메뉴 건너뛰기




Volumn 7, Issue 10, 2012, Pages

Immobilized Metal Affinity Chromatography Co-Purifies TGF-β1 with Histidine-Tagged Recombinant Extracellular Proteins

Author keywords

[No Author keywords available]

Indexed keywords

BONE MORPHOGENETIC PROTEIN 2; MESSENGER RNA; NICKEL; RECOMBINANT FIBRILLIN 1; RECOMBINANT PROTEIN; SMAD2 PROTEIN; SMAD3 PROTEIN; TRANSFORMING GROWTH FACTOR BETA1; UNCLASSIFIED DRUG;

EID: 84868320653     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0048629     Document Type: Article
Times cited : (18)

References (43)
  • 2
    • 0034686077 scopus 로고    scopus 로고
    • Recombinant laminin-8 (alpha(4)beta(1)gamma(1)). Production, purification, and interactions with integrins
    • Kortesmaa J, Yurchenco P, Tryggvason K, (2000) Recombinant laminin-8 (alpha(4)beta(1)gamma(1)). Production, purification, and interactions with integrins. J Biol Chem 275: 14853-14859.
    • (2000) J Biol Chem , vol.275 , pp. 14853-14859
    • Kortesmaa, J.1    Yurchenco, P.2    Tryggvason, K.3
  • 3
    • 34547493570 scopus 로고    scopus 로고
    • Fibulin-5 binds human smooth-muscle cells through alpha5beta1 and alpha4beta1 integrins, but does not support receptor activation
    • Lomas AC, Mellody KT, Freeman LJ, Bax DV, Shuttleworth CA, et al. (2007) Fibulin-5 binds human smooth-muscle cells through alpha5beta1 and alpha4beta1 integrins, but does not support receptor activation. Biochem J 405: 417-428.
    • (2007) Biochem J , vol.405 , pp. 417-428
    • Lomas, A.C.1    Mellody, K.T.2    Freeman, L.J.3    Bax, D.V.4    Shuttleworth, C.A.5
  • 4
    • 34247501749 scopus 로고    scopus 로고
    • LTBP-2 specifically interacts with the amino-terminal region of fibrillin-1 and competes with LTBP-1 for binding to this microfibrillar protein
    • Hirani R, Hanssen E, Gibson MA, (2007) LTBP-2 specifically interacts with the amino-terminal region of fibrillin-1 and competes with LTBP-1 for binding to this microfibrillar protein. Matrix Biol 26: 213-223.
    • (2007) Matrix Biol , vol.26 , pp. 213-223
    • Hirani, R.1    Hanssen, E.2    Gibson, M.A.3
  • 5
    • 0141780878 scopus 로고    scopus 로고
    • Cell adhesion to fibrillin-1 molecules and microfibrils is mediated by alpha5 beta1 and alphav beta3 integrins
    • Bax DV, Bernard SE, Lomas A, Morgan A, Humphries J, et al. (2003) Cell adhesion to fibrillin-1 molecules and microfibrils is mediated by alpha5 beta1 and alphav beta3 integrins. J Biol Chem 278: 34605-34616.
    • (2003) J Biol Chem , vol.278 , pp. 34605-34616
    • Bax, D.V.1    Bernard, S.E.2    Lomas, A.3    Morgan, A.4    Humphries, J.5
  • 6
    • 42949094169 scopus 로고    scopus 로고
    • Making recombinant extracellular matrix proteins
    • Ruggiero F, Koch M, (2008) Making recombinant extracellular matrix proteins. Methods 45: 75-85.
    • (2008) Methods , vol.45 , pp. 75-85
    • Ruggiero, F.1    Koch, M.2
  • 7
    • 0016717761 scopus 로고
    • Metal chelate affinity chromatography, a new approach to protein fractionation
    • Porath J, Carlsson J, Olsson I, Belfrage G, (1975) Metal chelate affinity chromatography, a new approach to protein fractionation. Nature 258: 598-599.
