메뉴 건너뛰기




Volumn 395, Issue 3, 2006, Pages 579-586

Collagen binding by the mannose receptor mediated through the fibronectin type II domain

Author keywords

Carbohydrate recognition domain; Cell adhesion; Collagen; ELISA; Fibronectin type II domain; Mannose receptor

Indexed keywords

AMINO ACIDS; ASSAYS; BIOCHEMICAL ENGINEERING; BIOCHEMISTRY; CARBOHYDRATES; CELL CULTURE; PROTEINS; SUGARS;

EID: 33646235210     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20052027     Document Type: Article
Times cited : (85)

References (45)
  • 1
    • 0031820273 scopus 로고    scopus 로고
    • The C-type lectin superfamily in the immune system
    • Weis, W. I., Taylor, M. E. and Drickamer, K. (1998) The C-type lectin superfamily in the immune system. Immunol. Rev. 163, 19-34
    • (1998) Immunol. Rev. , vol.163 , pp. 19-34
    • Weis, W.I.1    Taylor, M.E.2    Drickamer, K.3
  • 2
    • 0025362207 scopus 로고
    • Primary structure of the mannose receptor contains multiple motifs resembling carbohydrate-recognition domains
    • Taylor, M. E., Conary, J. T., Lennarz, M. R., Stahl, P. D. and Drickamer, K. (1990) Primary structure of the mannose receptor contains multiple motifs resembling carbohydrate-recognition domains. J. Biol. Chem. 265, 12156-12162
    • (1990) J. Biol. Chem. , vol.265 , pp. 12156-12162
    • Taylor, M.E.1    Conary, J.T.2    Lennarz, M.R.3    Stahl, P.D.4    Drickamer, K.5
  • 3
    • 0026508876 scopus 로고
    • Contribution to ligand binding by multiple carbohydrate-recognition domains in the macrophage mannose receptor
    • Taylor, M. E., Bezouska, K. and Drickamer, K. (1992) Contribution to ligand binding by multiple carbohydrate-recognition domains in the macrophage mannose receptor. J. Biol. Chem. 267, 1719-1726
    • (1992) J. Biol. Chem. , vol.267 , pp. 1719-1726
    • Taylor, M.E.1    Bezouska, K.2    Drickamer, K.3
  • 4
    • 0027535749 scopus 로고
    • Structural requirements for high affinity binding of complex ligands by the macrophage mannose receptor
    • Taylor, M. E. and Drickamer, K. (1993) Structural requirements for high affinity binding of complex ligands by the macrophage mannose receptor. J. Biol. Chem. 268, 399-404
    • (1993) J. Biol. Chem. , vol.268 , pp. 399-404
    • Taylor, M.E.1    Drickamer, K.2
  • 6
    • 0025739266 scopus 로고
    • Binding of tissue-type plasminogen activator by the mannose receptor
    • Otter, M., Barrett-Bergshoeff, M. M. and Rijken, D. C. (1991) Binding of tissue-type plasminogen activator by the mannose receptor. J. Biol. Chem. 266, 13931-13935
    • (1991) J. Biol. Chem. , vol.266 , pp. 13931-13935
    • Otter, M.1    Barrett-Bergshoeff, M.M.2    Rijken, D.C.3
  • 9
    • 0034599596 scopus 로고    scopus 로고
    • Crystal structure of the cysteine-rich domain of mannose receptor complexed with a sulfated carbohydrate ligand
    • Liu, Y., Chirino, A. J., Leteux, C., Feizi, T., Misulovin, Z., Nussenzweig, M. C. and Bjorkman, P. J. (2000) Crystal structure of the cysteine-rich domain of mannose receptor complexed with a sulfated carbohydrate ligand. J. Exp. Med. 191, 1105-1115
    • (2000) J. Exp. Med. , vol.191 , pp. 1105-1115
    • Liu, Y.1    Chirino, A.J.2    Leteux, C.3    Feizi, T.4    Misulovin, Z.5    Nussenzweig, M.C.6    Bjorkman, P.J.7
