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Volumn 277, Issue 16, 2010, Pages 3343-3352

Direct integration of cell-free-synthesized connexin-43 into liposomes and hemichannel formation

Author keywords

cell free membrane protein synthesis; chaperone like function for hemichannels; connexin; liposome; membrane protein orientation

Indexed keywords

CONNEXIN 43; LIPOSOME;

EID: 77955246394     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2010.07736.x     Document Type: Article
Times cited : (63)

References (40)
  • 1
    • 0031954925 scopus 로고    scopus 로고
    • Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms
    • Wallin E Heijne GV (1998) Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms. Protein Sci 7, 1029 1038.
    • (1998) Protein Sci , vol.7 , pp. 1029-1038
    • Wallin, E.1    Heijne, G.V.2
  • 2
    • 0029101114 scopus 로고
    • Reconstitution of membrane proteins into liposomes: Application to energy-transducing membrane proteins
    • Rigaud JL, Pitard B Levy D (1995) Reconstitution of membrane proteins into liposomes: application to energy-transducing membrane proteins. Biochim Biophys Acta 1231, 223 246.
    • (1995) Biochim Biophys Acta , vol.1231 , pp. 223-246
    • Rigaud, J.L.1    Pitard, B.2    Levy, D.3
  • 3
    • 28244458078 scopus 로고    scopus 로고
    • Evaluation of detergents for the soluble expression of α-helical and β-barrel-type integral membrane proteins by a preparative scale individual cell-free expression system
    • Klammt C, Schwarz D, Fendler K, Haase W, Dötsch V Bernhard F (2005) Evaluation of detergents for the soluble expression of α-helical and β-barrel-type integral membrane proteins by a preparative scale individual cell-free expression system. FEBS J 272, 6024 6038.
    • (2005) FEBS J , vol.272 , pp. 6024-6038
    • Klammt, C.1    Schwarz, D.2    Fendler, K.3    Haase, W.4    Dötsch, V.5    Bernhard, F.6
  • 4
    • 33748307399 scopus 로고    scopus 로고
    • Cell-free expression as an emerging technique for the large scale production of integral membrane protein
    • Klammt C, Schwarz D, Löhr F, Schneider B, Dötsch V Bernhard F (2006) Cell-free expression as an emerging technique for the large scale production of integral membrane protein. FEBS J 273, 4141 4153.
    • (2006) FEBS J , vol.273 , pp. 4141-4153
    • Klammt, C.1    Schwarz, D.2    Löhr, F.3    Schneider, B.4    Dötsch, V.5    Bernhard, F.6
  • 5
    • 34347391677 scopus 로고    scopus 로고
    • Functional analysis of cell-free-produced human endothelin B receptor reveals transmembrane segment 1 as an essential area for ET-1 binding and homodimer formation
    • Klammt C, Srivastava A, Eifler N, Junge F, Beyermann M, Schwarz D, Michel H, Doetsch V Bernhard F (2007) Functional analysis of cell-free-produced human endothelin B receptor reveals transmembrane segment 1 as an essential area for ET-1 binding and homodimer formation. FEBS J 274, 3257 3269.
    • (2007) FEBS J , vol.274 , pp. 3257-3269
    • Klammt, C.1    Srivastava, A.2    Eifler, N.3    Junge, F.4    Beyermann, M.5    Schwarz, D.6    Michel, H.7    Doetsch, V.8    Bernhard, F.9
  • 7
    • 54049126868 scopus 로고    scopus 로고
    • Wheat germ cell-free translation, purification, and assembly of a functional human stearoyl-CoA desaturase complex
    • Goren MA Fox BG (2008) Wheat germ cell-free translation, purification, and assembly of a functional human stearoyl-CoA desaturase complex. Protein Expr Purif 62, 172 178.
    • (2008) Protein Expr Purif , vol.62 , pp. 172-178
    • Goren, M.A.1    Fox, B.G.2
  • 8
    • 34447630299 scopus 로고    scopus 로고
