메뉴 건너뛰기




Volumn 31, Issue 16, 2010, Pages 4600-4608

Characterization of amine donor and acceptor sites for tissue type transglutaminase using a sequence from the C-terminus of human fibrillin-1 and the N-terminus of osteonectin

Author keywords

Collagen crosslinking; Extracellular matrix; Natural probes; Specificity; Tissue targeting; Transglutaminase

Indexed keywords

COLLAGEN CROSSLINKING; EXTRACELLULAR MATRICES; EXTRACELLULAR MATRIX; NATURAL PROBES; TRANSGLUTAMINASES;

EID: 77950050368     PISSN: 01429612     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biomaterials.2010.01.094     Document Type: Article
Times cited : (6)

References (40)
  • 1
    • 0026338017 scopus 로고
    • Transglutaminases: multifunctional cross-linking enzymes that stabilize tissues
    • Greenberg C., Birckbichler P., Rice R. Transglutaminases: multifunctional cross-linking enzymes that stabilize tissues. FASEB J 1991, 5:3071-3077.
    • (1991) FASEB J , vol.5 , pp. 3071-3077
    • Greenberg, C.1    Birckbichler, P.2    Rice, R.3
  • 2
    • 0027516486 scopus 로고
    • Expression of tissue transglutaminase in skeletal tissues correlates with events of terminal differentiation of chondrocytes
    • Aeschlimann D., Wetterwald A., Fleisch H., Paulsson M. Expression of tissue transglutaminase in skeletal tissues correlates with events of terminal differentiation of chondrocytes. J Cell Biol 1993, 120:1461-1470.
    • (1993) J Cell Biol , vol.120 , pp. 1461-1470
    • Aeschlimann, D.1    Wetterwald, A.2    Fleisch, H.3    Paulsson, M.4
  • 3
    • 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., et al. Gh: a GTP-binding protein with transglutaminase activity and receptor signaling function. Science 1994, 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
  • 4
    • 0023159034 scopus 로고
    • Induction and activation of tissue transglutaminase during programmed cell death
    • Fesus L., Thomazy V., Falus A. Induction and activation of tissue transglutaminase during programmed cell death. FEBS Lett 1987, 224:104-108.
    • (1987) FEBS Lett , vol.224 , pp. 104-108
    • Fesus, L.1    Thomazy, V.2    Falus, A.3
  • 5
    • 0036901574 scopus 로고    scopus 로고
    • Transglutaminases: nature's biological glues
    • Griffin M., Ca sadio R., Bergamini C.M. Transglutaminases: nature's biological glues. Biochem J 2002, 368:377-396.
    • (2002) Biochem J , vol.368 , pp. 377-396
    • Griffin, M.1    Ca sadio, R.2    Bergamini, C.M.3
  • 6
    • 0031228921 scopus 로고    scopus 로고
    • Protein cross-linking mediated by tissue transglutaminase correlates with the maturation of extracellular matrices during lung development
    • Schittny J.C., Paulsson M., Vallan C., Burri P.H., Kedei N., Aeschlimann D. Protein cross-linking mediated by tissue transglutaminase correlates with the maturation of extracellular matrices during lung development. Am J Respir Cell Mol Biol 1997, 17:334-343.
    • (1997) Am J Respir Cell Mol Biol , vol.17 , pp. 334-343
    • Schittny, J.C.1    Paulsson, M.2    Vallan, C.3    Burri, P.H.4    Kedei, N.5    Aeschlimann, D.6
  • 7
    • 2142850468 scopus 로고    scopus 로고
    • Molecular basis of elastic fiber formation: critical interactions and a tropoelastin fibrillin-1 cross-link
    • Rock M.J., Cain S.A., Freeman L.J., Morgan A., Mellody K., Marson A., et al. Molecular basis of elastic fiber formation: critical interactions and a tropoelastin fibrillin-1 cross-link. J Biol Chem 2004, 279:23748-23758.