  • 10
    • 0030610465 scopus 로고    scopus 로고
    • 4-4-GalNAcβ1,4GlcNAcβ1,2Manα-specific receptor from rat liver
    • 4-4-GalNAcβ1,4GlcNAcβ1,2Manα-specific receptor from rat liver. J. Biol. Chem. 272, 14629-14637
    • (1997) J. Biol. Chem. , vol.272 , pp. 14629-14637
    • Fiete, D.1    Baenziger, J.U.2
  • 12
    • 0030609968 scopus 로고    scopus 로고
    • Evolution of a family of receptors containing multiple C-type carbohydrate-recognition domains
    • Taylor, M. E. (1997) Evolution of a family of receptors containing multiple C-type carbohydrate-recognition domains. Glycobiology 7, v-viii
    • (1997) Glycobiology , vol.7
    • Taylor, M.E.1
  • 13
    • 0023919959 scopus 로고
    • H-ras oncogene-transformed human bronchial epithelial cells (TBE-1) secrete a single metalloprotease capable of degrading basement membrane collagen
    • Collier, I. E., Wilhelm, S. M., Eisen, A. Z., Marmer, B. L., Grant, G. A., Seltzer, J. L., Kronberger, A., He, C. S., Bauer, E. A. and Goldberg, G. I. (1988) H-ras oncogene-transformed human bronchial epithelial cells (TBE-1) secrete a single metalloprotease capable of degrading basement membrane collagen. J. Biol. Chem. 263, 6579-6587
    • (1988) J. Biol. Chem. , vol.263 , pp. 6579-6587
    • Collier, I.E.1    Wilhelm, S.M.2    Eisen, A.Z.3    Marmer, B.L.4    Grant, G.A.5    Seltzer, J.L.6    Kronberger, A.7    He, C.S.8    Bauer, E.A.9    Goldberg, G.I.10
  • 14
    • 0024330327 scopus 로고
    • The SV40 transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophages
    • Wilhelm, S. M., Collier, I. E., Marmer, B. L., Eisen, A. Z., Grant, G. A. and Goldberg, G. I. (1989) The SV40 transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophages. J. Biol. Chem. 264, 17213-17221
    • (1989) J. Biol. Chem. , vol.264 , pp. 17213-17221
    • Wilhelm, S.M.1    Collier, I.E.2    Marmer, B.L.3    Eisen, A.Z.4    Grant, G.A.5    Goldberg, G.I.6
  • 15
    • 0022407061 scopus 로고
    • Characterization of human blood coagulation factor XII cDNA: Prediction of the primary structure of factor XII and the tertiary structure of β-factor XIIa
    • Cool, D. E., Edgell, C. J., Louie, G. V., Zoller, M. J., Brayer, G. D. and MacGillivray, R. T. (1985) Characterization of human blood coagulation factor XII cDNA: prediction of the primary structure of factor XII and the tertiary structure of β-factor XIIa. J. Biol. Chem. 260, 13666-13676
    • (1985) J. Biol. Chem. , vol.260 , pp. 13666-13676
    • Cool, D.E.1    Edgell, C.J.2    Louie, G.V.3    Zoller, M.J.4    Brayer, G.D.5    MacGillivray, R.T.6
  • 16
    • 0023840372 scopus 로고
    • Cloning and sequence analysis of the cation-independent mannose 6-phosphate receptor
    • Lobel, P., Dahms, N. M. and and Kornfeld, S. (1988) Cloning and sequence analysis of the cation-independent mannose 6-phosphate receptor. J. Biol. Chem. 263, 2563-2570
    • (1988) J. Biol. Chem. , vol.263 , pp. 2563-2570
    • Lobel, P.1    Dahms, N.M.2    Kornfeld, S.3
  • 17
  • 18
    • 0022102304 scopus 로고
    • Primary structure of human fibronectin: Differential splicing may generate at least 10 polypeptides from a single gene
