메뉴 건너뛰기




Volumn 14, Issue 9, 2003, Pages 3592-3604

Identification and characterization of the endocytic transmembrane glycoprotein Endo180 as a novel collagen receptor

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CLATHRIN; COLLAGEN RECEPTOR; COLLAGEN TYPE 5; CYSTEINE; FIBRONECTIN; LECTIN; MANNOSE RECEPTOR; MEMBRANE PROTEIN; PROTEIN ENDO180; RECEPTOR; UNCLASSIFIED DRUG;

EID: 0042221682     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E02-12-0814     Document Type: Article
Times cited : (131)

References (47)
  • 1
    • 0034634627 scopus 로고    scopus 로고
    • A novel model system for characterization of phagosomal maturation, acidification, and intracellular collagen degradation in fibroblasts
    • Arora, P.D., Manolson, M.F., Downey, G.P., Sodek, J., and McCulloch, C.A. (2000). A novel model system for characterization of phagosomal maturation, acidification, and intracellular collagen degradation in fibroblasts. J. Biol. Chem. 275, 35432-35441.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35432-35441
    • Arora, P.D.1    Manolson, M.F.2    Downey, G.P.3    Sodek, J.4    McCulloch, C.A.5
  • 2
    • 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(Pt 2), 403-407.
    • (1994) Biochem. J. , vol.298 , Issue.PART 2 , pp. 403-407
    • Banyai, L.1    Tordai, H.2    Patthy, L.3
  • 3
    • 0034695451 scopus 로고    scopus 로고
    • A urokinase receptor-associated protein with specific collagen binding properties
    • Behrendt, N., Jensen, O.N., Engelholm, L.H., Mortz, E., Mann, M., and Dano, 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    Mortz, E.4    Mann, M.5    Dano, K.6
  • 4
    • 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
  • 5
    • 0026554217 scopus 로고
    • Affinity of integrins for damaged extracellular matrix: Alpha v beta 3 binds to denatured collagen type I through RGD sites
    • Davis, G.E. (1992). Affinity of integrins for damaged extracellular matrix: alpha v beta 3 binds to denatured collagen type I through RGD sites. Biochem. Biophys. Res. Commun. 182, 1025-1031.
    • (1992) Biochem. Biophys. Res. Commun. , vol.182 , pp. 1025-1031
    • Davis, G.E.1
  • 6
    • 0037136405 scopus 로고    scopus 로고
    • The mannose receptor family
    • East, L., and Isacke, C.M. (2002). The mannose receptor family. Biochem. Biophys. Acta 1572, 364-386.
    • (2002) Biochem. Biophys. Acta , vol.1572 , pp. 364-386
    • East, L.1    Isacke, C.M.2
  • 7
    • 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
  • 8
    • 0347457065 scopus 로고    scopus 로고
    • Characterization of sugar binding by the mannose receptor family member, Endo180
    • East, L., Rushton, S., Taylor, M.E., and Isacke, C.M. (2002). Characterization of sugar binding by the mannose receptor family member, Endo180. 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
  • 9
    • 0034769468 scopus 로고    scopus 로고
    • The urokinase plasminogen activator receptor-associated protein/endo180 is coexpressed with its interaction partners urokinase plasminogen activator receptor and matrix metalloprotease-13 during osteogenesis
    • Engelholm, L.H. et al. (2001). The urokinase plasminogen activator receptor-associated protein/endo180 is coexpressed with its interaction partners urokinase plasminogen activator receptor and matrix metalloprotease-13 during osteogenesis. Lab. Invest. 81, 1403-1414.
    • (2001) Lab. Invest. , vol.81 , pp. 1403-1414
    • Engelholm, L.H.1
  • 10
    • 0037417411 scopus 로고    scopus 로고
    • uPARAP/Endo180 is essential for cellular uptake of collagen and promotes fibroblast collagen adhesion
    • Engelholm, L.H. et al. (2003). uPARAP/Endo180 is essential for cellular uptake of collagen and promotes fibroblast collagen adhesion. J. Cell Biol. 160, 1009-1015.
