메뉴 건너뛰기




Volumn 287, Issue 22, 2012, Pages 18005-18017

Transglutaminase-2 interaction with heparin: Identification of a heparin binding site that regulates cell adhesion to fibronectin-transglutaminase-2 matrix

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PARTNERS; BINDING SURFACE; CANCER PROGRESSION; CELL SURFACES; EXTRACELLULAR; HEPARAN SULFATES; HEPARIN BINDING; HEPARIN-BINDING SITE; HIGH AFFINITY; LINEAR SEQUENCE; MOLECULAR BASIS; MULTIFUNCTIONAL PROTEIN; PENTASACCHARIDES; PROTEOGLYCANS; SITE DIRECTED MUTAGENESIS; SPATIAL PROXIMITY; THREE-DIMENSIONAL STRUCTURE; TISSUE REMODELING; WILD TYPES; WOUND HEALING;

EID: 84861557321     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.337089     Document Type: Article
Times cited : (51)

References (50)
  • 1
    • 67651071286 scopus 로고    scopus 로고
    • Transglutaminases and disease. Lessons from genetically engineered mouse models and inherited disorders
    • Iismaa, S. E., Mearns, B. M., Lorand, L., and Graham, R. M. (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
  • 2
    • 60749095387 scopus 로고    scopus 로고
    • Single proteins might have dual but related functions in intracellular and extracellular microenvironments
    • Radisky, D. C., Stallings-Mann, M., Hirai, Y., and Bissell, M. J. (2009) Single proteins might have dual but related functions in intracellular and extracellular microenvironments. Nat. Rev. Mol. Cell Biol. 10, 228-234
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 228-234
    • Radisky, D.C.1    Stallings-Mann, M.2    Hirai, Y.3    Bissell, M.J.4
  • 3
    • 82755187317 scopus 로고    scopus 로고
    • Extracellular TG2. Emerging functions and regulation
    • Belkin, A. M. (2011) Extracellular TG2. Emerging functions and regulation. FEBS J. 278, 4704-4716
    • (2011) FEBS J. , vol.278 , pp. 4704-4716
    • Belkin, A.M.1
  • 4
    • 4143089161 scopus 로고    scopus 로고
    • Tissue transglutaminase in normal and abnormal wound healing: Review article
    • Verderio, E. A., Johnson, T., and 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
  • 7
    • 67650179228 scopus 로고    scopus 로고
    • Tissue transglutaminase regulates matrix metalloproteinase-2 in ovarian cancer by modulating cAMP-response element-binding protein activity
    • Satpathy, M., Shao, M., Emerson, R., Donner, D. B., and Matei, D. (2009) Tissue transglutaminase regulates matrix metalloproteinase-2 in ovarian cancer by modulating cAMP-response element-binding protein activity. J. Biol. Chem. 284, 15390-15399
    • (2009) J. Biol. Chem. , vol.284 , pp. 15390-15399
    • Satpathy, M.1    Shao, M.2    Emerson, R.3    Donner, D.B.4    Matei, D.5
  • 8
    • 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, M. A., Li, B., Regan, A. D., Feng, Q., Dusaban, S. S., and Cerione, R. A. (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
  • 12
    • 0037317032 scopus 로고    scopus 로고
    • Transglutaminases: Crosslinking enzymes with pleiotropic functions
    • DOI 10.1038/nrm1014
    • Lorand, L., and Graham, R. M. (2003) Transglutaminases. Cross-linking enzymes with pleiotropic functions. Nat. Rev. Mol. Cell Biol. 4, 140-156 (Pubitemid 36172696)
    • (2003) Nature Reviews Molecular Cell Biology , vol.4 , Issue.2 , pp. 140-156
    • Lorand, L.1    Graham, R.M.2
  • 15
    • 0028176166 scopus 로고
    • Gh, a GTP-binding protein with transglutaminase activity and receptor signaling function
    • Nakaoka, H., Perez, D. M., Baek, K. J., Das, T., Husain, A., Misono, K., Im, M. J., and Graham, R. M. (1994) Gh, a GTP-binding protein with transglutaminase activity and receptor signaling function. Science 264, 1593-1596
    • (1994) Science , vol.264 , pp. 1593-1596
    • Nakaoka, H.1    Perez, D.M.2    Baek, K.J.3    Das, T.4    Husain, A.5    Misono, K.6    Im, M.J.7    Graham, R.M.8
  • 16
    • 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., and 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