    • Kornblihtt, A. R., Umezawa, K., Vibe-Pedersen, K. and Baralle, F. E. (1985) Primary structure of human fibronectin: differential splicing may generate at least 10 polypeptides from a single gene. EMBO J. 4, 1755-1759
    • (1985) EMBO J. , vol.4 , pp. 1755-1759
    • Kornblihtt, A.R.1    Umezawa, K.2    Vibe-Pedersen, K.3    Baralle, F.E.4
  • 19
    • 0025110392 scopus 로고
    • A second fibronectin-binding region is present in collagen α chains
    • Guidry, C., Miller, E. J. and Hook, M. (1990) A second fibronectin-binding region is present in collagen α chains. J. Biol. Chem. 265, 19230-19236
    • (1990) J. Biol. Chem. , vol.265 , pp. 19230-19236
    • Guidry, C.1    Miller, E.J.2    Hook, M.3
  • 20
    • 0028326269 scopus 로고
    • The gelatin-binding site of human 72 kDa type IV collagenase (gelatinase A)
    • Banyai, L., Tordai, H. and Patthy, L. (1994) The gelatin-binding site of human 72 kDa type IV collagenase (gelatinase A). Biochem. J. 298, 403-407
    • (1994) Biochem. J. , vol.298 , pp. 403-407
    • Banyai, L.1    Tordai, H.2    Patthy, L.3
  • 21
    • 0026656315 scopus 로고
    • Alanine scanning mutagenesis and functional analysis of the fibronectin-like collagen-binding domain from human 92-kDa type IV collagenase
    • Collier, I. E., Krasnov, P. A., Strongin, A. Y., Birkedal-Hansen, H. and Goldberg, G. I. (1992) Alanine scanning mutagenesis and functional analysis of the fibronectin-like collagen-binding domain from human 92-kDa type IV collagenase. J. Biol. Chem. 267, 6776-6781
    • (1992) J. Biol. Chem. , vol.267 , pp. 6776-6781
    • Collier, I.E.1    Krasnov, P.A.2    Strongin, A.Y.3    Birkedal-Hansen, H.4    Goldberg, G.I.5
  • 22
    • 0026657161 scopus 로고
    • Major proteins of bovine seminal plasma exhibit novel interactions with phospholipid
    • Desnoyers, L. and Manjunath, P. (1992) Major proteins of bovine seminal plasma exhibit novel interactions with phospholipid. J. Biol. Chem. 267, 10149-10155
    • (1992) J. Biol. Chem. , vol.267 , pp. 10149-10155
    • Desnoyers, L.1    Manjunath, P.2
  • 23
    • 0033569704 scopus 로고    scopus 로고
    • The second type II module from human matrix metalloproteinase: Structure, function and dynamics
    • Briknarova, K., Grishaev, A., Banyai, L., Tordai, H., Patthy, L. and Llinas, M. (1999) The second type II module from human matrix metalloproteinase: structure, function and dynamics. Structure 7, 1235-1245
    • (1999) Structure , vol.7 , pp. 1235-1245
    • Briknarova, K.1    Grishaev, A.2    Banyai, L.3    Tordai, H.4    Patthy, L.5    Llinas, M.6
  • 24
    • 0033555301 scopus 로고    scopus 로고
    • The gelatin-binding site of the second type-II domain of gelatinase A/MMP-2
    • Tordai, H. and Patthy, L (1999) The gelatin-binding site of the second type-II domain of gelatinase A/MMP-2. Eur. J. Biochem. 259, 513-518
    • (1999) Eur. J. Biochem. , vol.259 , pp. 513-518
    • Tordai, H.1    Patthy, L.2
  • 26
    • 0034695451 scopus 로고    scopus 로고
    • A urokinase receptor-associated protein with specific collagen binding properties
    • Behrendt, N., Jensen, O. N., Engelholm, L. H., Mort, E., Mann, M. and Dane, K. (2000) A urokinase receptor-associated protein with specific collagen binding properties. J. Biol. Chem. 275, 1993-2002