    • (2003) J. Cell Biol. , vol.160 , pp. 1009-1015
    • Engelholm, L.H.1
  • 11
    • 0021929277 scopus 로고
    • The digestion of phagocytosed collagen is inhibited by the proteinase inhibitors leupeptin and E-64
    • Everts, V., Beertsen, W., and Tigchelaar-Gutter, W. (1985). The digestion of phagocytosed collagen is inhibited by the proteinase inhibitors leupeptin and E-64. Coll. Relat. Res. 5, 315-336.
    • (1985) Coll. Relat. Res. , vol.5 , pp. 315-336
    • Everts, V.1    Beertsen, W.2    Tigchelaar-Gutter, W.3
  • 12
    • 0018858817 scopus 로고
    • Collagen: Molecular diversity in the body's protein scaffold
    • Eyre, D.R. (1980). Collagen: molecular diversity in the body's protein scaffold. Science 207, 1315-1322.
    • (1980) Science , vol.207 , pp. 1315-1322
    • Eyre, D.R.1
  • 13
    • 0035490884 scopus 로고    scopus 로고
    • The endocytic pathway: A mosaic of domains
    • Gruenberg, J. (2001). The endocytic pathway: a mosaic of domains. Nat. Rev. Mol. Cell. Biol. 2, 721-730.
    • (2001) Nat. Rev. Mol. Cell. Biol. , vol.2 , pp. 721-730
    • Gruenberg, J.1
  • 14
    • 0030058079 scopus 로고    scopus 로고
    • Intracellular fate of endocytosed collagen in rat liver endothelial cells
    • Hellevik, T., Bondevik, A., and Smedsrod, B. (1996). Intracellular fate of endocytosed collagen in rat liver endothelial cells. Exp. Cell Res. 223, 39-49.
    • (1996) Exp. Cell Res. , vol.223 , pp. 39-49
    • Hellevik, T.1    Bondevik, A.2    Smedsrod, B.3
  • 15
    • 0037199973 scopus 로고    scopus 로고
    • The C-type lectin receptor Endo180 displays internalization and recycling properties distinct from other members of the mannose receptor family
    • Howard, M.J., and Isacke, C.M. (2002). The C-type lectin receptor Endo180 displays internalization and recycling properties distinct from other members of the mannose receptor family. J. Biol. Chem. 277, 32320-32331.
    • (2002) J. Biol. Chem. , vol.277 , pp. 32320-32331
    • Howard, M.J.1    Isacke, C.M.2
  • 16
    • 0024330317 scopus 로고
    • Further localization of the gelatin-binding determinants within fibronectin. Active fragments devoid of type II homologous repeat modules
    • Ingham, K.C., Brew, S.A., and Migliorini, M.M. (1989). Further localization of the gelatin-binding determinants within fibronectin. Active fragments devoid of type II homologous repeat modules. J. Biol. Chem. 264, 16977-16980.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16977-16980
    • Ingham, K.C.1    Brew, S.A.2    Migliorini, M.M.3
  • 17
    • 0025284820 scopus 로고
    • p180, a novel recycling transmembrane glycoprotein with restricted cell type expression
    • Isacke, C.M., van der Geer, P., Hunter, T., and Trowbridge, I.S. (1990). p180, a novel recycling transmembrane glycoprotein with restricted cell type expression. Mol. Cell. Biol. 10, 2606-2618.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 2606-2618
    • Isacke, C.M.1    Van der Geer, P.2    Hunter, T.3    Trowbridge, I.S.4
  • 19
    • 0038485623 scopus 로고    scopus 로고
    • All six modules of the gelatin-binding domain of fibronectin are required for full affinity
    • Katagiri, Y., Brew, S.A., and Ingham, K.C. (2003). All six modules of the gelatin-binding domain of fibronectin are required for full affinity. J. Biol. Chem. 278, 11897-11902.
    • (2003) J. Biol. Chem. , vol.278 , pp. 11897-11902
    • Katagiri, Y.1    Brew, S.A.2    Ingham, K.C.3
  • 20
    • 0036391436 scopus 로고    scopus 로고
    • Matrix metalloproteinases and collagen catabolism
    • Lauer-Fields, J.L., Juska, D., and Fields, G.B. (2002). Matrix metalloproteinases and collagen catabolism. Biopolymers 66, 19-32.