    • (1975) Nature , vol.258 , pp. 598-599
    • Porath, J.1    Carlsson, J.2    Olsson, I.3    Belfrage, G.4
  • 8
    • 0023659137 scopus 로고
    • New metal chelate adsorbent selective for proteins and peptides containing neighbouring histidine residues
    • Hochuli E, Dobeli H, Schacher A, (1987) New metal chelate adsorbent selective for proteins and peptides containing neighbouring histidine residues. J Chromatogr 411: 177-184.
    • (1987) J Chromatogr , vol.411 , pp. 177-184
    • Hochuli, E.1    Dobeli, H.2    Schacher, A.3
  • 9
    • 0025946803 scopus 로고
    • Rapid and efficient purification of native histidine-tagged protein expressed by recombinant vaccinia virus
    • Janknecht R, De MG, Lou J, Hipskind RA, Nordheim A, et al. (1991) Rapid and efficient purification of native histidine-tagged protein expressed by recombinant vaccinia virus. Proc Natl Acad Sci USA 88: 8972-8976.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 8972-8976
    • Janknecht, R.1    De, M.G.2    Lou, J.3    Hipskind, R.A.4    Nordheim, A.5
  • 10
    • 0032484139 scopus 로고    scopus 로고
    • The G3 domain of versican inhibits mesenchymal chondrogenesis via the epidermal growth factor-like motifs
    • Zhang Y, Cao L, Kiani CG, Yang BL, Yang BB, (1998) The G3 domain of versican inhibits mesenchymal chondrogenesis via the epidermal growth factor-like motifs. J Biol Chem 273: 33054-33063.
    • (1998) J Biol Chem , vol.273 , pp. 33054-33063
    • Zhang, Y.1    Cao, L.2    Kiani, C.G.3    Yang, B.L.4    Yang, B.B.5
  • 11
    • 80055086478 scopus 로고    scopus 로고
    • ADAMTSL6beta protein rescues fibrillin-1 microfibril disorder in a Marfan syndrome mouse model through the promotion of fibrillin-1 assembly
    • Saito M, Kurokawa M, Oda M, Oshima M, Tsutsui K, et al. (2011) ADAMTSL6beta protein rescues fibrillin-1 microfibril disorder in a Marfan syndrome mouse model through the promotion of fibrillin-1 assembly. J Biol Chem 286: 38602-38613.
    • (2011) J Biol Chem , vol.286 , pp. 38602-38613
    • Saito, M.1    Kurokawa, M.2    Oda, M.3    Oshima, M.4    Tsutsui, K.5
  • 12
    • 77953530644 scopus 로고    scopus 로고
    • Granulin epithelin precursor: a bone morphogenic protein 2-inducible growth factor that activates Erk1/2 signaling and JunB transcription factor in chondrogenesis
    • Feng JQ, Guo FJ, Jiang BC, Zhang Y, Frenkel S, et al. (2010) Granulin epithelin precursor: a bone morphogenic protein 2-inducible growth factor that activates Erk1/2 signaling and JunB transcription factor in chondrogenesis. FASEB J 24: 1879-1892.
    • (2010) FASEB J , vol.24 , pp. 1879-1892
    • Feng, J.Q.1    Guo, F.J.2    Jiang, B.C.3    Zhang, Y.4    Frenkel, S.5
  • 13
    • 79953221473 scopus 로고    scopus 로고
    • Progranulin promotes neurite outgrowth and neuronal differentiation by regulating GSK-3beta
    • Gao X, Joselin AP, Wang L, Kar A, Ray P, et al. (2010) Progranulin promotes neurite outgrowth and neuronal differentiation by regulating GSK-3beta. Protein Cell 1: 552-562.
