47
    • 28444488402 scopus 로고    scopus 로고
    • The p53 oncoprotein is a substrate for tissue transglutaminase kinase activity
    • DOI 10.1016/j.bbrc.2005.11.071, PII S0006291X05025982
    • Mishra S, Murphy LJ (2006) The p53 oncoprotein is a substrate for tissue transglutaminase kinase activity. Biochem Biophys Res Comm 339:726-730 (Pubitemid 41739727)
    • (2006) Biochemical and Biophysical Research Communications , vol.339 , Issue.2 , pp. 726-730
    • Mishra, S.1    Murphy, L.J.2
  • 48
  • 49
    • 78650709900 scopus 로고    scopus 로고
    • Extracellular transglutaminase 2 has a role in cell adhesion, whereas intracellular transglutaminase 2 is involved in regulation of endothelial cell proliferation and apoptosis
    • Nadalutti C, Viiri KM, Kaukinen K, Maki M, Lindfors K (2011) Extracellular transglutaminase 2 has a role in cell adhesion, whereas intracellular transglutaminase 2 is involved in regulation of endothelial cell proliferation and apoptosis. Cell Prolif 44:49-58
    • (2011) Cell Prolif , vol.44 , pp. 49-58
    • Nadalutti, C.1    Viiri, K.M.2    Kaukinen, K.3    Maki, M.4    Lindfors, K.5
  • 50
    • 75749134894 scopus 로고    scopus 로고
    • Regulation of ATPase activity of transglutaminase 2 by MT1-MMP: Implications for mineralization of MC3T3-E1 osteoblast cultures
    • Nakano Y, Forsprecher J, Kaartinen MT (2010) Regulation of ATPase activity of transglutaminase 2 by MT1-MMP: implications for mineralization of MC3T3-E1 osteoblast cultures. J Cell Physiol 223:260-269
    • (2010) J Cell Physiol , vol.223 , pp. 260-269
    • Nakano, Y.1    Forsprecher, J.2    Kaartinen, M.T.3
  • 51
    • 43749105347 scopus 로고    scopus 로고
    • Size distribution and molecular associations of plasma fibronectin and fibronectin crosslinked by transglutaminase 2
    • Nelea V, Nakano Y, Kaartinen MT (2008) Size distribution and molecular associations of plasma fibronectin and fibronectin crosslinked by transglutaminase 2. Protein J 27:223-233
    • (2008) Protein J , vol.27 , pp. 223-233
    • Nelea, V.1    Nakano, Y.2    Kaartinen, M.T.3
  • 52
    • 0032988045 scopus 로고    scopus 로고
    • Interaction of tissue transglutaminase with nuclear transport protein importin-α3
    • DOI 10.1016/S0014-5793(99)00018-6, PII S0014579399000186
    • Peng XJ, Zhang YH, Zhang HF, Graner S, Williams JF, Levitt ML, Lokshin A (1999) Interaction of tissue transglutaminase with nuclear transport protein importin-alpha 3. FEBS Lett 446:35-39 (Pubitemid 29127245)
    • (1999) FEBS Letters , vol.446 , Issue.1 , pp. 35-39
    • Peng, X.1    Zhang, Y.2    Zhang, H.3    Graner, S.4    Williams, J.F.5    Levitt, M.L.6    Lokshin, A.7
  • 53
    • 26444591889 scopus 로고    scopus 로고
    • TGF-β1 up-regulates transglutaminase two and fibronectin in dermal fibroblasts: A possible mechanism for the stabilization of tissue inflammation
    • DOI 10.1007/s00403-005-0582-8
    • Quan G, Choi JY, Lee DS, Lee SC (2005) TGF-beta up-regulates transglutaminase two and fibronectin in dermal fibroblasts: a possible mechanism for the stabilization of tissue inflammation. Arch Dermatol Res 297:84-90 (Pubitemid 41431547)
    • (2005) Archives of Dermatological Research , vol.297 , Issue.2 , pp. 84-90
    • Quan, G.1    Choi, J.-Y.2    Lee, D.-S.3    Lee, S.-C.4
  • 55
    • 67650513329 scopus 로고    scopus 로고
    • Heparan sulphate proteoglycans are receptors for the cell-surface trafficking and biological activity of transglutaminase-2