    • (2002) Biopolymers , vol.66 , pp. 19-32
    • Lauer-Fields, J.L.1    Juska, D.2    Fields, G.B.3
  • 21
    • 0029763527 scopus 로고    scopus 로고
    • Role of integrins in regulation of collagen phagocytosis by human fibroblasts
    • Lee, W., Sodek, J., and McCulloch, C.A. (1996). Role of integrins in regulation of collagen phagocytosis by human fibroblasts. J. Cell. Physiol. 168, 695-704.
    • (1996) J. Cell. Physiol. , vol.168 , pp. 695-704
    • Lee, W.1    Sodek, J.2    McCulloch, C.A.3
  • 22
    • 0034749944 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Multifunctional effectors of inflammation in multiple sclerosis and bacterial meningitis
    • Leppert, D., Lindberg, R.L., Kappos, L., and Leib, S.L. (2001). Matrix metalloproteinases: multifunctional effectors of inflammation in multiple sclerosis and bacterial meningitis. Brain Res. Rev. 36, 249-257.
    • (2001) Brain Res. Rev. , vol.36 , pp. 249-257
    • Leppert, D.1    Lindberg, R.L.2    Kappos, L.3    Leib, S.L.4
  • 23
    • 0020065365 scopus 로고
    • Ultrastructural localization of type V collagen in rat kidney
    • Martinez-Hernandez, A., Gay, S., and Miller, E.J. (1982). Ultrastructural localization of type V collagen in rat kidney. J. Cell Biol. 92, 343-349.
    • (1982) J. Cell Biol. , vol.92 , pp. 343-349
    • Martinez-Hernandez, A.1    Gay, S.2    Miller, E.J.3
  • 24
    • 0027682593 scopus 로고
    • New members of the collagen superfamily
    • Mayne, R., and Brewton, R.G. (1993). New members of the collagen superfamily. Curr. Opin. Cell Biol. 5, 883-890.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 883-890
    • Mayne, R.1    Brewton, R.G.2
  • 25
    • 0034933664 scopus 로고    scopus 로고
    • The urokinase plasminogen activator receptor (uPAR) as a target for the diagnosis and therapy of cancer
    • Mazar, A.P. (2001). The urokinase plasminogen activator receptor (uPAR) as a target for the diagnosis and therapy of cancer. Anticancer Drugs 12, 387-400.
    • (2001) Anticancer Drugs , vol.12 , pp. 387-400
    • Mazar, A.P.1
  • 26
    • 0020619227 scopus 로고
    • A role for collagen phagocytosis by fibroblasts in scar remodeling: An ultrastructural stereologic study
    • McGaw, W.T., and Ten Cate, A.R. (1983). A role for collagen phagocytosis by fibroblasts in scar remodeling: an ultrastructural stereologic study. J. Invest. Dermatol. 81, 375-378.
    • (1983) J. Invest. Dermatol. , vol.81 , pp. 375-378
    • McGaw, W.T.1    Ten Cate, A.R.2
  • 27
    • 0029752791 scopus 로고    scopus 로고
    • Endocytosis and molecular sorting
    • Mellman, I. (1996). Endocytosis and molecular sorting. Annu. Rev. Cell Dev. Biol. 12, 575-625.
    • (1996) Annu. Rev. Cell Dev. Biol. , vol.12 , pp. 575-625
    • Mellman, I.1
  • 28
    • 0022820769 scopus 로고
    • Mapping the collagen-binding site of human fibronectin by expression in Escherichia coli
    • Owens, R.J., and Baralle, F.E. (1986). Mapping the collagen-binding site of human fibronectin by expression in Escherichia coli. EMBO J. 5, 2825-2830.
    • (1986) EMBO J. , vol.5 , pp. 2825-2830
    • Owens, R.J.1    Baralle, F.E.2
  • 29
    • 0018150997 scopus 로고
    • Pathology of collagen degradation. A review
    • Perez-Tamayo, R. (1978). Pathology of collagen degradation. A review. Am. J. Pathol. 92, 508-566.
    • (1978) Am. J. Pathol. , vol.92 , pp. 508-566
    • Perez-Tamayo, R.1
  • 30
    • 0031569351 scopus 로고    scopus 로고
    • Solution structure of a type 2 module from fibronectin: Implications for the structure and function of the gelatin-binding domain
    • Pickford, A.R., Potts, J.R., Bright, J.R., Phan, I., and Campbell, I.D. (1997). Solution structure of a type 2 module from fibronectin: implications for the structure and function of the gelatin-binding domain. Structure 5, 359-370.
