메뉴 건너뛰기




Volumn 275, Issue 3, 2008, Pages 515-526

The chaperone and potential mannan-binding lectin (MBL) co-receptor calreticulin interacts with MBL through the binding site for MBL-associated serine proteases

Author keywords

Calreticulin; Chaperone; Collectin; Mannan binding lectin; Serine protease

Indexed keywords

CALRETICULIN; CHAPERONE; COLLECTIN; COMPLEMENT COMPONENT C1Q; MANNAN BINDING LECTIN; MANNAN BINDING LECTIN ASSOCIATED SERINE PROTEINASE; MUTANT PROTEIN; RECEPTOR PROTEIN; STREPTAVIDIN;

EID: 38149115537     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2007.06218.x     Document Type: Article
Times cited : (36)

References (77)
  • 1
    • 0041534400 scopus 로고    scopus 로고
    • Collections and ficolins: Humoral lectins of the innate immune defense
    • Holmskov U, Thiel S Jensenius JC (2003) Collections and ficolins: humoral lectins of the innate immune defense. Annu Rev Immunol 21, 547 578.
    • (2003) Annu Rev Immunol , vol.21 , pp. 547-578
    • Holmskov, U.1    Thiel, S.2    Jensenius, J.C.3
  • 3
    • 1642562871 scopus 로고    scopus 로고
    • The mannose-binding lectin (MBL) route for activation of complement
    • Kojima M, Presanis JS Sim RB (2003) The mannose-binding lectin (MBL) route for activation of complement. Adv Exp Med Biol 535, 229 250.
    • (2003) Adv Exp Med Biol , vol.535 , pp. 229-250
    • Kojima, M.1    Presanis, J.S.2    Sim, R.B.3
  • 4
    • 33644833588 scopus 로고    scopus 로고
    • Collectins: Opsonins for apoptotic cells and regulators of inflammation
    • Stuart LM, Henson PM Vandivier RW (2006) Collectins: opsonins for apoptotic cells and regulators of inflammation. Curr Dir Autoimmun 9, 143 161.
    • (2006) Curr Dir Autoimmun , vol.9 , pp. 143-161
    • Stuart, L.M.1    Henson, P.M.2    Vandivier, R.W.3
  • 6
    • 2542423115 scopus 로고    scopus 로고
    • Mannan-binding lectin - A soluble pattern recognition molecule
    • Gadjeva M, Takahashi K Thiel S (2004) Mannan-binding lectin - a soluble pattern recognition molecule. Mol Immunol 41, 113 121.
    • (2004) Mol Immunol , vol.41 , pp. 113-121
    • Gadjeva, M.1    Takahashi, K.2    Thiel, S.3
  • 7
    • 0022844505 scopus 로고
    • Mannose-binding proteins isolated from rat liver contain carbohydrate-recognition domains linked to collagenous tails. Complete primary structures and homology with pulmonary surfactant apoprotein
    • Drickamer K, Dordal MS Reynolds L (1986) Mannose-binding proteins isolated from rat liver contain carbohydrate-recognition domains linked to collagenous tails. Complete primary structures and homology with pulmonary surfactant apoprotein. J Biol Chem 261, 6878 6887.
    • (1986) J Biol Chem , vol.261 , pp. 6878-6887
    • Drickamer, K.1    Dordal, M.S.2    Reynolds, L.3
  • 8
    • 15744379234 scopus 로고    scopus 로고
    • Characterization of the oligomer structure of recombinant human mannan-binding lectin
    • Jensen PH, Weilguny D, Matthiesen F, Mcguire KA, Shi L Hojrup P (2005) Characterization of the oligomer structure of recombinant human mannan-binding lectin. J Biol Chem 280, 11043 11051.
    • (2005) J Biol Chem , vol.280 , pp. 11043-11051
    • Jensen, P.H.1    Weilguny, D.2    Matthiesen, F.3    McGuire, K.A.4    Shi, L.5    Hojrup, P.6
  • 9
    • 0025230703 scopus 로고
    • Binding of the pentamer/hexamer forms of mannan-binding protein to zymosan activates the proenzyme C1r2C1s2 complex, of the classical pathway of complement, without involvement of C1q
    • Lu JH, Thiel S, Wiedemann H, Timpl R Reid KB (1990) Binding of the pentamer/hexamer forms of mannan-binding protein to zymosan activates the proenzyme C1r2C1s2 complex, of the classical pathway of complement, without involvement of C1q. J Immunol 144, 2287 2294.
    • (1990) J Immunol , vol.144 , pp. 2287-2294
    • Lu, J.H.1    Thiel, S.2    Wiedemann, H.3    Timpl, R.4    Reid, K.B.5
  • 10
    • 0028533911 scopus 로고
    • Human mannose-binding protein carbohydrate recognition domain trimerizes through a triple alpha-helical coiled-coil
    • Sheriff S, Chang CY Ezekowitz RA (1994) Human mannose-binding protein carbohydrate recognition domain trimerizes through a triple alpha-helical coiled-coil. Nat Struct Biol 1, 789 794.