    • Functional cell-free synthesis of a seven helix membrane protein: In situ insertion of bacteriorhodopsin into liposomes
    • Kalmbach R, Chizhov I, Schumacher MC, Friedrich T, Bamberg E Engelhard M (2007) Functional cell-free synthesis of a seven helix membrane protein: in situ insertion of bacteriorhodopsin into liposomes. J Mol Biol 371, 621 629.
    • (2007) J Mol Biol , vol.371 , pp. 621-629
    • Kalmbach, R.1    Chizhov, I.2    Schumacher, M.C.3    Friedrich, T.4    Bamberg, E.5    Engelhard, M.6
  • 10
  • 11
    • 0030028301 scopus 로고    scopus 로고
    • The gap junction communication channel
    • Kumar NM Gilula NB (1996) The gap junction communication channel. Cell 83, 381 388.
    • (1996) Cell , vol.83 , pp. 381-388
    • Kumar, N.M.1    Gilula, N.B.2
  • 12
  • 13
    • 0028077475 scopus 로고
    • Membrane insertion of gap junction connexins: Polytopic channel forming membrane proteins
    • Falk MM, Kumar NM Gilula NB (1994) Membrane insertion of gap junction connexins: polytopic channel forming membrane proteins. J Cell Biol 127, 343 355.
    • (1994) J Cell Biol , vol.127 , pp. 343-355
    • Falk, M.M.1    Kumar, N.M.2    Gilula, N.B.3
  • 14
    • 0029936545 scopus 로고    scopus 로고
    • Membrane integration of in vitro-translated gap junction proteins: Co- and post-translational mechanisms
    • Zhang JT, Chen M, Foote CI Nicholson BJ (1996) Membrane integration of in vitro-translated gap junction proteins: co- and post-translational mechanisms. Mol Biol Cell 7, 471 482.
    • (1996) Mol Biol Cell , vol.7 , pp. 471-482
    • Zhang, J.T.1    Chen, M.2    Foote, C.I.3    Nicholson, B.J.4
  • 15
    • 0033560718 scopus 로고    scopus 로고
    • Synthesis and assembly of connexins in vitro into homomeric and heteromeric functional gap junction hemichannels
    • Ahmad S, Diez JA, George CH Evans WH (1999) Synthesis and assembly of connexins in vitro into homomeric and heteromeric functional gap junction hemichannels. Biochem J 339, 247 253.
    • (1999) Biochem J , vol.339 , pp. 247-253
    • Ahmad, S.1    Diez, J.A.2    George, C.H.3    Evans, W.H.4
  • 16
    • 0036683707 scopus 로고    scopus 로고
    • Post-translational integration and oligomerization of connexin 26 in plasma membranes and evidence of formation of membrane pores: Implications for the assembly of gap junctions
    • Ahmad S Evans WH (2002) Post-translational integration and oligomerization of connexin 26 in plasma membranes and evidence of formation of membrane pores: implications for the assembly of gap junctions. Biochem J 365, 693 699.
    • (2002) Biochem J , vol.365 , pp. 693-699
    • Ahmad, S.1    Evans, W.H.2
  • 17
    • 67349228772 scopus 로고    scopus 로고
    • Direct formation of proteo-liposomes by in vitro synthesis and cellular cytosolic delivery with connexin-expressing liposomes
    • Kaneda M, Nomura SM, Ichinose S, Kondo S, Nakahama K, Akiyoshi K Morita I (2009) Direct formation of proteo-liposomes by in vitro synthesis and cellular cytosolic delivery with connexin-expressing liposomes. Biomaterials 30, 3971 3977.
    • (2009) Biomaterials , vol.30 , pp. 3971-3977
    • Kaneda, M.1    Nomura, S.M.2    Ichinose, S.3    Kondo, S.4    Nakahama, K.5    Akiyoshi, K.6    Morita, I.7
  • 18
    • 0027298688 scopus 로고
    • Possible role of phosphorylation in the function of chicken MyoD1
    • Nakamura S (1993) Possible role of phosphorylation in the function of chicken MyoD1. J Biol Chem 268, 11670 11677.
    • (1993) J Biol Chem , vol.268 , pp. 11670-11677
    • Nakamura, S.1
  • 20
    • 33748307400 scopus 로고    scopus 로고