    • (1997) Structure , vol.5 , pp. 359-370
    • Pickford, A.R.1    Potts, J.R.2    Bright, J.R.3    Phan, I.4    Campbell, I.D.5
  • 31
    • 0035794672 scopus 로고    scopus 로고
    • The hairpin structure of the (6)F1(1)F2(2)F2 fragment from human fibronectin enhances gelatin binding
    • Pickford, A.R., Smith, S.P., Staunton, D., Boyd, J., and Campbell, I.D. (2001). The hairpin structure of the (6)F1(1)F2(2)F2 fragment from human fibronectin enhances gelatin binding. EMBO J. 20, 1519-1529.
    • (2001) EMBO J. , vol.20 , pp. 1519-1529
    • Pickford, A.R.1    Smith, S.P.2    Staunton, D.3    Boyd, J.4    Campbell, I.D.5
  • 32
    • 0033818463 scopus 로고    scopus 로고
    • Urokinase receptor: A molecular organizer in cellular communication
    • Preissner, K.T., Kanse, S.M., and May, A.E. (2000). Urokinase receptor: a molecular organizer in cellular communication. Curr. Opin. Cell Biol. 12, 621-628.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 621-628
    • Preissner, K.T.1    Kanse, S.M.2    May, A.E.3
  • 33
    • 0029006974 scopus 로고
    • Collagens: Molecular biology, diseases, and potentials for therapy
    • Prockop, D.J., and Kivirikko, K.I. (1995). Collagens: molecular biology, diseases, and potentials for therapy. Annu. Rev. Biochem. 64, 403-434.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 403-434
    • Prockop, D.J.1    Kivirikko, K.I.2
  • 34
    • 0043180427 scopus 로고    scopus 로고
    • Three-dimensional interplay among the ligand binding domains of the uPAR-associated protein, Endo180
    • Epub ahead of print
    • Rivera-Calzada, A., Robertson, D., MacFayden, J.R., Boskovic, J., Isacke, C.M., and Llorca, O. (2003). Three-dimensional interplay among the ligand binding domains of the uPAR-associated protein, Endo180. EMBO Rep. (Epub ahead of print). Available at: http://emboreports.npgjournals.com. Accessed August 11, 2003.
    • (2003) EMBO Rep.
    • Rivera-Calzada, A.1    Robertson, D.2    MacFayden, J.R.3    Boskovic, J.4    Isacke, C.M.5    Llorca, O.6
  • 35
    • 0019302455 scopus 로고
    • Co-distribution of collagen types IV and AB2 in basement membranes and mesangium of the kidney, an immunoferritin study of ultrathin frozen sections
    • Roll, F.J., Madri, J.A., Albert, J., and Furthmayr, H. (1980). Co-distribution of collagen types IV and AB2 in basement membranes and mesangium of the kidney, an immunoferritin study of ultrathin frozen sections. J. Cell Biol. 85, 597-616.
    • (1980) J. Cell Biol. , vol.85 , pp. 597-616
    • Roll, F.J.1    Madri, J.A.2    Albert, J.3    Furthmayr, H.4
  • 36
    • 0037051665 scopus 로고    scopus 로고
    • Urokinase receptor-associated protein (uPARAP) is expressed in connection with malignant as well as benign lesions of the human breast and occurs in specific populations of stromal cells
    • Schnack Nielsen, B., Rank, F., Engelholm, L.H., Holm, A., Dano, K., and Behrendt, N. (2002). Urokinase receptor-associated protein (uPARAP) is expressed in connection with malignant as well as benign lesions of the human breast and occurs in specific populations of stromal cells. Int. J. Cancer 98, 656-664.
    • (2002) Int. J. Cancer , vol.98 , pp. 656-664
    • Schnack Nielsen, B.1    Rank, F.2    Engelholm, L.H.3    Holm, A.4    Dano, K.5    Behrendt, N.6
  • 37
    • 0034069897 scopus 로고    scopus 로고
    • Endo180, an endocytic recycling glycoprotein related to the macrophage mannose receptor is expressed on fibroblasts, endothelial cells and macrophages and functions as a lectin receptor
    • Sheikh, H., Yarwood, H., Ashworth, A., and Isacke, C.M. (2000). Endo180, an endocytic recycling glycoprotein related to the macrophage mannose receptor is expressed on fibroblasts, endothelial cells and macrophages and functions as a lectin receptor. J. Cell Sci. 113, 1021-1032.