    • Scarpellini A, Germack R, Lortat-Jacob H, Muramtsu T, Johnson TS, Billett E, Verderio EA (2009) Heparan sulphate proteoglycans are receptors for the cell-surface trafficking and biological activity of transglutaminase-2. J Biol Chem 284:18411-18423
    • (2009) J Biol Chem , vol.284 , pp. 18411-18423
    • Scarpellini, A.1    Germack, R.2    Lortat-Jacob, H.3    Muramtsu, T.4    Johnson, T.S.5    Billett, E.6    Verderio, E.A.7
  • 56
    • 34447286702 scopus 로고    scopus 로고
    • Transglutaminase 2 inhibitors and their therapeutic role in disease states
    • DOI 10.1016/j.pharmthera.2007.05.003, PII S0163725807000885
    • Siegel M, Khosla C (2007) Transglutaminase 2 inhibitors and their therapeutic role in disease states. Pharmacol Ther 115:232-245 (Pubitemid 47042912)
    • (2007) Pharmacology and Therapeutics , vol.115 , Issue.2 , pp. 232-245
    • Siegel, M.1    Khosla, C.2
  • 57
    • 0030032813 scopus 로고    scopus 로고
    • Measurement of tissue transglutaminase activity in a permeabilized cell system: Its regulation by Ca2+ and nucleotides
    • Smethurst PA, Griffin M (1996) Measurement of tissue transglutaminase activity in a permeabilized cell system: its regulation by Ca2+ and nucleotides. Biochem J 313:803-808
    • (1996) Biochem J , vol.313 , pp. 803-808
    • Smethurst, P.A.1    Griffin, M.2
  • 59
    • 68549094202 scopus 로고    scopus 로고
    • The treatment of collagen fibrils by tissue transglutaminase to promote vascular smooth muscle cell contractile signaling
    • Spurlin TA, Bhadriraju K, Chung KH, Tona A, Plant AL (2009) The treatment of collagen fibrils by tissue transglutaminase to promote vascular smooth muscle cell contractile signaling. Biomaterials 30:5486-5496
    • (2009) Biomaterials , vol.30 , pp. 5486-5496
    • Spurlin, T.A.1    Bhadriraju, K.2    Chung, K.H.3    Tona, A.4    Plant, A.L.5
  • 62
    • 0027405028 scopus 로고
    • Expression induced by interleukin-6 of tissue-type transglutaminase in human hepatoblastoma HepG2 cells
    • Suto N, Ikura K, Sasaki R (1993) Expression induced by interleukin-6 of tissue-type transglutaminase in human hepatoblastoma Hepg2 cells. J Biol Chem 268:7469-7473 (Pubitemid 23105644)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.10 , pp. 7469-7473
    • Suto, N.1    Ikura, K.2    Sasaki, R.3
  • 63
    • 34447574642 scopus 로고    scopus 로고
    • The integrin α5β1 regulates chondrocyte hypertrophic differentiation induced by GTP-bound transglutaminase 2
    • DOI 10.1016/j.matbio.2007.04.005, PII S0945053X07000479
    • Tanaka K, Yokosaki Y, Higashikawa F, Saito Y, Eboshida A, Ochi M (2007) The integrin alpha 5 beta 1 regulates chondrocyte hypertrophic differentiation induced by GTP-bound transglutaminase 2. Matrix Biol 26:409-418 (Pubitemid 47081395)
    • (2007) Matrix Biology , vol.26 , Issue.6 , pp. 409-418
    • Tanaka, K.1    Yokosaki, Y.2    Higashikawa, F.3    Saito, Y.4    Eboshida, A.5    Ochi, M.6
  • 65
    • 51049089580 scopus 로고    scopus 로고
    • Fibronectin-tissue transglutaminase matrix rescues RGD-impaired cell adhesion through syndecan-4 and beta1 integrin co-signaling
    • Telci D, Wang Z, Li X, Verderio EA, Humphries MJ, Baccarini M, Basaga H, Griffin M (2008) Fibronectin-tissue transglutaminase matrix rescues RGD-impaired cell adhesion through syndecan-4 and beta1 integrin co-signaling. J Biol Chem 283:20937-20947