    • (2000) J. Biol. Chem. , vol.275 , pp. 1993-2002
    • Behrendt, N.1    Jensen, O.N.2    Engelholm, L.H.3    Mort, E.4    Mann, M.5    Dane, K.6
  • 27
    • 0042221682 scopus 로고    scopus 로고
    • Identification and characterization of the endocytic transmembrane glycoprotein Endo180 as a novel collagen receptor
    • Wienke, D., MacFadyen, J. R. and Isacke, C. M. (2003) Identification and characterization of the endocytic transmembrane glycoprotein Endo180 as a novel collagen receptor. Mol. Biol. Cell 14, 3592-3604
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3592-3604
    • Wienke, D.1    MacFadyen, J.R.2    Isacke, C.M.3
  • 29
    • 0041662269 scopus 로고    scopus 로고
    • A targeted deletion in the endocytic receptor gene Endo180 results in a defect in collagen uptake
    • East, L., McCarthy, A., Wienke, D., Sturge, J., Ashworth, A. and Isacke, C. M. (2003) A targeted deletion in the endocytic receptor gene Endo180 results in a defect in collagen uptake. EMBO Rep. 4, 710-716
    • (2003) EMBO Rep. , vol.4 , pp. 710-716
    • East, L.1    McCarthy, A.2    Wienke, D.3    Sturge, J.4    Ashworth, A.5    Isacke, C.M.6
  • 31
    • 0033569567 scopus 로고    scopus 로고
    • Multiple interactions between pituitary hormones and the mannose receptor
    • Simpson, D. Z., Hitchen, P. G., Elmhirst, E. L. and Taylor, M. E. (1999) Multiple interactions between pituitary hormones and the mannose receptor. Biochem. J. 343, 403-411
    • (1999) Biochem. J. , vol.343 , pp. 403-411
    • Simpson, D.Z.1    Hitchen, P.G.2    Elmhirst, E.L.3    Taylor, M.E.4
  • 32
    • 0035805584 scopus 로고    scopus 로고
    • An extended conformation of the macrophage mannose receptor
    • Napper, C. E., Dyson, M. H. and Taylor, M . E. (2001) An extended conformation of the macrophage mannose receptor. J. Biol. Chem. 276, 14759-14766
    • (2001) J. Biol. Chem. , vol.276 , pp. 14759-14766
    • Napper, C.E.1    Dyson, M.H.2    Taylor, M.E.3
  • 33
    • 0347457065 scopus 로고    scopus 로고
    • Characterization of sugar binding by the mannose receptor family member, Endo-180
    • East, L., Rushton, S., Taylor, M. E. and Isacke, C. M. (2002) Characterization of sugar binding by the mannose receptor family member, Endo-180. J. Biol. Chem. 277, 50469-50475
    • (2002) J. Biol. Chem. , vol.277 , pp. 50469-50475
    • East, L.1    Rushton, S.2    Taylor, M.E.3    Isacke, C.M.4
  • 35
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of protein electroblotted onto polvinylidene difluoride membranes
    • Matsudaira, P. (1987) Sequence from picomole quantities of protein electroblotted onto polvinylidene difluoride membranes. J. Biol. Chem. 262, 10035-10038
    • (1987) J. Biol. Chem. , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 36
    • 0003474266 scopus 로고    scopus 로고
    • Ligand binding
    • Creighton, T. E., ed., Oxford University Press, New York
    • Levitzki, A. (1997) Ligand binding. In Protein Function: a Practical Approach (Creighton, T. E., ed.), pp. 101-129, Oxford University Press, New York
    • (1997) Protein Function: A Practical Approach , pp. 101-129
    • Levitzki, A.1
  • 38
    • 0032707339 scopus 로고    scopus 로고
    • Expression and secretion of proteins in E. coli