    • (2010) Protein Cell , vol.1 , pp. 552-562
    • Gao, X.1    Joselin, A.P.2    Wang, L.3    Kar, A.4    Ray, P.5
  • 14
    • 0034676061 scopus 로고    scopus 로고
    • A novel member of the netrin family, beta-netrin, shares homology with the beta chain of laminin: identification, expression, and functional characterization
    • Koch M, Murrell JR, Hunter DD, Olson PF, Jin W, et al. (2000) A novel member of the netrin family, beta-netrin, shares homology with the beta chain of laminin: identification, expression, and functional characterization. J Cell Biol 151: 221-234.
    • (2000) J Cell Biol , vol.151 , pp. 221-234
    • Koch, M.1    Murrell, J.R.2    Hunter, D.D.3    Olson, P.F.4    Jin, W.5
  • 15
    • 0000351017 scopus 로고
    • Microfibrils: fine filamentous components of the tissue space
    • Low FN, (1962) Microfibrils: fine filamentous components of the tissue space. Anat Rec 142: 131-137.
    • (1962) Anat Rec , vol.142 , pp. 131-137
    • Low, F.N.1
  • 16
    • 0014465980 scopus 로고
    • The elastic fiber: the separation and partial characterization of its macromolecular components
    • Ross R, Bornstein P, (1969) The elastic fiber: the separation and partial characterization of its macromolecular components. J Cell Biol 40: 366-381.
    • (1969) J Cell Biol , vol.40 , pp. 366-381
    • Ross, R.1    Bornstein, P.2
  • 17
    • 0023002893 scopus 로고
    • Fibrillin, a new 350-kD glycoprotein, is a component of extracellular microfibrils
    • Sakai LY, Keene DR, Engvall E, (1986) Fibrillin, a new 350-kD glycoprotein, is a component of extracellular microfibrils. J Cell Biol 103: 2499-2509.
    • (1986) J Cell Biol , vol.103 , pp. 2499-2509
    • Sakai, L.Y.1    Keene, D.R.2    Engvall, E.3
  • 18
    • 18144366620 scopus 로고    scopus 로고
    • HEK293 cell line: a vehicle for the expression of recombinant proteins
    • Thomas P, Smart TG, (2005) HEK293 cell line: a vehicle for the expression of recombinant proteins. J Pharmacol Toxicol Methods 51: 187-200.
    • (2005) J Pharmacol Toxicol Methods , vol.51 , pp. 187-200
    • Thomas, P.1    Smart, T.G.2
  • 19
    • 46649104796 scopus 로고    scopus 로고
    • Targeting of bone morphogenetic protein growth factor complexes to fibrillin
    • Sengle G, Charbonneau NL, Ono RN, Sasaki T, Alvarez J, et al. (2008) Targeting of bone morphogenetic protein growth factor complexes to fibrillin. J Biol Chem 283: 13874-13888.
    • (2008) J Biol Chem , vol.283 , pp. 13874-13888
    • Sengle, G.1    Charbonneau, N.L.2    Ono, R.N.3    Sasaki, T.4    Alvarez, J.5
  • 20
    • 79953144610 scopus 로고    scopus 로고
    • Prodomains of transforming growth factor beta (TGFbeta) superfamily members specify different functions: extracellular matrix interactions and growth factor bioavailability
    • Sengle G, Ono RN, Sasaki T, Sakai LY, (2011) Prodomains of transforming growth factor beta (TGFbeta) superfamily members specify different functions: extracellular matrix interactions and growth factor bioavailability. J Biol Chem 286: 5087-5099.
    • (2011) J Biol Chem , vol.286 , pp. 5087-5099
    • Sengle, G.1    Ono, R.N.2    Sasaki, T.3    Sakai, L.Y.4
  • 21
    • 0023429489 scopus 로고
    • Type 1 transforming growth factor beta: amplified expression and secretion of mature and precursor polypeptides in Chinese hamster ovary cells
    • Gentry LE, Webb NR, Lim GJ, Brunner AM, Ranchalis JE, et al. (1987) Type 1 transforming growth factor beta: amplified expression and secretion of mature and precursor polypeptides in Chinese hamster ovary cells. Mol Cell Biol 7: 3418-3427.