    • (1994) Nat Struct Biol , vol.1 , pp. 789-794
    • Sheriff, S.1    Chang, C.Y.2    Ezekowitz, R.A.3
  • 11
    • 14044278783 scopus 로고    scopus 로고
    • The two major oligomeric forms of human mannan-binding lectin: Chemical characterization, carbohydrate-binding properties, and interaction with MBL-associated serine proteases
    • Teillet F, Dublet B, Andrieu JP, Gaboriaud C, Arlaud GJ Thielens NM (2005) The two major oligomeric forms of human mannan-binding lectin: chemical characterization, carbohydrate-binding properties, and interaction with MBL-associated serine proteases. J Immunol 174, 2870 2877.
    • (2005) J Immunol , vol.174 , pp. 2870-2877
    • Teillet, F.1    Dublet, B.2    Andrieu, J.P.3    Gaboriaud, C.4    Arlaud, G.J.5    Thielens, N.M.6
  • 12
    • 0026464832 scopus 로고
    • Structure of a C-type mannose-binding protein complexed with an oligosaccharide
    • Weis WI, Drickamer K Hendrickson WA (1992) Structure of a C-type mannose-binding protein complexed with an oligosaccharide. Nature 360, 127 134.
    • (1992) Nature , vol.360 , pp. 127-134
    • Weis, W.I.1    Drickamer, K.2    Hendrickson, W.A.3
  • 13
    • 0026445745 scopus 로고
    • Activation of the classical complement pathway by mannose-binding protein in association with a novel C1s-like serine protease
    • Matsushita M Fujita T (1992) Activation of the classical complement pathway by mannose-binding protein in association with a novel C1s-like serine protease. J Exp Med 176, 1497 1502.
    • (1992) J Exp Med , vol.176 , pp. 1497-1502
    • Matsushita, M.1    Fujita, T.2
  • 14
    • 0028343828 scopus 로고
    • Molecular characterization of a novel serine protease involved in activation of the complement system by mannose-binding protein
    • Sato T, Endo Y, Matsushita M Fujita T (1994) Molecular characterization of a novel serine protease involved in activation of the complement system by mannose-binding protein. Int Immunol 6, 665 669.
    • (1994) Int Immunol , vol.6 , pp. 665-669
    • Sato, T.1    Endo, Y.2    Matsushita, M.3    Fujita, T.4
  • 15
    • 0036748253 scopus 로고    scopus 로고
    • The mannan-binding lectin-associated serine proteases (MASPs) and MAp19: Four components of the lectin pathway activation complex encoded by two genes
    • Schwaeble W, Dahl MR, Thiel S, Stover C Jensenius JC (2002) The mannan-binding lectin-associated serine proteases (MASPs) and MAp19: four components of the lectin pathway activation complex encoded by two genes. Immunobiology 205, 455 466.
    • (2002) Immunobiology , vol.205 , pp. 455-466
    • Schwaeble, W.1    Dahl, M.R.2    Thiel, S.3    Stover, C.4    Jensenius, J.C.5
  • 16
    • 27844451895 scopus 로고    scopus 로고
    • Mannan-binding-lectin-associated serine proteases, characteristics and disease associations
    • Sorensen R, Thiel S Jensenius JC (2005) Mannan-binding-lectin-associated serine proteases, characteristics and disease associations. Springer Semin Immunopathol 27, 299 319.
    • (2005) Springer Semin Immunopathol , vol.27 , pp. 299-319
    • Sorensen, R.1    Thiel, S.2    Jensenius, J.C.3
  • 17
    • 0033559136 scopus 로고    scopus 로고
    • Two constituents of the initiation complex of the mannan-binding lectin activation pathway of complement are encoded by a single structural gene
    • Stover CM, Thiel S, Thelen M, Lynch NJ, Vorup-Jensen T, Jensenius JC Schwaeble WJ (1999) Two constituents of the initiation complex of the mannan-binding lectin activation pathway of complement are encoded by a single structural gene. J Immunol 162, 3481 3490.
    • (1999) J Immunol , vol.162 , pp. 3481-3490
    • Stover, C.M.1    Thiel, S.2    Thelen, M.3    Lynch, N.J.4    Vorup-Jensen, T.5    Jensenius, J.C.6    Schwaeble, W.J.7
  • 19
    • 0034661696 scopus 로고    scopus 로고
    • Interaction of C1q and mannan-binding lectin (MBL) with C1r C1s MBL-associated serine proteases 1 and 2, and the MBL-associated protein MAp19
    • Thiel S, Petersen SV, Vorup-Jensen T, Matsushita M, Fujita T, Stover CM, Schwaeble WJ Jensenius JC (2000) Interaction of C1q and mannan-binding lectin (MBL) with C1r C1s MBL-associated serine proteases 1 and 2, and the MBL-associated protein MAp19. J Immunol 165, 878 887.