    • (2000) J. Cell Sci. , vol.113 , pp. 1021-1032
    • Sheikh, H.1    Yarwood, H.2    Ashworth, A.3    Isacke, C.M.4
  • 38
    • 0028215098 scopus 로고
    • Collagen-binding recombinant fibronectin fragments containing type II domains
    • Skorstengaard, K., Holtet, T.L., Etzerodt, M., and Thogersen, H.C. (1994). Collagen-binding recombinant fibronectin fragments containing type II domains. FEBS Lett. 343, 47-50.
    • (1994) FEBS Lett. , vol.343 , pp. 47-50
    • Skorstengaard, K.1    Holtet, T.L.2    Etzerodt, M.3    Thogersen, H.C.4
  • 39
    • 0021806728 scopus 로고
    • Studies in vivo and in vitro on the uptake and degradation of soluble collagen alpha 1(I) chains in rat liver endothelial and Kupffer cells
    • Smedsrod, B., Johansson, S., and Pertoft, H. (1985). Studies in vivo and in vitro on the uptake and degradation of soluble collagen alpha 1(I) chains in rat liver endothelial and Kupffer cells. Biochem. J. 228, 415-424.
    • (1985) Biochem. J. , vol.228 , pp. 415-424
    • Smedsrod, B.1    Johansson, S.2    Pertoft, H.3
  • 40
  • 42
    • 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
  • 43
    • 0019514776 scopus 로고
    • A stereologic analysis of collagen phagocytosis by fibroblasts in three soft connective tissues with differing rates of collagen turnover
    • Svoboda, E.L., Shiga, A., and Deporter, D.A. (1981). A stereologic analysis of collagen phagocytosis by fibroblasts in three soft connective tissues with differing rates of collagen turnover. Anat. Rec. 199, 473-480.
    • (1981) Anat. Rec. , vol.199 , pp. 473-480
    • Svoboda, E.L.1    Shiga, A.2    Deporter, D.A.3
  • 44
    • 0034091793 scopus 로고    scopus 로고
    • Discoidin domain receptor 1 is activated independently of beta(1) integrin
    • Vogel, W., Brakebusch, C., Fassler, R., Alves, F., Ruggiero, F., and Pawson, T. (2000). Discoidin domain receptor 1 is activated independently of beta(1) integrin. J. Biol. Chem. 275, 5779-5784.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5779-5784
    • Vogel, W.1    Brakebusch, C.2    Fassler, R.3    Alves, F.4    Ruggiero, F.5    Pawson, T.6
  • 45
    • 0035085253 scopus 로고    scopus 로고
    • Discoidin domain receptor 1 tyrosine kinase has an essential role in mammary gland development
    • Vogel, W.F., Aszodi, A., Alves, F., and Pawson, T. (2001). Discoidin domain receptor 1 tyrosine kinase has an essential role in mammary gland development. Mol. Cell. Biol. 21, 2906-2917.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 2906-2917
    • Vogel, W.F.1    Aszodi, A.2    Alves, F.3    Pawson, T.4
  • 46
    • 0029835572 scopus 로고    scopus 로고
    • Characterization of a novel member of the macrophage mannose receptor type C lectin family
    • Wu, K., Yuan, J., and Lasky, L.A. (1996). Characterization of a novel member of the macrophage mannose receptor type C lectin family. J. Biol. Chem. 271, 21323-21330.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21323-21330
    • Wu, K.1    Yuan, J.2    Lasky, L.A.3
  • 47
    • 0025053161 scopus 로고
    • Distribution of type I collagen in human kidney diseases in comparison with type III collagen
    • Yoshioka, K., Tohda, M., Takemura, T., Akano, N., Matsubara, K., Ooshima, A., and Maki, S. (1990). Distribution of type I collagen in human kidney diseases in comparison with type III collagen. J. Pathol. 162, 141-148.
    • (1990) J. Pathol. , vol.162 , pp. 141-148
    • Yoshioka, K.1    Tohda, M.2    Takemura, T.3    Akano, N.4    Matsubara, K.5    Ooshima, A.6    Maki, S.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.