    • Cell-free translation systems for protein engineering
    • Shimizu Y, Kuruma Y, Ying BW, Umekage S Ueda T (2006) Cell-free translation systems for protein engineering. FEBS J 273, 4133 4140.
    • (2006) FEBS J , vol.273 , pp. 4133-4140
    • Shimizu, Y.1    Kuruma, Y.2    Ying, B.W.3    Umekage, S.4    Ueda, T.5
  • 21
    • 23244445172 scopus 로고    scopus 로고
    • Development of a minimal cell-free translation system for the synthesis of presecretory and integral membrane proteins
    • Kuruma Y, Nishiyama K, Shimizu Y, Müller M Ueda T (2005) Development of a minimal cell-free translation system for the synthesis of presecretory and integral membrane proteins. Biotechnol Prog 21, 1243 1251.
    • (2005) Biotechnol Prog , vol.21 , pp. 1243-1251
    • Kuruma, Y.1    Nishiyama, K.2    Shimizu, Y.3    Müller, M.4    Ueda, T.5
  • 23
    • 59249084001 scopus 로고    scopus 로고
    • A synthetic biology approach to the construction of membrane proteins in semi-synthetic minimal cells
    • Kuruma Y, Stano P, Ueda T Luisi PL (2009) A synthetic biology approach to the construction of membrane proteins in semi-synthetic minimal cells. Biochim Biophys Acta 1788, 567 574.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 567-574
    • Kuruma, Y.1    Stano, P.2    Ueda, T.3    Luisi, P.L.4
  • 24
    • 0031278523 scopus 로고    scopus 로고
    • Refolding of carbonic anhydrase assisted by 1-palmitoyl-2-oleoyl-sn- glycero-3-phosphocholine liposomes
    • Kuboi R, Yoshimoto M, Walde P Luisi PL (1997) Refolding of carbonic anhydrase assisted by 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine liposomes. Biotechnol Prog 13, 828 836.
    • (1997) Biotechnol Prog , vol.13 , pp. 828-836
    • Kuboi, R.1    Yoshimoto, M.2    Walde, P.3    Luisi, P.L.4
  • 25
    • 0033006157 scopus 로고    scopus 로고
    • Oxidative refolding of denatured/reduced lysozyme utilizing the chaperone-like function of liposomes and immobilized liposome chromatography
    • Yoshimoto M Kuboi R (1999) Oxidative refolding of denatured/reduced lysozyme utilizing the chaperone-like function of liposomes and immobilized liposome chromatography. Biotechnol Prog 15, 480 487.
    • (1999) Biotechnol Prog , vol.15 , pp. 480-487
    • Yoshimoto, M.1    Kuboi, R.2
  • 26
    • 0035849794 scopus 로고    scopus 로고
    • Connexin43 suppresses proliferation of osteosarcoma U2OS cells through post-transcriptional regulation of p27
    • Zhang YW, Morita I, Ikeda M, Ma KW Murota S (2001) Connexin43 suppresses proliferation of osteosarcoma U2OS cells through post-transcriptional regulation of p27. Oncogene 20, 4138 4149.
    • (2001) Oncogene , vol.20 , pp. 4138-4149
    • Zhang, Y.W.1    Morita, I.2    Ikeda, M.3    Ma, K.W.4    Murota, S.5
  • 27
    • 0023644895 scopus 로고
    • Topological analysis of the major protein in isolated intact rat liver gap junctions and gap junction-derived single membrane structures
    • Zimmer DB, Green CR, Evans WH Gilula NB (1987) Topological analysis of the major protein in isolated intact rat liver gap junctions and gap junction-derived single membrane structures. J Biol Chem 262, 7751 7763.
    • (1987) J Biol Chem , vol.262 , pp. 7751-7763
    • Zimmer, D.B.1    Green, C.R.2    Evans, W.H.3    Gilula, N.B.4
  • 28
    • 0035886760 scopus 로고    scopus 로고
    • Green fluorescent protein rendered susceptible to proteolysis: Positions for protease-sensitive insertions
    • Chiang CF, Okou DT, Griffin TB, Verret CR Williams MNV (2001) Green fluorescent protein rendered susceptible to proteolysis: positions for protease-sensitive insertions. Arch Biochem Biophys 394, 229 235.