    • (2004) J Biol Chem , vol.279 , pp. 23748-23758
    • Rock, M.J.1    Cain, S.A.2    Freeman, L.J.3    Morgan, A.4    Mellody, K.5    Marson, A.6
  • 8
    • 23044517305 scopus 로고    scopus 로고
    • Coacervation is promoted by molecular interactions between the PF2 segment of fibrillin-1 and the domain 4 region of tropoelastin
    • Clarke A.W., Wise S.G., Cain S.A., Kielty C.M., Weiss A.S. Coacervation is promoted by molecular interactions between the PF2 segment of fibrillin-1 and the domain 4 region of tropoelastin. Biochemistry 2005, 44:10271-10281.
    • (2005) Biochemistry , vol.44 , pp. 10271-10281
    • Clarke, A.W.1    Wise, S.G.2    Cain, S.A.3    Kielty, C.M.4    Weiss, A.S.5
  • 9
    • 0031470781 scopus 로고    scopus 로고
    • Alignment of fibrillin molecules in elastic microfibrils is defined by transglutaminase-derived cross-links
    • Qian R., Glanville R. Alignment of fibrillin molecules in elastic microfibrils is defined by transglutaminase-derived cross-links. Biochemistry 1997, 36:15841-15847.
    • (1997) Biochemistry , vol.36 , pp. 15841-15847
    • Qian, R.1    Glanville, R.2
  • 10
    • 0029783016 scopus 로고    scopus 로고
    • Morphology and biomechanics of the microfibrillar network of sea cucumber dermis
    • Thurmond F.A., Trotter J.A. Morphology and biomechanics of the microfibrillar network of sea cucumber dermis. J Exp Biol 1996, 199:1817-1828.
    • (1996) J Exp Biol , vol.199 , pp. 1817-1828
    • Thurmond, F.A.1    Trotter, J.A.2
  • 11
    • 0026612802 scopus 로고
    • 726 in nidogen as the amine acceptor in transglutaminase-catalyzed cross-linking of laminin-nidogen complexes
    • 726 in nidogen as the amine acceptor in transglutaminase-catalyzed cross-linking of laminin-nidogen complexes. J Biol Chem 1992, 267:11316-11321.
    • (1992) J Biol Chem , vol.267 , pp. 11316-11321
    • Aeschlimann, D.1    Paulsson, M.2    Mann, K.3
  • 12
    • 0026522680 scopus 로고
    • Factors that govern the specificity of transglutaminase-catalysed modification of proteins and peptides
    • Coussons P.J., Price N.C., Kelly S.M., Smith B., Sawyer L. Factors that govern the specificity of transglutaminase-catalysed modification of proteins and peptides. Biochem J 1992, 282:929-930.
    • (1992) Biochem J , vol.282 , pp. 929-930
    • Coussons, P.J.1    Price, N.C.2    Kelly, S.M.3    Smith, B.4    Sawyer, L.5
  • 13
    • 0028069414 scopus 로고
    • Lys-17 is the amine-donor substrate site for transglutaminase in beta βA3-crystallin
    • Groenen P.J., Grootjans J.J., Lubsen N.H., Bloe mendal H., de Jong W.W. Lys-17 is the amine-donor substrate site for transglutaminase in beta βA3-crystallin. J Biol Chem 1994, 269:831-833.
    • (1994) J Biol Chem , vol.269 , pp. 831-833
    • Groenen, P.J.1    Grootjans, J.J.2    Lubsen, N.H.3    Bloe mendal, H.4    de Jong, W.W.5
  • 14
    • 0025793355 scopus 로고
    • Mass spectrometric identification of the amino donor and acceptor sites in a transglutaminase protein substrate secreted from rat seminal vesicles
    • Porta R., Esposito C., Metafora S., Malorni A., Pucci P., Siciliano R., et al. Mass spectrometric identification of the amino donor and acceptor sites in a transglutaminase protein substrate secreted from rat seminal vesicles. Biochemistry 1991, 30:3114-3120.
    • (1991) Biochemistry , vol.30 , pp. 3114-3120
    • Porta, R.1    Esposito, C.2    Metafora, S.3    Malorni, A.4    Pucci, P.5    Siciliano, R.6
  • 15
    • 0023681956 scopus 로고
    • β-Endorphin modification by transglutaminase in vitro: identification by FAB/MS of glutamine-11 and lysine-29 as acyl donor and acceptor sites
    • Pucci P., Malorni A., Marino G., Metafora S., Esposito C., Porta R. β-Endorphin modification by transglutaminase in vitro: identification by FAB/MS of glutamine-11 and lysine-29 as acyl donor and acceptor sites. Biochem Biophys Res Commun 1988, 154:735-740.