    • (2008) J Biol Chem , vol.283 , pp. 20937-20947
    • Telci, D.1    Wang, Z.2    Li, X.3    Verderio, E.A.4    Humphries, M.J.5    Baccarini, M.6    Basaga, H.7    Griffin, M.8
  • 66
    • 70350380992 scopus 로고    scopus 로고
    • Increased TG2 expression can result in induction of transforming growth factor beta 1, causing increased synthesis and deposition of matrix proteins, which can be regulated by nitric oxide
    • Telci D, Collighan RJ, Basaga H, Griffin M (2009) Increased TG2 expression can result in induction of transforming growth factor beta 1, causing increased synthesis and deposition of matrix proteins, which can be regulated by nitric oxide. J Biol Chem 284:29547-29558
    • (2009) J Biol Chem , vol.284 , pp. 29547-29558
    • Telci, D.1    Collighan, R.J.2    Basaga, H.3    Griffin, M.4
  • 67
    • 70249137178 scopus 로고    scopus 로고
    • Over-expression of integrin beta 3 can partially overcome the defect of integrin beta 3 signaling in transglutaminase 2 null macrophages
    • Toth B, Sarang Z, Vereb G, Zhang AL, Tanaka S, Melino G, Fesus L, Szondy Z (2009) Over-expression of integrin beta 3 can partially overcome the defect of integrin beta 3 signaling in transglutaminase 2 null macrophages. Imm Lett 126:22-28
    • (2009) Imm Lett , vol.126 , pp. 22-28
    • Toth, B.1    Sarang, Z.2    Vereb, G.3    Zhang, A.L.4    Tanaka, S.5    Melino, G.6    Fesus, L.7    Szondy, Z.8
  • 69
    • 0031869591 scopus 로고    scopus 로고
    • Regulated expression of tissue transglutaminase in Swiss 3T3 fibroblasts: Effects on the processing of fibronectin, cell attachment, and cell death
    • DOI 10.1006/excr.1997.3874
    • Verderio E, Nicholas B, Gross S, Griffin M (1998) Regulated expression of tissue transglutaminase in Swiss 3T3 fibroblasts: effects on the processing of fibronectin, cell attachment, and cell death. Exp Cell Res 239:119-138 (Pubitemid 28368484)
    • (1998) Experimental Cell Research , vol.239 , Issue.1 , pp. 119-138
    • Verderio, E.1    Nicholas, B.2    Gross, S.3    Griffin, M.4
  • 70
    • 0142242157 scopus 로고    scopus 로고
    • A novel rgd-independent cell adhesion pathway mediated by fibronectin-bound tissue transglutaminase rescues cells from anoikis
    • DOI 10.1074/jbc.M303303200
    • Verderio EA, Telci D, Okoye A, Melino G, Griffin M (2003) A novel RGD-independent cell adhesion pathway mediated by fibronectin- bound tissue transglutaminase rescues cells from anoikis. J Biol Chem 278:42604-42614 (Pubitemid 37310534)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.43 , pp. 42604-42614
    • Verderio, E.A.M.1    Telci, D.2    Okoye, A.3    Melino, G.4    Griffin, M.5
  • 71
    • 4143089161 scopus 로고    scopus 로고
    • Tissue transglutaminase in normal and abnormal wound healing: Review article
    • Verderio EA, Johnson T, Griffin M (2004) Tissue transglutaminase in normal and abnormal wound healing: review article. Amino Acids 26:387-404 (Pubitemid 39093142)
    • (2004) Amino Acids , vol.26 , Issue.4 , pp. 387-404
    • Verderio, E.A.M.1    Johnson, T.2    Griffin, M.3
  • 72
    • 33751285778 scopus 로고    scopus 로고
    • Increased expression of tissue transglutaminase in pancreatic ductal adenocarcinoma and its implications in drug resistance and metastasis
    • DOI 10.1158/0008-5472.CAN-06-2387