  • 17
    • 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., and 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
  • 18
    • 0034695929 scopus 로고    scopus 로고
    • Tissue transglutaminase is an integrin binding adhesion coreceptor for fibronectin
    • Akimov, S. S., Krylov, D., Fleischman, L. F., and Belkin, A. M. (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
  • 19
    • 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, E. A., Telci, D., Okoye, A., Melino, G., and Griffin, M. (2003) A novel RGD-independent cel 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
  • 20
    • 51049089580 scopus 로고    scopus 로고
    • Fibronectin tissue transglutaminase matrix rescues RGD-impaired cell adhesion through syndecan-4 and β1 integrin co-signaling
    • Telci, D., Wang, Z., Li, X., Verderio, E. A., Humphries, M. J., Baccarini, M., Basaga, H., and Griffin, M. (2008) Fibronectin tissue transglutaminase matrix rescues RGD-impaired cell adhesion through syndecan-4 and β1 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
  • 21
    • 82755161784 scopus 로고    scopus 로고
    • 2+-dependent action of a multifunctional protein
    • 2+-dependent action of a multifunctional protein. FEBS J. 278, 4717-4739
    • (2011) FEBS J. , vol.278 , pp. 4717-4739
    • Király, R.1    Demény, M.2    Fésüs, L.3
  • 22
    • 79955692581 scopus 로고    scopus 로고
    • Unconventional secretion of tissue transglutaminase involves phospholipid-dependent delivery into recycling endosomes
    • Zemskov, E. A., Mikhailenko, I., Hsia, R. C., Zaritskaya, L., and Belkin, A. M. (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
  • 23
    • 67650513329 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans are receptors for the cell-surface trafficking and biological activity of transglutaminase-2
    • Scarpellini, A., Germack, R., Lortat-Jacob, H., Muramatsu, T., Billett, E., Johnson, T., and Verderio, E. A. (2009) Heparan sulfate 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    Muramatsu, T.4    Billett, E.5    Johnson, T.6    Verderio, E.A.7
  • 24
    • 62949246706 scopus 로고    scopus 로고
    • Novel interactions of TG2 with heparan sulfate proteoglycans. Reflection on physiological implications
    • Verderio, E. A., Scarpellini, A., and Johnson, T. S. (2009) Novel interactions of TG2 with heparan sulfate proteoglycans. reflection on physiological implications. Amino Acids 36, 671-677
    • (2009) Amino Acids , vol.36 , pp. 671-677
    • Verderio, E.A.1    Scarpellini, A.2    Johnson, T.S.3
  • 25
    • 77955890413 scopus 로고    scopus 로고
    • Significance of the syndecan-4-transglutaminase-2 interaction
    • Verderio, E., and Scarpellini, A. (2010) Significance of the syndecan-4-transglutaminase-2 interaction. ScientificWorldJournal 10, 1073-1077
    • (2010) ScientificWorldJournal , vol.10 , pp. 1073-1077
    • Verderio, E.1    Scarpellini, A.2
  • 26
    • 25444451599 scopus 로고    scopus 로고
    • Chemokine-glycosaminoglycan binding: Specificity for CCR2 ligand binding to highly sulfated oligosaccharides using FTICR mass spectrometry
    • DOI 10.1074/jbc.M505738200
    • Yu, Y., Sweeney, M. D., Saad, O. M., Crown, S. E., Hsu, A. R., Handel, T. M., and Leary, J. A. (2005) Chemokine-glycosaminoglycan binding. Specificity for CCR2 ligand binding to highly sulfated oligosaccharides using FTICR mass spectrometry. J. Biol. Chem. 280, 32200-32208 (Pubitemid 41361827)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.37 , pp. 32200-32208
    • Yu, Y.1    Sweeney, M.D.2    Saad, O.M.3    Crown, S.E.4    Handel, T.M.5    Leary, J.A.6
  • 27
    • 34247610845 scopus 로고    scopus 로고
    • Heparan sulphate proteoglycans fine-tune mammalian physiology
    • DOI 10.1038/nature05817, PII NATURE05817
    • Bishop, J. R., Schuksz, M., and Esko, J. D. (2007) Heparan sulfate proteoglycans fine-tune mammalian physiology. Nature 446, 1030-1037 (Pubitemid 46676065)