    • (1988) Biochem Biophys Res Commun , vol.154 , pp. 735-740
    • Pucci, P.1    Malorni, A.2    Marino, G.3    Metafora, S.4    Esposito, C.5    Porta, R.6
  • 16
    • 0027289153 scopus 로고
    • Cross-linking of a synthetic partial-length (1-28) peptide of the Alzheimer βA4 amyloid protein by transglutaminase
    • Ikura K., Takahata K., Sasaki R. Cross-linking of a synthetic partial-length (1-28) peptide of the Alzheimer βA4 amyloid protein by transglutaminase. FEBS Lett 1993, 326:109-111.
    • (1993) FEBS Lett , vol.326 , pp. 109-111
    • Ikura, K.1    Takahata, K.2    Sasaki, R.3
  • 17
    • 0027524175 scopus 로고
    • Structural and functional similarities of bovine alpha-crystallin and mouse small heat-shock protein. A family of chaperones
    • Merck K.B., Groenen P.J., Voorter C.E., Haard-Hoekman W.A.D., Horwitzt H.B., de Jong W.W. Structural and functional similarities of bovine alpha-crystallin and mouse small heat-shock protein. A family of chaperones. J Biol Chem 1993, 268:1046-1052.
    • (1993) J Biol Chem , vol.268 , pp. 1046-1052
    • Merck, K.B.1    Groenen, P.J.2    Voorter, C.E.3    Haard-Hoekman, W.A.D.4    Horwitzt, H.B.5    de Jong, W.W.6
  • 18
    • 0027282230 scopus 로고
    • Human-immunodeficiency-virus transmembrane glycoprotein gp41 is an amino acceptor and donor substrate for transglutaminase in vitro
    • Mariniello L., Esposito C., Pierro P.D., Cozzolino A., Pucci P., Porta R. Human-immunodeficiency-virus transmembrane glycoprotein gp41 is an amino acceptor and donor substrate for transglutaminase in vitro. Eur J Biochem 1993, 215:99-104.
    • (1993) Eur J Biochem , vol.215 , pp. 99-104
    • Mariniello, L.1    Esposito, C.2    Pierro, P.D.3    Cozzolino, A.4    Pucci, P.5    Porta, R.6
  • 19
    • 0026585827 scopus 로고
    • The carboxy-terminal lysine of αβ-crystallin is an amine-donor substrate for tissue transglutaminase
    • Groenen P.J.T.A., Bloemendal H., de Jong W.W. The carboxy-terminal lysine of αβ-crystallin is an amine-donor substrate for tissue transglutaminase. Eur J Biochem 1992, 205:671-674.
    • (1992) Eur J Biochem , vol.205 , pp. 671-674
    • Groenen, P.J.T.A.1    Bloemendal, H.2    de Jong, W.W.3
  • 20
    • 0028832277 scopus 로고
    • Two adjacent N-terminal glutamines of BM-40 (Osteonectin, SPARC) act as amine acceptor sites in transglutaminase-catalyzed modification
    • Hohenadl C., Mann K., Mayer U., Timpl R., Paulsson M., Aeschlimann D. Two adjacent N-terminal glutamines of BM-40 (Osteonectin, SPARC) act as amine acceptor sites in transglutaminase-catalyzed modification. J Biol Chem 1995, 270:23415-23420.
    • (1995) J Biol Chem , vol.270 , pp. 23415-23420
    • Hohenadl, C.1    Mann, K.2    Mayer, U.3    Timpl, R.4    Paulsson, M.5    Aeschlimann, D.6
  • 21
    • 0031788996 scopus 로고    scopus 로고
    • A novel in situ method for the detection of deficient transglutaminase activity in the skin
    • Raghunath M., Hennies H.C., Velten F., Wiebe V., Steinert P.M., Reis A., et al. A novel in situ method for the detection of deficient transglutaminase activity in the skin. Arch Dermatol Res 1998, 290:621-627.