    • Verma A, Wang H, Manavathi B, Fok JY, Mann AP, Kumar R, Mehta K (2006) Increased expression of tissue transglutaminase in pancreatic ductal adenocarcinoma and its implications in drug resistance and metastasis. Cancer Res 66:10525-10533 (Pubitemid 44799775)
    • (2006) Cancer Research , vol.66 , Issue.21 , pp. 10525-10533
    • Verma, A.1    Wang, H.2    Manavathi, B.3    Fok, J.Y.4    Mann, A.P.5    Kumar, R.6    Mehta, K.7
  • 74
    • 78650069909 scopus 로고    scopus 로고
    • RGD-independent cell adhesion via a tissue transglutaminase-fibronectin matrix promotes fibronectin fibril deposition and requires syndecan-4/2 and {alpha} 5{beta}1 integrin co-signaling
    • Wang Z, Collighan RJ, Gross SR, Danen EH, Orend G, Telci D, Griffin M (2010) RGD-independent cell adhesion via a tissue transglutaminase-fibronectin matrix promotes fibronectin fibril deposition and requires syndecan-4/2 and {alpha}5{beta}1 integrin co-signaling. J Biol Chem 285:40212-40229
    • (2010) J Biol Chem , vol.285 , pp. 40212-40229
    • Wang, Z.1    Collighan, R.J.2    Gross, S.R.3    Danen, E.H.4    Orend, G.5    Telci, D.6    Griffin, M.7
  • 75
    • 78650047218 scopus 로고    scopus 로고
    • Importance of syndecan-4 and syndecan-2 in osteoblast cell adhesion and survival mediated by a tissue transglutaminase-fibronectin complex
    • Wang Z, Telci D, Griffin M (2011) Importance of syndecan-4 and syndecan-2 in osteoblast cell adhesion and survival mediated by a tissue transglutaminase-fibronectin complex. Exp Cell Res 317:367-381
    • (2011) Exp Cell Res , vol.317 , pp. 367-381
    • Wang, Z.1    Telci, D.2    Griffin, M.3
  • 78
    • 34247349128 scopus 로고    scopus 로고
    • Transglutaminase 2 inhibitor, KCC009, disrupts fibronectin assembly in the extracellular matrix and sensitizes orthotopic glioblastomas to chemotherapy
    • DOI 10.1038/sj.onc.1210048, PII 1210048
    • Yuan L, Siegel M, Choi K, Khosla C, Miller CR, Jackson EN, Piwnica-Worms D, Rich KM (2007) Transglutaminase 2 inhibitor, KCC009, disrupts fibronectin assembly in the extracellular matrix and sensitizes orthotopic glioblastomas to chemotherapy. Oncogene 26:2563-2573 (Pubitemid 46632005)
    • (2007) Oncogene , vol.26 , Issue.18 , pp. 2563-2573
    • Yuan, L.1    Siegel, M.2    Choi, K.3    Khosla, C.4    Miller, C.R.5    Jackson, E.N.6    Piwnica-Worms, D.7    Rich, K.M.8
  • 79
    • 67650221578 scopus 로고    scopus 로고
    • Regulation of platelet-derived growth factor receptor function by integrin-associated cell surface transglutaminase
    • Zemskov EA, Loukinova E, Mikhailenko I, Coleman RA, Strickland DK, Belkin AM (2009) Regulation of platelet-derived growth factor receptor function by integrin-associated cell surface transglutaminase. J Biol Chem 284:16693-16703
    • (2009) J Biol Chem , vol.284 , pp. 16693-16703
    • Zemskov, E.A.1    Loukinova, E.2    Mikhailenko, I.3    Coleman, R.A.4    Strickland, D.K.5    Belkin, A.M.6
  • 80
    • 79955692581 scopus 로고    scopus 로고
    • Unconventional secretion of tissue transglutaminase involves phospholipid-dependent delivery into recycling endosomes
    • Zemskov EA, Mikhailenko I, Hsia RC, Zaritskaya L, Belkin AM (2011) Unconventional secretion of tissue transglutaminase involves phospholipid-dependent delivery into recycling endosomes. PLoS One 6:e19414
    • (2011) PLoS One , vol.6
    • Zemskov, E.A.1    Mikhailenko, I.2    Hsia, R.C.3    Zaritskaya, L.4    Belkin, A.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.