    • (2007) Nature , vol.446 , Issue.7139 , pp. 1030-1037
    • Bishop, J.R.1    Schuksz, M.2    Esko, J.D.3
  • 28
    • 0037022619 scopus 로고    scopus 로고
    • Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity
    • DOI 10.1073/pnas.042454899
    • Liu, S., Cerione, R. A., and Clardy, J. (2002) Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity. Proc. Natl. Acad. Sci. U.S.A. 99, 2743-2747 (Pubitemid 34240531)
    • (2002) Proceedings of the National Academy of Sciences of the United States of America , vol.99 , Issue.5 , pp. 2743-2747
    • Liu, S.1    Cerione, R.A.2    Clardy, J.3
  • 29
    • 77954143820 scopus 로고    scopus 로고
    • Crystal structure of human transglutaminase 2 in complex with adenosine triphosphate
    • Han, B. G., Cho, J. W., Cho, Y. D., Jeong, K. C., Kim, S. Y., and Lee, B. I. (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.G.1    Cho, J.W.2    Cho, Y.D.3    Jeong, K.C.4    Kim, S.Y.5    Lee, B.I.6
  • 31
    • 0037039447 scopus 로고    scopus 로고
    • High selectivity of human tissue transglutaminase for immunoactive gliadin peptides: Implications for Celiac Sprue
    • DOI 10.1021/bi011715x
    • Piper, J. L., Gray, G. M., and Khosla, C. (2002) High selectivity of human tissue transglutaminase for immunoactive gliadin peptides. Implications for celiac sprue. Biochemistry 41, 386-393 (Pubitemid 34049414)
    • (2002) Biochemistry , vol.41 , Issue.1 , pp. 386-393
    • Piper, J.L.1    Gray, G.M.2    Khosla, C.3
  • 33
    • 37249005205 scopus 로고    scopus 로고
    • The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability
    • DOI 10.1038/nprot.2007.321, PII NPROT.2007.321
    • Niesen, F. H., Berglund, H., and Vedadi, M. (2007) The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability. Nat. Protoc. 2, 2212-2221 (Pubitemid 351565860)
    • (2007) Nature Protocols , vol.2 , Issue.9 , pp. 2212-2221
    • Niesen, F.H.1    Berglund, H.2    Vedadi, M.3
  • 34
    • 0010115712 scopus 로고    scopus 로고
    • Reduced expression of tissue transglutaminase in a human endothelial cell line leads to changes in cell spreading, cell adhesion and reduced polymerisation of fibronectin
    • Jones, R. A., Nicholas, B., Mian, S., Davies, P. J., and Griffin, M. (1997) Reduced expression of tissue transglutaminase in a human endothelial cell line leads to changes in cell spreading, cell adhesion, and reduced polymerisation of fibronectin. J. Cell Sci. 110, 2461-2472 (Pubitemid 127699160)
    • (1997) Journal of Cell Science , vol.110 , Issue.19 , pp. 2461-2472
    • Jones, R.A.1    Nicholas, B.2    Mian, S.3    Davies, P.J.A.4    Griffin, M.5
  • 35
    • 0035913529 scopus 로고    scopus 로고
    • Evaluation and reparametrization of the OPLS-AA force field for proteins via comparison with accurate quantum chemical calculations on peptides
    • DOI 10.1021/jp003919d
    • Kaminski, G. A., Friesner, R. A., Tirado-Rives, J., and Jorgensen, W. L. (2001) Evaluation and reparametrization of the OPLSAA force field for proteins via comparison with accurate quantum chemical calculations on peptides. J. Phys. Chem. B 105, 6474-6487 (Pubitemid 35339015)
    • (2001) Journal of Physical Chemistry B , vol.105 , Issue.28 , pp. 6474-6487
    • Kaminski, G.A.1    Friesner, R.A.2    Tirado-Rives, J.3    Jorgensen, W.L.4
  • 36
    • 0027164634 scopus 로고
    • N.m.r. And molecular-modelling studies of the solution conformation of heparin
    • Mulloy, B., Forster, M. J., Jones, C., and Davies, D. B. (1993) NMR and molecular-modeling studies of the solution conformation of heparin. Biochem. J. 293, 849-858 (Pubitemid 23244575)
    • (1993) Biochemical Journal , vol.293 , Issue.3 , pp. 849-858
    • Mulloy, B.1    Forster, M.J.2    Jones, C.3    Davies, D.B.4
  • 39
    • 11144234551 scopus 로고    scopus 로고
    • A novel strategy for defining critical amino acid residues involved in protein/glycosaminoglycan interactions