    • Pines, O. and Inouye, M. (1999) Expression and secretion of proteins in E. coli. Mol. Biotechnol. 12, 25-34
    • (1999) Mol. Biotechnol. , vol.12 , pp. 25-34
    • Pines, O.1    Inouye, M.2
  • 39
    • 0029010660 scopus 로고
    • Extracellular matrix binding properties of recombinant fibronectin type II-like modules of human 72-kDa gelatinase/type IV collagenase: High affinity binding to native type I collagen but not native type IV collagen
    • Steffensen, B., Wallon, U. M. and Overall, C. M. (1995) Extracellular matrix binding properties of recombinant fibronectin type II-like modules of human 72-kDa gelatinase/type IV collagenase: high affinity binding to native type I collagen but not native type IV collagen. J. Biol. Chem. 270, 11555-11566
    • (1995) J. Biol. Chem. , vol.270 , pp. 11555-11566
    • Steffensen, B.1    Wallon, U.M.2    Overall, C.M.3
  • 41
    • 0025149128 scopus 로고
    • Circulating C-terminal propeptide of type I procollagen is cleared mainly via the mannose receptor in liver endothelial cells
    • Smedsrod, B., Melkko, J., Risteli, L. and Risteli, J. (1990) Circulating C-terminal propeptide of type I procollagen is cleared mainly via the mannose receptor in liver endothelial cells. Biochem. J. 271, 345-350
    • (1990) Biochem. J. , vol.271 , pp. 345-350
    • Smedsrod, B.1    Melkko, J.2    Risteli, L.3    Risteli, J.4
  • 42
    • 0344947889 scopus 로고    scopus 로고
    • Mannose receptor and its putative ligands in normal murine lymphoid and nonlymphoid organs: In situ expression of mannose receptor by selected macrophages, endothelial cells, perivascular microglia, and mesangial cells, but not dendritic cells
    • Linehan, S. A., Martinez-Pomares, L., Stahl, P. D. and Gordon, S. (1999) Mannose receptor and its putative ligands in normal murine lymphoid and nonlymphoid organs: in situ expression of mannose receptor by selected macrophages, endothelial cells, perivascular microglia, and mesangial cells, but not dendritic cells. J. Exp. Med. 189, 1961-1972
    • (1999) J. Exp. Med. , vol.189 , pp. 1961-1972
    • Linehan, S.A.1    Martinez-Pomares, L.2    Stahl, P.D.3    Gordon, S.4
  • 43
    • 0035088954 scopus 로고    scopus 로고
    • Regional and cellular expression of the mannose receptor in the post-natal developing mouse brain
    • Burudi, E. M. E. and Regnier-Vigouroux, A. (2001) Regional and cellular expression of the mannose receptor in the post-natal developing mouse brain. Cell Tissue Res. 303, 307-317
    • (2001) Cell Tissue Res. , vol.303 , pp. 307-317
    • Burudi, E.M.E.1    Regnier-Vigouroux, A.2
  • 45
    • 0029009977 scopus 로고
    • The receptor DEC-205 expressed by dendritic cells and thymic epithelial cells is involved in antigen processing
    • Jiang, W., Swiggard, W. J., Heufler, C., Peng, M., Mirza, A., Steinman, R. M. and Nussenzweig, M. C. (1995) The receptor DEC-205 expressed by dendritic cells and thymic epithelial cells is involved in antigen processing. Nature (London) 375, 151-155
    • (1995) Nature (London) , vol.375 , pp. 151-155
    • Jiang, W.1    Swiggard, W.J.2    Heufler, C.3    Peng, M.4    Mirza, A.5    Steinman, R.M.6    Nussenzweig, M.C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.