    • (1998) Arch Dermatol Res , vol.290 , pp. 621-627
    • Raghunath, M.1    Hennies, H.C.2    Velten, F.3    Wiebe, V.4    Steinert, P.M.5    Reis, A.6
  • 23
    • 0015156377 scopus 로고
    • Transamidating enzymes: I. Rapid chromatographic assays
    • Lorand L., Campbell L.K. Transamidating enzymes: I. Rapid chromatographic assays. Anal Biochem 1971, 44:207-220.
    • (1971) Anal Biochem , vol.44 , pp. 207-220
    • Lorand, L.1    Campbell, L.K.2
  • 25
    • 0036000156 scopus 로고    scopus 로고
    • Formation of fibrinogen-based hydrogels using phototriggerable diplasmalogen liposomes
    • Zhang Z.-Y., Shum P., Yates M., Messersmith P.B., Thompson D.H. Formation of fibrinogen-based hydrogels using phototriggerable diplasmalogen liposomes. Bioconjugate Chem 2002, 13:640-646.
    • (2002) Bioconjugate Chem , vol.13 , pp. 640-646
    • Zhang, Z.-Y.1    Shum, P.2    Yates, M.3    Messersmith, P.B.4    Thompson, D.H.5
  • 26
    • 0025195103 scopus 로고
    • Labeling of e{open}-lysine crosslinking sites in proteins with peptide substrates of factor XIIIa and transglutaminase
    • Parameswaran K.N., Velasco P.T., Wilson J., Lorand L. Labeling of e{open}-lysine crosslinking sites in proteins with peptide substrates of factor XIIIa and transglutaminase. Proc Natl Acad Sci USA 1990, 87:8472-8475.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 8472-8475
    • Parameswaran, K.N.1    Velasco, P.T.2    Wilson, J.3    Lorand, L.4
  • 27
    • 0037317032 scopus 로고    scopus 로고
    • Transglutaminases: crosslinking enzymes with pleiotropic functions
    • Lorand L., Graham R.M. Transglutaminases: crosslinking enzymes with pleiotropic functions. Nature Rev Mol Cell Biol 2003, 4:140-156.
    • (2003) Nature Rev Mol Cell Biol , vol.4 , pp. 140-156
    • Lorand, L.1    Graham, R.M.2
  • 28
    • 0026488212 scopus 로고
    • Isolation of transglutaminase-reactive sequences from complex biological systems: a prominent lysine donor sequence in bovine lens
    • Lorand L., Valasco P.T., Murthy S.N.P., Wilson J., Parameswaran K.N. Isolation of transglutaminase-reactive sequences from complex biological systems: a prominent lysine donor sequence in bovine lens. Proc Natl Acad Sci USA 1992, 89:11161-11163.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 11161-11163
    • Lorand, L.1    Valasco, P.T.2    Murthy, S.N.P.3    Wilson, J.4    Parameswaran, K.N.5
  • 29
    • 0023470593 scopus 로고
    • βB1 crystallin is an amine-donor substrate for tissue transglutaminase
    • Mulders J.W.M., Hoekman W.A., Bloemendal H., de Jong W.W. βB1 crystallin is an amine-donor substrate for tissue transglutaminase. Exp Cell Res 1987, 171:296-305.
    • (1987) Exp Cell Res , vol.171 , pp. 296-305
    • Mulders, J.W.M.1    Hoekman, W.A.2    Bloemendal, H.3    de Jong, W.W.4
  • 30
    • 0029147474 scopus 로고
    • Substrate requirements for transglutaminases. Influence of the amino acid residue preceding the amine donor lysine in a native protein
    • Grootjans J.J., Groenen P.J.T.A., de Jong W.W. Substrate requirements for transglutaminases. Influence of the amino acid residue preceding the amine donor lysine in a native protein. J Biol Chem 1995, 270:22855-22858.
    • (1995) J Biol Chem , vol.270 , pp. 22855-22858
    • Grootjans, J.J.1    Groenen, P.J.T.A.2    de Jong, W.W.3
  • 31
    • 0028297494 scopus 로고
    • The amine-donor substrate specificity of tissue-type transglutaminase. Influence of amino acid residues flanking the amine-donor lysine residue
    • Groenen P.J.T.A., Smulders R.H.P.H., Peters R.F.R., Grootjans J.J., Ijssel P.R.L.A.V.D., Bloemendal H., et al. The amine-donor substrate specificity of tissue-type transglutaminase. Influence of amino acid residues flanking the amine-donor lysine residue. Eur J Biochem 1994, 220:795-799.
