메뉴 건너뛰기




Volumn 288, Issue 2, 2013, Pages 995-1008

The C-terminal peptide of chondroadherin modulates cellular activity by selectively binding to heparan sulfate chains

Author keywords

[No Author keywords available]

Indexed keywords

C-TERMINAL PEPTIDES; C-TERMINAL SEQUENCES; CELL LINES; CELL SURFACE RECEPTORS; CELL SURFACES; CELLULAR ACTIVITIES; CHONDROSARCOMA; CYTOSKELETONS; DIFFERENTIAL REGULATION; DOSE-DEPENDENT MANNER; FOCAL ADHESIONS; GLYCOSAMINOGLYCANS; HEPARAN SULFATES; HEPARIN BINDING; INTEGRIN RECEPTORS; INTRACELLULAR SIGNALING; LEUCINE-RICH REPEATS; MURINE OSTEOBLASTS; PROTEIN CORE; PROTEOGLYCANS; TYPE II;

EID: 84872358077     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.430512     Document Type: Article
Times cited : (21)

References (42)
  • 1
    • 0002565653 scopus 로고
    • Cartilage specific collagens. Structural studies
    • Kuettner, K. E., Schleyerbach, R., Peyron, J. G., and Hascall, V. C. eds Raven Press, New York
    • Eyre, D., Wu, J. J., and Woods, P. (1992) Cartilage specific collagens. Structural studies. in Articular Cartilage and Osteoarthritis. (Kuettner, K. E., Schleyerbach, R., Peyron, J. G., and Hascall, V. C. eds) pp. 118-131, Raven Press, New York
    • (1992) Articular Cartilage and Osteoarthritis , pp. 118-131
    • Eyre, D.1    Wu, J.J.2    Woods, P.3
  • 2
    • 0027717615 scopus 로고
    • Binding of fibromodulin and decorin to separate sites on fibrillar collagens
    • Hedbom, E., and Heinegård, D. (1993) Binding of fibromodulin and decorin to separate sites on fibrillar collagens. J. Biol. Chem. 268, 27307-27312
    • (1993) J. Biol. Chem. , vol.268 , pp. 27307-27312
    • Hedbom, E.1    Heinegård, D.2
  • 3
    • 0032493665 scopus 로고    scopus 로고
    • Cartilage oligomeric matrix protein shows high affinity zinc-dependent interaction with triple helical collagen
    • DOI 10.1074/jbc.273.32.20397
    • Rosenberg, K., Olsson, H., Mörgelin, M., and Heinegård, D. (1998) Cartilage oligomeric matrix protein shows high affinity zinc-dependent interaction with triple helical collagen. J. Biol. Chem. 273, 20397-20403 (Pubitemid 28377606)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.32 , pp. 20397-20403
    • Rosenberg, K.1    Olsson, H.2    Morgelin, M.3    Heinegard, D.4
  • 4
    • 0021715115 scopus 로고
    • Specific inhibition of type I and type II collagen fibrillogenesis by the small proteoglycan of tendon
    • Vogel, K. G., Paulsson, M., and Heinegård, D. (1984) Specific inhibition of type I and type II collagen fibrillogenesis by the small proteoglycan of tendon. Biochem. J. 223, 587-597 (Pubitemid 15209051)
    • (1984) Biochemical Journal , vol.223 , Issue.3 , pp. 587-597
    • Vogel, K.G.1    Paulsson, M.2    Heinegard, D.3
  • 5
    • 0040973727 scopus 로고    scopus 로고
    • The matrilins: A novel family of oligomeric extracellular matrix proteins
    • Deák, F., Wagener, R., Kiss, I., and Paulsson, M. (1999) The matrilins: a novel family of oligomeric extracellular matrix proteins. Matrix Biol. 18, 55-64
    • (1999) Matrix Biol. , vol.18 , pp. 55-64
    • Deák, F.1    Wagener, R.2    Kiss, I.3    Paulsson, M.4
  • 6
    • 37349085705 scopus 로고    scopus 로고
    • Cell biology, biochemistry, and molecular biology of articular cartilage in osteoarthritis
    • Moskowitz, R. W., Altman, R., Buckwalter, J., Goldberg, V. M., and Hochberg, M., eds Wolters Kluwer/Lippincott, Philadelphia
    • Sandell, L. J., Heinegård, D., and Herring, T. (2007) Cell biology, biochemistry, and molecular biology of articular cartilage in osteoarthritis. in Osteoarthritis (Moskowitz, R. W., Altman, R., Buckwalter, J., Goldberg, V. M., and Hochberg, M., eds) pp. 73-106, Wolters Kluwer/Lippincott, Philadelphia