    • (1987) Mol Cell Biol , vol.7 , pp. 3418-3427
    • Gentry, L.E.1    Webb, N.R.2    Lim, G.J.3    Brunner, A.M.4    Ranchalis, J.E.5
  • 22
    • 0023732890 scopus 로고
    • Molecular events in the processing of recombinant type 1 pre-pro-transforming growth factor beta to the mature polypeptide
    • Gentry LE, Lioubin MN, Purchio AF, Marquardt H, (1988) Molecular events in the processing of recombinant type 1 pre-pro-transforming growth factor beta to the mature polypeptide. Mol Cell Biol 8: 4162-4168.
    • (1988) Mol Cell Biol , vol.8 , pp. 4162-4168
    • Gentry, L.E.1    Lioubin, M.N.2    Purchio, A.F.3    Marquardt, H.4
  • 23
    • 0027976521 scopus 로고
    • Latent transforming growth factor-ß1 associates to fibroblast extracellular matrix via latent TGF-ß binding protein
    • Taipale J, Miyazono K, Heldin CH, Keski-Oja J, (1994) Latent transforming growth factor-ß1 associates to fibroblast extracellular matrix via latent TGF-ß binding protein. J Cell Biol 124: 171-181.
    • (1994) J Cell Biol , vol.124 , pp. 171-181
    • Taipale, J.1    Miyazono, K.2    Heldin, C.H.3    Keski-Oja, J.4
  • 24
    • 0025765844 scopus 로고
    • A role of the latent TGF-ß1-binding protein in the assembly and secretion of TGF-ß1
    • Miyazono K, Olofsson A, Colosetti P, Heldin CH, (1991) A role of the latent TGF-ß1-binding protein in the assembly and secretion of TGF-ß1. EMBO J 10: 1091-1101.
    • (1991) EMBO J , vol.10 , pp. 1091-1101
    • Miyazono, K.1    Olofsson, A.2    Colosetti, P.3    Heldin, C.H.4
  • 25
    • 0037439630 scopus 로고    scopus 로고
    • Making sense of latent TGFbeta activation
    • Annes JP, Munger JS, Rifkin DB, (2003) Making sense of latent TGFbeta activation. J Cell Sci 116: 217-224.
    • (2003) J Cell Sci , vol.116 , pp. 217-224
    • Annes, J.P.1    Munger, J.S.2    Rifkin, D.B.3
  • 26
    • 0025129867 scopus 로고
    • Concomitant loss of transforming growth factor (TGF)-beta receptor types I and II in TGF-beta-resistant cell mutants implicates both receptor types in signal transduction
    • Laiho M, Weis MB, Massague J, (1990) Concomitant loss of transforming growth factor (TGF)-beta receptor types I and II in TGF-beta-resistant cell mutants implicates both receptor types in signal transduction. J Biol Chem 265: 18518-18524.
    • (1990) J Biol Chem , vol.265 , pp. 18518-18524
    • Laiho, M.1    Weis, M.B.2    Massague, J.3
  • 27
    • 0026496172 scopus 로고
    • TGF beta signals through a heteromeric protein kinase receptor complex
    • Wrana JL, Attisano L, Carcamo J, Zentella A, Doody J, et al. (1992) TGF beta signals through a heteromeric protein kinase receptor complex. Cell 71: 1003-1014.
    • (1992) Cell , vol.71 , pp. 1003-1014
    • Wrana, J.L.1    Attisano, L.2    Carcamo, J.3    Zentella, A.4    Doody, J.5
  • 29
    • 0029786212 scopus 로고    scopus 로고
    • Receptor-associated Mad homologues synergize as effectors of the TGF-beta response
    • Zhang Y, Feng X, We R, Derynck R, (1996) Receptor-associated Mad homologues synergize as effectors of the TGF-beta response. Nature 383: 168-172.