    • (2000) J Immunol , vol.165 , pp. 878-887
    • Thiel, S.1    Petersen, S.V.2    Vorup-Jensen, T.3    Matsushita, M.4    Fujita, T.5    Stover, C.M.6    Schwaeble, W.J.7    Jensenius, J.C.8
  • 20
    • 0035871632 scopus 로고    scopus 로고
    • Interaction properties of human mannan-binding lectin (MBL)-associated serine proteases-1 and -2, MBL-associated protein 19, and MBL
    • Thielens NM, Cseh S, Thiel S, Vorup-Jensen T, Rossi V, Jensenius JC Arlaud GJ (2001) Interaction properties of human mannan-binding lectin (MBL)-associated serine proteases-1 and -2, MBL-associated protein 19, and MBL. J Immunol 166, 5068 5077.
    • (2001) J Immunol , vol.166 , pp. 5068-5077
    • Thielens, N.M.1    Cseh, S.2    Thiel, S.3    Vorup-Jensen, T.4    Rossi, V.5    Jensenius, J.C.6    Arlaud, G.J.7
  • 21
    • 0034663925 scopus 로고    scopus 로고
    • Distinct pathways of mannan-binding lectin (MBL)- and C1-complex autoactivation revealed by reconstitution of MBL with recombinant MBL-associated serine protease-2
    • Vorup-Jensen T, Petersen SV, Hansen AG, Poulsen K, Schwaeble W, Sim RB, Reid KB, Davis SJ, Thiel S Jensenius JC (2000) Distinct pathways of mannan-binding lectin (MBL)- and C1-complex autoactivation revealed by reconstitution of MBL with recombinant MBL-associated serine protease-2. J Immunol 165, 2093 2100.
    • (2000) J Immunol , vol.165 , pp. 2093-2100
    • Vorup-Jensen, T.1    Petersen, S.V.2    Hansen, A.G.3    Poulsen, K.4    Schwaeble, W.5    Sim, R.B.6    Reid, K.B.7    Davis, S.J.8    Thiel, S.9    Jensenius, J.C.10
  • 22
    • 0031694012 scopus 로고    scopus 로고
    • MASP-2, the C3 convertase generating protease of the MBLectin complement activating pathway
    • Vorup-Jensen T, Jensenius JC Thiel S (1998) MASP-2, the C3 convertase generating protease of the MBLectin complement activating pathway. Immunobiology 199, 348 357.
    • (1998) Immunobiology , vol.199 , pp. 348-357
    • Vorup-Jensen, T.1    Jensenius, J.C.2    Thiel, S.3
  • 23
    • 0035854681 scopus 로고    scopus 로고
    • Stoichiometry of complexes between mannose-binding protein and its associated serine proteases. Defining functional units for complement activation
    • Chen CB Wallis R (2001) Stoichiometry of complexes between mannose-binding protein and its associated serine proteases. Defining functional units for complement activation. J Biol Chem 276, 25894 25902.
    • (2001) J Biol Chem , vol.276 , pp. 25894-25902
    • Chen, C.B.1    Wallis, R.2
  • 24
    • 0035900697 scopus 로고    scopus 로고
    • Identification of a site on mannan-binding lectin critical for enhancement of phagocytosis
    • Arora M, Munoz E Tenner AJ (2001) Identification of a site on mannan-binding lectin critical for enhancement of phagocytosis. J Biol Chem 276, 43087 43094.
    • (2001) J Biol Chem , vol.276 , pp. 43087-43094
    • Arora, M.1    Munoz, E.2    Tenner, A.J.3
  • 25
    • 29144445250 scopus 로고    scopus 로고
    • Heteroligomeric forms of codon 54 mannose binding lectin (MBL) in circulation demonstrate reduced in vitro function
    • Dean MM, Heatley S Minchinton RM (2006) Heteroligomeric forms of codon 54 mannose binding lectin (MBL) in circulation demonstrate reduced in vitro function. Mol Immunol 43, 950 961.
    • (2006) Mol Immunol , vol.43 , pp. 950-961
    • Dean, M.M.1    Heatley, S.2    Minchinton, R.M.3
  • 26
    • 2442676733 scopus 로고    scopus 로고
    • Disease-associated mutations in human mannose-binding lectin compromise oligomerization and activity of the final protein
    • Larsen F, Madsen HO, Sim RB, Koch C Garred P (2004) Disease-associated mutations in human mannose-binding lectin compromise oligomerization and activity of the final protein. J Biol Chem 279, 21302 21311.