    • (1994) Eur J Biochem , vol.220 , pp. 795-799
    • Groenen, P.J.T.A.1    Smulders, R.H.P.H.2    Peters, R.F.R.3    Grootjans, J.J.4    Ijssel, P.R.L.A.V.D.5    Bloemendal, H.6
  • 32
    • 0032937875 scopus 로고    scopus 로고
    • Carboxy-terminal conversion of profibrillin to fibrillin at a basic site by PACE/furin-like activity required for incorporation in the matrix
    • Raghunath M., Putnam E.A., Ritty T., Hamstra D., Park E.S., Tschodrich-Rotter M., et al. Carboxy-terminal conversion of profibrillin to fibrillin at a basic site by PACE/furin-like activity required for incorporation in the matrix. J Cell Sci 1999, 112:1093-1100.
    • (1999) J Cell Sci , vol.112 , pp. 1093-1100
    • Raghunath, M.1    Putnam, E.A.2    Ritty, T.3    Hamstra, D.4    Park, E.S.5    Tschodrich-Rotter, M.6
  • 34
    • 0034637513 scopus 로고    scopus 로고
    • Cross-linking of plasminogen activator inhibitor 2 and 2-antiplasmin to fibrin(ogen)
    • Ritchie H., Lawrie L.C., Crombie P.W., Mosesson M.W., Booth N.A. Cross-linking of plasminogen activator inhibitor 2 and 2-antiplasmin to fibrin(ogen). J Biol Chem 2000, 275:24915-24920.
    • (2000) J Biol Chem , vol.275 , pp. 24915-24920
    • Ritchie, H.1    Lawrie, L.C.2    Crombie, P.W.3    Mosesson, M.W.4    Booth, N.A.5
  • 35
    • 0033558206 scopus 로고    scopus 로고
    • Revised genomic organization of FBN1 and significance for regulated gene expression
    • Biery N.J., Eldadah Z.A., Moore C.S., Stetten G., Spencer F., Dietz H.C. Revised genomic organization of FBN1 and significance for regulated gene expression. Genomics 1999, 56:70-77.
    • (1999) Genomics , vol.56 , pp. 70-77
    • Biery, N.J.1    Eldadah, Z.A.2    Moore, C.S.3    Stetten, G.4    Spencer, F.5    Dietz, H.C.6
  • 37
    • 0024224559 scopus 로고
    • The glutamine residues reactive in transglutaminase-catalyzed cross-linking of involucrin
    • Simon M., Green H. The glutamine residues reactive in transglutaminase-catalyzed cross-linking of involucrin. J Biol Chem 1988, 263:18093-18098.
    • (1988) J Biol Chem , vol.263 , pp. 18093-18098
    • Simon, M.1    Green, H.2
  • 39
    • 13344260002 scopus 로고    scopus 로고
    • Retinoid-induced differentiation of acute promyelocytic leukemia involves PML-RAR alpha-mediated increase of type II transglutaminase
    • Benedetti L., Grignani F., Scicchitano B., Jetten A., Diverio D., Coco F.L., et al. Retinoid-induced differentiation of acute promyelocytic leukemia involves PML-RAR alpha-mediated increase of type II transglutaminase. Blood 1996, 87:1939-1950.
    • (1996) Blood , vol.87 , pp. 1939-1950
    • Benedetti, L.1    Grignani, F.2    Scicchitano, B.3    Jetten, A.4    Diverio, D.5    Coco, F.L.6
  • 40
    • 42749083406 scopus 로고    scopus 로고
    • Enzymatically crosslinked collagen-mimetic dendrimers that promote integrin-targeted cell adhesion
    • Khew S.T., Yang Q.J., Tong Y.W. Enzymatically crosslinked collagen-mimetic dendrimers that promote integrin-targeted cell adhesion. Biomaterials 2009, 29:3034-3045.
    • (2009) Biomaterials , vol.29 , pp. 3034-3045
    • Khew, S.T.1    Yang, Q.J.2    Tong, Y.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.