    • (1996) Nature , vol.383 , pp. 168-172
    • Zhang, Y.1    Feng, X.2    We, R.3    Derynck, R.4
  • 30
    • 0030300115 scopus 로고    scopus 로고
    • MADR2 is a substrate of the TGFbeta receptor and its phosphorylation is required for nuclear accumulation and signaling
    • Macias-Silva M, Abdollah S, Hoodless PA, Pirone R, Attisano L, et al. (1996) MADR2 is a substrate of the TGFbeta receptor and its phosphorylation is required for nuclear accumulation and signaling. Cell 87: 1215-1224.
    • (1996) Cell , vol.87 , pp. 1215-1224
    • Macias-Silva, M.1    Abdollah, S.2    Hoodless, P.A.3    Pirone, R.4    Attisano, L.5
  • 31
    • 0031685620 scopus 로고    scopus 로고
    • TGF-beta signal transduction
    • Massague J, (1998) TGF-beta signal transduction. Annu Rev Biochem 67: 753-791.
    • (1998) Annu Rev Biochem , vol.67 , pp. 753-791
    • Massague, J.1
  • 32
    • 0026066232 scopus 로고
    • Characteristics of an infinite life span diploid human fibroblast cell strain and a near-diploid strain arising from a clone of cells expressing a transfected v-myc oncogene
    • Morgan TL, Yang DJ, Fry DG, Hurlin PJ, Kohler SK, et al. (1991) Characteristics of an infinite life span diploid human fibroblast cell strain and a near-diploid strain arising from a clone of cells expressing a transfected v-myc oncogene. Exp Cell Res 197: 125-136.
    • (1991) Exp Cell Res , vol.197 , pp. 125-136
    • Morgan, T.L.1    Yang, D.J.2    Fry, D.G.3    Hurlin, P.J.4    Kohler, S.K.5
  • 33
    • 0033989847 scopus 로고    scopus 로고
    • Characterisation of fibrillin-1 cDNA clones in a human fibroblast cell line that assembles microfibrils
    • Kettle S, Card CM, Hutchinson S, Sykes B, Handford PA, (2000) Characterisation of fibrillin-1 cDNA clones in a human fibroblast cell line that assembles microfibrils. Int J Biochem Cell Biol 32: 201-214.
    • (2000) Int J Biochem Cell Biol , vol.32 , pp. 201-214
    • Kettle, S.1    Card, C.M.2    Hutchinson, S.3    Sykes, B.4    Handford, P.A.5
  • 34
    • 0035955677 scopus 로고    scopus 로고
    • MAGP-1, Protein interaction studies with tropoelastin and fibrillin-1
    • Jensen SA, Reinhardt DP, Gibson MA, Weiss AS, (2001) MAGP-1, Protein interaction studies with tropoelastin and fibrillin-1. J Biol Chem 276: 39661-39666.
    • (2001) J Biol Chem , vol.276 , pp. 39661-39666
    • Jensen, S.A.1    Reinhardt, D.P.2    Gibson, M.A.3    Weiss, A.S.4
  • 35
    • 0029761338 scopus 로고    scopus 로고
    • Fibrillin-1 and fibulin-2 interact and are colocalized in some tissues
    • Reinhardt DP, Sasaki T, Dzamba BJ, Keene DR, Chu ML, et al. (1996) Fibrillin-1 and fibulin-2 interact and are colocalized in some tissues. J Biol Chem 271: 19489-19496.
    • (1996) J Biol Chem , vol.271 , pp. 19489-19496
    • Reinhardt, D.P.1    Sasaki, T.2    Dzamba, B.J.3    Keene, D.R.4    Chu, M.L.5
  • 36
    • 77956276068 scopus 로고    scopus 로고
    • Staining proteins in gels with silver nitrate
    • pdb.prot4727
    • Simpson RJ, (2007) Staining proteins in gels with silver nitrate. Cold Spring Harb Protoc 2007: pdb.prot4727.
    • (2007) Cold Spring Harb Protoc , vol.2007
    • Simpson, R.J.1
  • 37
    • 0037184979 scopus 로고    scopus 로고
    • Homo- and heterotypic fibrillin-1 and -2 interactions constitute the basis for the assembly of microfibrils
    • Lin G, Tiedemann K, Vollbrandt T, Peters H, Bätge B, et al. (2002) Homo- and heterotypic fibrillin-1 and-2 interactions constitute the basis for the assembly of microfibrils. J Biol Chem 277: 50795-50804.