    • (2004) J Biol Chem , vol.279 , pp. 21302-21311
    • Larsen, F.1    Madsen, H.O.2    Sim, R.B.3    Koch, C.4    Garred, P.5
  • 27
    • 0028971585 scopus 로고
    • The Gly-54->Asp allelic form of human mannose-binding protein (MBP) fails to bind MBP-associated serine protease
    • Matsushita M, Ezekowitz RA Fujita T (1995) The Gly-54->Asp allelic form of human mannose-binding protein (MBP) fails to bind MBP-associated serine protease. Biochem J 311, 1021 1023.
    • (1995) Biochem J , vol.311 , pp. 1021-1023
    • Matsushita, M.1    Ezekowitz, R.A.2    Fujita, T.3
  • 28
    • 13544272608 scopus 로고    scopus 로고
    • Stability junction at a common mutation site in the collagenous domain of the mannose binding lectin
    • Mohs A, Li Y, Doss-Pepe E, Baum J Brodsky B (2005) Stability junction at a common mutation site in the collagenous domain of the mannose binding lectin. Biochemistry 44, 1793 1799.
    • (2005) Biochemistry , vol.44 , pp. 1793-1799
    • Mohs, A.1    Li, Y.2    Doss-Pepe, E.3    Baum, J.4    Brodsky, B.5
  • 29
    • 1842740356 scopus 로고    scopus 로고
    • Localization of the serine protease-binding sites in the collagen-like domain of mannose-binding protein: Indirect effects of naturally occurring mutations on protease binding and activation
    • Wallis R, Shaw JM, Uitdehaag J, Chen CB, Torgersen D Drickamer K (2004) Localization of the serine protease-binding sites in the collagen-like domain of mannose-binding protein: indirect effects of naturally occurring mutations on protease binding and activation. J Biol Chem 279, 14065 14073.
    • (2004) J Biol Chem , vol.279 , pp. 14065-14073
    • Wallis, R.1    Shaw, J.M.2    Uitdehaag, J.3    Chen, C.B.4    Torgersen, D.5    Drickamer, K.6
  • 30
    • 27744558235 scopus 로고    scopus 로고
    • Decoupling of carbohydrate binding and MASP-2 autoactivation in variant mannose-binding lectins associated with immunodeficiency
    • Wallis R, Lynch NJ, Roscher S, Reid KB Schwaeble WJ (2005) Decoupling of carbohydrate binding and MASP-2 autoactivation in variant mannose-binding lectins associated with immunodeficiency. J Immunol 175, 6846 6851.
    • (2005) J Immunol , vol.175 , pp. 6846-6851
    • Wallis, R.1    Lynch, N.J.2    Roscher, S.3    Reid, K.B.4    Schwaeble, W.J.5
  • 31
    • 34247631620 scopus 로고    scopus 로고
    • Identification of the site of human mannan-binding lectin involved in the interaction with its partner serine proteases: The essential role of Lys55
    • Teillet F, Lacroix M, Thiel S, Weilguny D, Agger T, Arlaud GJ Thielens NM (2007) Identification of the site of human mannan-binding lectin involved in the interaction with its partner serine proteases: the essential role of Lys55. J Immunol 178, 5710 5716.
    • (2007) J Immunol , vol.178 , pp. 5710-5716
    • Teillet, F.1    Lacroix, M.2    Thiel, S.3    Weilguny, D.4    Agger, T.5    Arlaud, G.J.6    Thielens, N.M.7
  • 32
    • 0033947551 scopus 로고    scopus 로고
    • C1q: Structure, function, and receptors
    • Kishore U Reid KB (2000) C1q: structure, function, and receptors. Immunopharmacology 49, 159 170.
    • (2000) Immunopharmacology , vol.49 , pp. 159-170
    • Kishore, U.1    Reid, K.B.2
  • 34
    • 0345550400 scopus 로고    scopus 로고
    • Impact of mannose-binding lectin on susceptibility to infectious diseases
    • Eisen DP Minchinton RM (2003) Impact of mannose-binding lectin on susceptibility to infectious diseases. Clin Infect Dis 37, 1496 1505.
    • (2003) Clin Infect Dis , vol.37 , pp. 1496-1505
    • Eisen, D.P.1    Minchinton, R.M.2
  • 35
    • 5144222255 scopus 로고    scopus 로고
    • Complement: A unique innate immune sensor for danger signals
    • Gasque P (2004) Complement: a unique innate immune sensor for danger signals. Mol Immunol 41, 1089 1098.
    • (2004) Mol Immunol , vol.41 , pp. 1089-1098
    • Gasque, P.1
  • 36
    • 33644842388 scopus 로고    scopus 로고
    • Role of complement and other innate immune mechanisms in the removal of apoptotic cells
    • Ogden CA Elkon KB (2006) Role of complement and other innate immune mechanisms in the removal of apoptotic cells. Curr Dir Autoimmun 9, 120 142.