    • DOI 10.1074/jbc.M409760200
    • Vivès, R. R., Crublet, E., Andrieu, J. P., Gagnon, J., Rousselle, P., and Lortat-Jacob, H. (2004) A novel strategy for defining critical amino acid residues involved in protein/glycosaminoglycan interactions. J. Biol. Chem. 279, 54327-54333 (Pubitemid 40053171)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.52 , pp. 54327-54333
    • Vives, R.R.1    Crublet, E.2    Andrieu, J.-P.3    Gagnon, J.4    Rousselle, P.5    Lortat-Jacob, H.6
  • 40
    • 33744950386 scopus 로고    scopus 로고
    • Mutation of a critical arginine in the GTP-binding site of transglutaminase 2 disinhibits intracellular cross-linking activity
    • DOI 10.1074/jbc.M600146200
    • Begg, G. E., Holman, S. R., Stokes, P. H., Matthews, J. M., Graham, R. M., and Iismaa, S. E. (2006) Mutation of a critical arginine in the GTP-binding site of transglutaminase 2 disinhibits intracellular cross-linking activity. J. Biol. Chem. 281, 12603-12609 (Pubitemid 43855349)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.18 , 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
  • 41
    • 38549156658 scopus 로고    scopus 로고
    • Transglutaminase 2 undergoes a large conformational change upon activation
    • Pinkas, D. M., Strop, P., Brunger, A. T., and 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
  • 42
    • 73249136226 scopus 로고    scopus 로고
    • Semi-rigid solution structures of heparin by constrained X-ray scattering modeling. New insight into heparin-protein complexes
    • Khan, S., Gor, J., Mulloy, B., and Perkins, S. J. (2010) Semi-rigid solution structures of heparin by constrained X-ray scattering modeling. New insight into heparin-protein complexes. J. Mol. Biol. 395, 504-521
    • (2010) J. Mol. Biol. , vol.395 , pp. 504-521
    • Khan, S.1    Gor, J.2    Mulloy, B.3    Perkins, S.J.4
  • 43
    • 0030878831 scopus 로고    scopus 로고
    • Combined NMR and molecular modeling study of an iduronic acid-containing trisaccharide related to antithrombotic heparin fragments
    • DOI 10.1016/S0968-0896(97)00087-4, PII S0968089697000874
    • Cros, S., Petitou, M., Sizun, P., Pérez, S., and Imberty, A. (1997) Combined NMR and molecular modeling study of an iduronic acid-containing trisaccharide related to antithrombotic heparin fragments. Bioorg. Med. Chem. 5, 1301-1309 (Pubitemid 27321215)
    • (1997) Bioorganic and Medicinal Chemistry , vol.5 , Issue.7 , pp. 1301-1309
    • Cros, S.1    Petitou, M.2    Sizun, P.3    Perez, S.4    Imberty, A.5
  • 44
    • 0035896615 scopus 로고    scopus 로고
    • Characterization of the stromal cell-derived factor-1α-heparin complex
    • Sadir, R., Baleux, F., Grosdidier, A., Imberty, A., and Lortat-Jacob, H. (2001) Characterization of the stromal cell-derived factor-1α-heparin complex. J. Biol. Chem. 276, 8288-8296
    • (2001) J. Biol. Chem. , vol.276 , pp. 8288-8296
    • Sadir, R.1    Baleux, F.2    Grosdidier, A.3    Imberty, A.4    Lortat-Jacob, H.5
  • 45
    • 46749147598 scopus 로고    scopus 로고
    • Extracellular transglutaminase 2 is catalytically inactive but is transiently activated upon tissue injury
    • Siegel, M., Strnad, P., Watts, R. E., Choi, K., Jabri, B., Omary, M. B., and Khosla, C. (2008) Extracellular transglutaminase 2 is catalytically inactive but is transiently activated upon tissue injury. PLoS One 3, e1861
    • (2008) PLoS One , vol.3
    • Siegel, M.1    Strnad, P.2    Watts, R.E.3    Choi, K.4    Jabri, B.5    Omary, M.B.6    Khosla, C.7
  • 48
    • 70350380992 scopus 로고    scopus 로고
    • Increased TG2 expression can result in induction of transforming growth factor β1, causing increased synthesis and deposition of matrix proteins, which can be regulated by nitric oxide
    • Telci, D., Collighan, R. J., Basaga, H., and Griffin, M. (2009) Increased TG2 expression can result in induction of transforming growth factor β1, 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.