    • (2002) J Biol Chem , vol.277 , pp. 50795-50804
    • Lin, G.1    Tiedemann, K.2    Vollbrandt, T.3    Peters, H.4    Bätge, B.5
  • 38
    • 2142850468 scopus 로고    scopus 로고
    • Molecular basis of elastic fiber formation. Critical interactions and a tropoelastin-fibrillin-1 cross-link
    • Rock MJ, Cain SA, Freeman LJ, Morgan A, Mellody K, et al. (2004) Molecular basis of elastic fiber formation. Critical interactions and a tropoelastin-fibrillin-1 cross-link. J Biol Chem 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
  • 39
    • 67650529853 scopus 로고    scopus 로고
    • Latent transforming growth factor beta-binding proteins and fibulins compete for fibrillin-1 and exhibit exquisite specificities in binding sites
    • Ono RN, Sengle G, Charbonneau NL, Carlberg V, Bachinger HP, et al. (2009) Latent transforming growth factor beta-binding proteins and fibulins compete for fibrillin-1 and exhibit exquisite specificities in binding sites. J Biol Chem 284: 16872-16881.
    • (2009) J Biol Chem , vol.284 , pp. 16872-16881
    • Ono, R.N.1    Sengle, G.2    Charbonneau, N.L.3    Carlberg, V.4    Bachinger, H.P.5
  • 40
    • 0037462678 scopus 로고    scopus 로고
    • Latent transforming growth factor beta-binding protein 1 interacts with fibrillin and is a microfibril-associated protein
    • Isogai Z, Ono RN, Ushiro S, Keene DR, Chen Y, et al. (2003) Latent transforming growth factor beta-binding protein 1 interacts with fibrillin and is a microfibril-associated protein. J Biol Chem 278: 2750-2757.
    • (2003) J Biol Chem , vol.278 , pp. 2750-2757
    • Isogai, Z.1    Ono, R.N.2    Ushiro, S.3    Keene, D.R.4    Chen, Y.5
  • 41
    • 54449085747 scopus 로고    scopus 로고
    • Deficiency in microfibril-associated glycoprotein-1 leads to complex phenotypes in multiple organ systems
    • Weinbaum JS, Broekelmann TJ, Pierce RA, Werneck CC, Segade F, et al. (2008) Deficiency in microfibril-associated glycoprotein-1 leads to complex phenotypes in multiple organ systems. J Biol Chem 283: 25533-25543.
    • (2008) J Biol Chem , vol.283 , pp. 25533-25543
    • Weinbaum, J.S.1    Broekelmann, T.J.2    Pierce, R.A.3    Werneck, C.C.4    Segade, F.5
  • 42
    • 0024372267 scopus 로고
    • Recombinant TGF-beta 1 is synthesized as a two-component latent complex that shares some structural features with the native platelet latent TGF-beta 1 complex
    • Wakefield LM, Smith DM, Broz S, Jackson M, Levinson AD, et al. (1989) Recombinant TGF-beta 1 is synthesized as a two-component latent complex that shares some structural features with the native platelet latent TGF-beta 1 complex. Growth Factors 1: 203-218.
    • (1989) Growth Factors , vol.1 , pp. 203-218
    • Wakefield, L.M.1    Smith, D.M.2    Broz, S.3    Jackson, M.4    Levinson, A.D.5
  • 43
    • 79959250326 scopus 로고    scopus 로고
    • Latent TGF-beta structure and activation
    • Shi M, Zhu J, Wang R, Chen X, Mi L, et al. (2011) Latent TGF-beta structure and activation. Nature 474: 343-349.
    • (2011) Nature , vol.474 , pp. 343-349
    • Shi, M.1    Zhu, J.2    Wang, R.3    Chen, X.4    Mi, L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.