    • (2001) Arch Biochem Biophys , vol.394 , pp. 229-235
    • Chiang, C.F.1    Okou, D.T.2    Griffin, T.B.3    Verret, C.R.4    Williams, M.N.V.5
  • 29
    • 33847639732 scopus 로고    scopus 로고
    • Applications of phospholipid bilayer nanodiscs in the study of membranes and membrane proteins
    • Nath A, Atkins WM Sligar SG (2007) Applications of phospholipid bilayer nanodiscs in the study of membranes and membrane proteins. Biochemistry 46, 2059 2069.
    • (2007) Biochemistry , vol.46 , pp. 2059-2069
    • Nath, A.1    Atkins, W.M.2    Sligar, S.G.3
  • 31
    • 0027364529 scopus 로고
    • Multisubunit assembly of an integral plasma membrane channel protein, gap junction connexin43, occurs after exit from the ER
    • Musil LS Goodenough DA (1993) Multisubunit assembly of an integral plasma membrane channel protein, gap junction connexin43, occurs after exit from the ER. Cell 74, 1065 1077.
    • (1993) Cell , vol.74 , pp. 1065-1077
    • Musil, L.S.1    Goodenough, D.A.2
  • 32
    • 0029096749 scopus 로고
    • Physical characterization of gap junction membrane connexons (hemi-channels) isolated from rat liver
    • Cascio M, Kumar NM, Safarik R Gilula NB (1993) Physical characterization of gap junction membrane connexons (hemi-channels) isolated from rat liver. J Biol Chem 270, 18643 18648.
    • (1993) J Biol Chem , vol.270 , pp. 18643-18648
    • Cascio, M.1    Kumar, N.M.2    Safarik, R.3    Gilula, N.B.4
  • 33
    • 0000210839 scopus 로고    scopus 로고
    • Gating connexin 43 channels reconstituted in lipid vesicles by mitogen-activated protein kinase phosphorylation
    • Kim DY, Kam Y, Koo SK Joe CO (1999) Gating connexin 43 channels reconstituted in lipid vesicles by mitogen-activated protein kinase phosphorylation. J Biol Chem 274, 5581 5587.
    • (1999) J Biol Chem , vol.274 , pp. 5581-5587
    • Kim, D.Y.1    Kam, Y.2    Koo, S.K.3    Joe, C.O.4
  • 34
    • 34247644332 scopus 로고    scopus 로고
    • Change in permeant size selectivity by phosphorylation of connexin 43 gap-junctional hemichannlels by PKC
    • Bao X, Lee SC, Reuss L Altenberg GA (2007) Change in permeant size selectivity by phosphorylation of connexin 43 gap-junctional hemichannlels by PKC. Proc Natl Acad Sci USA 104, 4919 4924.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 4919-4924
    • Bao, X.1    Lee, S.C.2    Reuss, L.3    Altenberg, G.A.4
  • 35
    • 0017349804 scopus 로고
    • A simple fluorescent method to determine complement-mediated liposome immune lysis
    • Smolarsky D, Teitelbaum D, Sela M Gitler C (1977) A simple fluorescent method to determine complement-mediated liposome immune lysis. J Immunol Methods 15, 255 265.
    • (1977) J Immunol Methods , vol.15 , pp. 255-265
    • Smolarsky, D.1    Teitelbaum, D.2    Sela, M.3    Gitler, C.4
  • 36
    • 0026702457 scopus 로고
    • Determination of ion permeability by fluorescence quenching
    • Garcia AM (1992) Determination of ion permeability by fluorescence quenching. Methods Enzymol 207, 501 510.
    • (1992) Methods Enzymol , vol.207 , pp. 501-510
    • Garcia, A.M.1
  • 38
    • 0030928440 scopus 로고    scopus 로고
    • Protein-induced leakage and membrane destabilization of phosphatidylcholine and phosphatidylserine liposomes
    • Dimitrova MN Matsumura H (1997) Protein-induced leakage and membrane destabilization of phosphatidylcholine and phosphatidylserine liposomes. Colloids Surf B Biointerfaces 8, 287 294.
    • (1997) Colloids Surf B Biointerfaces , vol.8 , pp. 287-294
    • Dimitrova, M.N.1    Matsumura, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.