    • (2006) Curr Dir Autoimmun , vol.9 , pp. 120-142
    • Ogden, C.A.1    Elkon, K.B.2
  • 38
    • 0141918816 scopus 로고    scopus 로고
    • The role of mannose-binding lectin in health and disease
    • Turner MW (2003) The role of mannose-binding lectin in health and disease. Mol Immunol 40, 423 429.
    • (2003) Mol Immunol , vol.40 , pp. 423-429
    • Turner, M.W.1
  • 40
    • 2442650484 scopus 로고    scopus 로고
    • CC1q-R (calreticulin) and gC1q-R/p33: Ubiquitously expressed multi-ligand binding cellular proteins involved in inflammation and infection
    • Ghebrehiwet B Peerschke EI (2004) cC1q-R (calreticulin) and gC1q-R/p33: ubiquitously expressed multi-ligand binding cellular proteins involved in inflammation and infection. Mol Immunol 41, 173 183.
    • (2004) Mol Immunol , vol.41 , pp. 173-183
    • Ghebrehiwet, B.1    Peerschke, E.I.2
  • 41
    • 0036748314 scopus 로고    scopus 로고
    • Expression and function of C1q receptors and C1q binding proteins at the cell surface
    • Ghiran I, Tyagi SR, Klickstein LB Nicholson-Weller A (2002) Expression and function of C1q receptors and C1q binding proteins at the cell surface. Immunobiology 205, 407 420.
    • (2002) Immunobiology , vol.205 , pp. 407-420
    • Ghiran, I.1    Tyagi, S.R.2    Klickstein, L.B.3    Nicholson-Weller, A.4
  • 42
    • 0036864199 scopus 로고    scopus 로고
    • Structure-function studies of the receptors for complement C1q
    • Mcgreal E Gasque P (2002) Structure-function studies of the receptors for complement C1q. Biochem Soc Trans 30, 1010 1014.
    • (2002) Biochem Soc Trans , vol.30 , pp. 1010-1014
    • McGreal, E.1    Gasque, P.2
  • 43
    • 0031689432 scopus 로고    scopus 로고
    • Interaction of C1q and the collectins with the potential receptors calreticulin (cC1qR/collectin receptor) and megalin
    • Sim RB, Moestrup SK, Stuart GR, Lynch NJ, Lu J, Schwaeble WJ Malhotra R (1998) Interaction of C1q and the collectins with the potential receptors calreticulin (cC1qR/collectin receptor) and megalin. Immunobiology 199, 208 224.
    • (1998) Immunobiology , vol.199 , pp. 208-224
    • Sim, R.B.1    Moestrup, S.K.2    Stuart, G.R.3    Lynch, N.J.4    Lu, J.5    Schwaeble, W.J.6    Malhotra, R.7
  • 44
    • 30444440869 scopus 로고    scopus 로고
    • Immune function of C1q and its modulators CD91 and CD93
    • Tarr J Eggleton P (2005) Immune function of C1q and its modulators CD91 and CD93. Crit Rev Immunol 25, 305 330.
    • (2005) Crit Rev Immunol , vol.25 , pp. 305-330
    • Tarr, J.1    Eggleton, P.2
  • 45
    • 2442629457 scopus 로고    scopus 로고
    • Calnexin, calreticulin, and ERp57: Teammates in glycoprotein folding
    • Ellgaard L Frickel EM (2003) Calnexin, calreticulin, and ERp57: teammates in glycoprotein folding. Cell Biochem Biophys 39, 223 247.
    • (2003) Cell Biochem Biophys , vol.39 , pp. 223-247
    • Ellgaard, L.1    Frickel, E.M.2
  • 47
    • 26244451375 scopus 로고    scopus 로고
    • The optimization of peptide cargo bound to MHC class I molecules by the peptide-loading complex
    • Elliott T Williams A (2005) The optimization of peptide cargo bound to MHC class I molecules by the peptide-loading complex. Immunol Rev 207, 89 99.
    • (2005) Immunol Rev , vol.207 , pp. 89-99
    • Elliott, T.1    Williams, A.2
  • 48
    • 0035070198 scopus 로고    scopus 로고
    • CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin
    • Basu S, Binder RJ, Ramalingam T Srivastava PK (2001) CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin. Immunity 14, 303 313.
    • (2001) Immunity , vol.14 , pp. 303-313
    • Basu, S.1    Binder, R.J.2    Ramalingam, T.3    Srivastava, P.K.4
  • 49
    • 0141918823 scopus 로고    scopus 로고
    • By binding SIRPalpha or calreticulin/CD91, lung collectins act as dual function surveillance molecules to suppress or enhance inflammation
    • Gardai SJ, Xiao YQ, Dickinson M, Nick JA, Voelker DR, Greene KE Henson PM (2003) By binding SIRPalpha or calreticulin/CD91, lung collectins act as dual function surveillance molecules to suppress or enhance inflammation. Cell 115, 13 23.
    • (2003) Cell , vol.115 , pp. 13-23
    • Gardai, S.J.1    Xiao, Y.Q.2    Dickinson, M.3    Nick, J.A.4    Voelker, D.R.5    Greene, K.E.6    Henson, P.M.7
  • 50
    • 0035903289 scopus 로고    scopus 로고
    • C1q and mannose binding lectin engagement of cell surface calreticulin and CD91 initiates macropinocytosis and uptake of apoptotic cells
    • Ogden CA, Decathelineau A, Hoffmann PR, Bratton D, Ghebrehiwet B, Fadok VA Henson PM (2001) C1q and mannose binding lectin engagement of cell surface calreticulin and CD91 initiates macropinocytosis and uptake of apoptotic cells. J Exp Med 194, 781 795.
    • (2001) J Exp Med , vol.194 , pp. 781-795
    • Ogden, C.A.1    Decathelineau, A.2    Hoffmann, P.R.3    Bratton, D.4    Ghebrehiwet, B.5    Fadok, V.A.6    Henson, P.M.7
  • 51
    • 0036785571 scopus 로고    scopus 로고
    • Role of surfactant proteins A, D, and C1q in the clearance of apoptotic cells in vivo and in vitro: Calreticulin and CD91 as a common collectin receptor complex
    • Vandivier RW, Ogden CA, Fadok VA, Hoffmann PR, Brown KK, Botto M, Walport MJ, Fisher JH, Henson PM Greene KE (2002) Role of surfactant proteins A, D, and C1q in the clearance of apoptotic cells in vivo and in vitro: calreticulin and CD91 as a common collectin receptor complex. J Immunol 169, 3978 3986.
    • (2002) J Immunol , vol.169 , pp. 3978-3986
    • Vandivier, R.W.1    Ogden, C.A.2    Fadok, V.A.3    Hoffmann, P.R.4    Brown, K.K.5    Botto, M.6    Walport, M.J.7    Fisher, J.H.8    Henson, P.M.9    Greene, K.E.10
  • 52
    • 27744555038 scopus 로고    scopus 로고
    • Differential CD91 dependence for calreticulin and Pseudomonas exotoxin-A endocytosis
    • Walters JJ Berwin B (2005) Differential CD91 dependence for calreticulin and Pseudomonas exotoxin-A endocytosis. Traffic 6, 1173 1182.
    • (2005) Traffic , vol.6 , pp. 1173-1182
    • Walters, J.J.1    Berwin, B.2
  • 53
    • 2642510766 scopus 로고    scopus 로고
    • Interaction of C1q with the receptor calreticulin requires a conformational change in C1q
    • Steino A, Jorgensen CS, Laursen I Houen G (2004) Interaction of C1q with the receptor calreticulin requires a conformational change in C1q. Scand J Immunol 59, 485 495.
    • (2004) Scand J Immunol , vol.59 , pp. 485-495
    • Steino, A.1    Jorgensen, C.S.2    Laursen, I.3    Houen, G.4
  • 54
    • 34247324005 scopus 로고    scopus 로고
    • Second-generation nanofiltered plasma-derived mannan-binding lectin product: Process and characteristics
    • Laursen I, Houen G, Hojrup P, Brouwer N, Krogsoe LB, Blou L Hansen PR (2007) Second-generation nanofiltered plasma-derived mannan-binding lectin product: process and characteristics. Vox Sang 92, 338 350.
    • (2007) Vox Sang , vol.92 , pp. 338-350
    • Laursen, I.1    Houen, G.2    Hojrup, P.3    Brouwer, N.4    Krogsoe, L.B.5    Blou, L.6    Hansen, P.R.7
  • 57
    • 3142733778 scopus 로고    scopus 로고
    • The X-ray structure of human mannan-binding lectin-associated protein 19 (MAp19) and its interaction site with mannan-binding lectin and L-ficolin
    • Gregory LA, Thielens NM, Matsushita M, Sorensen R, Arlaud GJ, Fontecilla-Camps JC Gaboriaud C (2004) The X-ray structure of human mannan-binding lectin-associated protein 19 (MAp19) and its interaction site with mannan-binding lectin and L-ficolin. J Biol Chem 279, 29391 29397.
    • (2004) J Biol Chem , vol.279 , pp. 29391-29397
    • Gregory, L.A.1    Thielens, N.M.2    Matsushita, M.3    Sorensen, R.4    Arlaud, G.J.5    Fontecilla-Camps, J.C.6    Gaboriaud, C.7
  • 58
    • 14044258721 scopus 로고    scopus 로고
    • Mass spectrometry analysis of the oligomeric C1q protein reveals the B chain as the target of trypsin cleavage and interaction with fucoidan
    • Tissot B, Gonnet F, Iborra A, Berthou C, Thielens N, Arlaud GJ Daniel R (2005) Mass spectrometry analysis of the oligomeric C1q protein reveals the B chain as the target of trypsin cleavage and interaction with fucoidan. Biochemistry 44, 2602 2609.
    • (2005) Biochemistry , vol.44 , pp. 2602-2609
    • Tissot, B.1    Gonnet, F.2    Iborra, A.3    Berthou, C.4    Thielens, N.5    Arlaud, G.J.6    Daniel, R.7
  • 60
    • 4644252585 scopus 로고    scopus 로고
    • A polypeptide binding conformation of calreticulin is induced by heat shock, calcium depletion, or by deletion of the C-terminal acidic region
    • Rizvi SM, Mancino L, Thammavongsa V, Cantley RL Raghavan M (2004) A polypeptide binding conformation of calreticulin is induced by heat shock, calcium depletion, or by deletion of the C-terminal acidic region. Mol Cell 15, 913 923.
    • (2004) Mol Cell , vol.15 , pp. 913-923
    • Rizvi, S.M.1    Mancino, L.2    Thammavongsa, V.3    Cantley, R.L.4    Raghavan, M.5
  • 61
    • 0033103513 scopus 로고    scopus 로고
    • Calreticulin, a peptide-binding chaperone of the endoplasmic reticulum, elicits tumor- and peptide-specific immunity
    • Basu S Srivastava PK (1999) Calreticulin, a peptide-binding chaperone of the endoplasmic reticulum, elicits tumor- and peptide-specific immunity. J Exp Med 189, 797 802.
    • (1999) J Exp Med , vol.189 , pp. 797-802
    • Basu, S.1    Srivastava, P.K.2
  • 62
    • 0034993230 scopus 로고    scopus 로고
    • Activation of human monocyte cell line U937 via cell surface calreticulin
    • Cho JH, Homma KJ, Kanegasaki S Natori S (2001) Activation of human monocyte cell line U937 via cell surface calreticulin. Cell Stress Chaperones 6, 148 152.
    • (2001) Cell Stress Chaperones , vol.6 , pp. 148-152
    • Cho, J.H.1    Homma, K.J.2    Kanegasaki, S.3    Natori, S.4
  • 63
    • 0035816569 scopus 로고    scopus 로고
    • The lectin chaperone calnexin utilizes polypeptide-based interactions to associate with many of its substrates in vivo
    • Danilczyk UG Williams DB (2001) The lectin chaperone calnexin utilizes polypeptide-based interactions to associate with many of its substrates in vivo. J Biol Chem 276, 25532 25540.
    • (2001) J Biol Chem , vol.276 , pp. 25532-25540
    • Danilczyk, U.G.1    Williams, D.B.2
  • 64
    • 0033197741 scopus 로고    scopus 로고
    • Calnexin discriminates between protein conformational states and functions as a molecular chaperone in vitro
    • Ihara Y, Cohen-Doyle MF, Saito Y Williams DB (1999) Calnexin discriminates between protein conformational states and functions as a molecular chaperone in vitro. Mol Cell 4, 331 341.
    • (1999) Mol Cell , vol.4 , pp. 331-341
    • Ihara, Y.1    Cohen-Doyle, M.F.2    Saito, Y.3    Williams, D.B.4
  • 65
    • 0033152788 scopus 로고    scopus 로고
    • Calreticulin displays in vivo peptide-binding activity and can elicit CTL responses against bound peptides
    • Nair S, Wearsch PA, Mitchell DA, Wassenberg JJ, Gilboa E Nicchitta CV (1999) Calreticulin displays in vivo peptide-binding activity and can elicit CTL responses against bound peptides. J Immunol 162, 6426 6432.
    • (1999) J Immunol , vol.162 , pp. 6426-6432
    • Nair, S.1    Wearsch, P.A.2    Mitchell, D.A.3    Wassenberg, J.J.4    Gilboa, E.5    Nicchitta, C.V.6
  • 66
    • 0033485263 scopus 로고    scopus 로고
    • Calreticulin functions in vitro as a molecular chaperone for both glycosylated and non-glycosylated proteins
    • Saito Y, Ihara Y, Leach MR, Cohen-Doyle MF Williams DB (1999) Calreticulin functions in vitro as a molecular chaperone for both glycosylated and non-glycosylated proteins. EMBO J 18, 6718 6729.
    • (1999) EMBO J , vol.18 , pp. 6718-6729
    • Saito, Y.1    Ihara, Y.2    Leach, M.R.3    Cohen-Doyle, M.F.4    Williams, D.B.5
  • 67
    • 0038037820 scopus 로고    scopus 로고
    • Role of calnexin in the glycan-independent quality control of proteolipid protein
    • Swanton E, High S Woodman P (2003) Role of calnexin in the glycan-independent quality control of proteolipid protein. EMBO J 22, 2948 2958.
    • (2003) EMBO J , vol.22 , pp. 2948-2958
    • Swanton, E.1    High, S.2    Woodman, P.3
  • 68
    • 0037310722 scopus 로고    scopus 로고
    • Natural substrates and inhibitors of mannan-binding lectin-associated serine protease-1 and -2: A study on recombinant catalytic fragments
    • Ambrus G, Gal P, Kojima M, Szilagyi K, Balczer J, Antal J, Graf L, Laich A, Moffatt BE, Schwaeble W et al. (2003) Natural substrates and inhibitors of mannan-binding lectin-associated serine protease-1 and -2: a study on recombinant catalytic fragments. J Immunol 170, 1374 1382.
    • (2003) J Immunol , vol.170 , pp. 1374-1382
    • Ambrus, G.1    Gal, P.2    Kojima, M.3    Szilagyi, K.4    Balczer, J.5    Antal, J.6    Graf, L.7    Laich, A.8    Moffatt, B.E.9    Schwaeble, W.10
  • 69
    • 0041566824 scopus 로고    scopus 로고
    • Mannan-binding lectin (MBL) production from human plasma
    • Laursen I (2003) Mannan-binding lectin (MBL) production from human plasma. Biochem Soc Trans 31, 758 762.
    • (2003) Biochem Soc Trans , vol.31 , pp. 758-762
    • Laursen, I.1
  • 70
    • 0030804488 scopus 로고    scopus 로고
    • Conjugation to preadsorbed preactivated proteins and efficient generation of anti peptide antibodies
    • Houen G, Jakobsen MH, Svaerke C, Koch C Barkholt V (1997) Conjugation to preadsorbed preactivated proteins and efficient generation of anti peptide antibodies. J Immunol Methods 206, 125 134.
    • (1997) J Immunol Methods , vol.206 , pp. 125-134
    • Houen, G.1    Jakobsen, M.H.2    Svaerke, C.3    Koch, C.4    Barkholt, V.5
  • 71
    • 12144289655 scopus 로고    scopus 로고
    • Characterization of recombinant mannan-binding lectin-associated serine protease (MASP)-3 suggests an activation mechanism different from that of MASP-1 and MASP-2
    • Zundel S, Cseh S, Lacroix M, Dahl MR, Matsushita M, Andrieu JP, Schwaeble WJ, Jensenius JC, Fujita T, Arlaud GJ et al. (2004) Characterization of recombinant mannan-binding lectin-associated serine protease (MASP)-3 suggests an activation mechanism different from that of MASP-1 and MASP-2. J Immunol 172, 4342 4350.
    • (2004) J Immunol , vol.172 , pp. 4342-4350
    • Zundel, S.1    Cseh, S.2    Lacroix, M.3    Dahl, M.R.4    Matsushita, M.5    Andrieu, J.P.6    Schwaeble, W.J.7    Jensenius, J.C.8    Fujita, T.9    Arlaud, G.J.10
  • 72
    • 0034856389 scopus 로고    scopus 로고
    • Human placental calreticulin characterization of domain structure and post-translational modifications
    • Hojrup P, Roepstorff P Houen G (2001) Human placental calreticulin characterization of domain structure and post-translational modifications. Eur J Biochem 268, 2558 2565.
    • (2001) Eur J Biochem , vol.268 , pp. 2558-2565
    • Hojrup, P.1    Roepstorff, P.2    Houen, G.3
  • 75
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680 685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 76
    • 0012456693 scopus 로고
    • Analysis of bacteriophage T7 early RNAs and proteins on slab gels
    • Studier FW (1973) Analysis of bacteriophage T7 early RNAs and proteins on slab gels. J Mol Biol 79, 237 248.
    • (1973) J Mol Biol , vol.79 , pp. 237-248
    • Studier, F.W.1
  • 77
    • 0036571319 scopus 로고    scopus 로고
    • Silver staining of proteins on electroblotting membranes and intensification of silver staining of proteins separated by polyacrylamide gel electrophoresis
    • Sorensen BK, Hojrup P, Ostergard E, Jorgensen CS, Enghild J, Ryder LR Houen G (2002) Silver staining of proteins on electroblotting membranes and intensification of silver staining of proteins separated by polyacrylamide gel electrophoresis. Anal Biochem 304, 33 41.
    • (2002) Anal Biochem , vol.304 , pp. 33-41
    • Sorensen, B.K.1    Hojrup, P.2    Ostergard, E.3    Jorgensen, C.S.4    Enghild, J.5    Ryder, L.R.6    Houen, G.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.