    • (2007) Osteoarthritis , pp. 73-106
    • Sandell, L.J.1    Heinegård, D.2    Herring, T.3
  • 7
    • 0141621124 scopus 로고    scopus 로고
    • Complexes of matrilin-1 and biglycan or decorin connect collagen VI microfibrils to both collagen II and aggrecan
    • DOI 10.1074/jbc.M304638200
    • Wiberg, C., Klatt, A. R., Wagener, R., Paulsson, M., Bateman, J. F., Heinegård, D., and Mörgelin, M. (2003) Complexes of matrilin-1 and biglycan or decorin connect collagen VI microfibrils to both collagen II and aggrecan. J. Biol. Chem. 278, 37698-37704 (Pubitemid 37175294)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.39 , pp. 37698-37704
    • Wiberg, C.1    Klatt, A.R.2    Wagener, R.3    Paulsson, M.4    Bateman, J.F.5    Heinegard, D.6    Morgelin, M.7
  • 8
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes, R. O. (1992) Integrins: Versatility, modulation, and signaling in cell adhesion. Cell 69, 11-25
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 9
    • 0031703639 scopus 로고    scopus 로고
    • Syndecan proteoglycans and cell adhesion
    • DOI 10.1016/S0945-053X(98)90095-6
    • Woods, A., Oh, E. S., and Couchman, J. R. (1998) Syndecan proteoglycans and cell adhesion. Matrix Biol. 17, 477-483 (Pubitemid 28566882)
    • (1998) Matrix Biology , vol.17 , Issue.7 , pp. 477-483
    • Woods, A.1    Oh, E.-S.2    Couchman, J.R.3
  • 10
    • 14244264636 scopus 로고    scopus 로고
    • Collagenous transmembrane proteins: Recent insights into biology and pathology
    • DOI 10.1074/jbc.R400034200
    • Franzke, C. W., Bruckner, P., and Bruckner-Tuderman, L. (2005) Collagenous transmembrane proteins: recent insights into biology and pathology. J. Biol. Chem. 280, 4005-4008 (Pubitemid 40288560)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.6 , pp. 4005-4008
    • Franzke, C.-W.1    Bruckner, P.2    Bruckner-Tuderman, L.3
  • 11
    • 0038607924 scopus 로고    scopus 로고
    • Molecular analysis of collagen binding by the human discoidin domain receptors, DDR1 and DDR2: Identification of collagen binding sites in DDR2
    • Leitinger, B. (2003) Molecular analysis of collagen binding by the human discoidin domain receptors, DDR1 and DDR2: Identification of collagen binding sites in DDR2. J. Biol. Chem. 278, 16761-16769
    • (2003) J. Biol. Chem. , vol.278 , pp. 16761-16769
    • Leitinger, B.1
  • 12
    • 0025282411 scopus 로고
    • CD44 is the principal cell surface receptor for hyaluronate
    • Aruffo, A., Stamenkovic, I., Melnick, M., Underhill, C. B., and Seed, B. (1990) CD44 is the principal cell surface receptor for hyaluronate. Cell 61, 1303-1313
    • (1990) Cell , vol.61 , pp. 1303-1313
    • Aruffo, A.1    Stamenkovic, I.2    Melnick, M.3    Underhill, C.B.4    Seed, B.5
  • 13
    • 1642473157 scopus 로고    scopus 로고
    • The transforming growth factor-β superfamily of receptors
    • de Caestecker, M. (2004) The transforming growth factor-β superfamily of receptors. Cytokine Growth Factor Rev. 15, 1-11
    • (2004) Cytokine Growth Factor Rev. , vol.15 , pp. 1-11
    • De Caestecker, M.1
  • 14
    • 0034142030 scopus 로고    scopus 로고
    • Syndecan-4 binding to the high affinity heparin-binding domain of fibronectin drives focal adhesion formation in fibroblasts
    • DOI 10.1006/abbi.1999.1607
    • Woods, A., Longley, R. L., Tumova, S., and Couchman, J. R. (2000) Syndecan-4 binding to the high affinity heparin-binding domain of fibronectin drives focal adhesion formation in fibroblasts. Arch. Biochem. Biophys. 374, 66-72 (Pubitemid 30084409)
    • (2000) Archives of Biochemistry and Biophysics , vol.374 , Issue.1 , pp. 66-72
    • Woods, A.1    Longley, R.L.2    Tumova, S.3    Couchman, J.R.4
  • 16
    • 33644788011 scopus 로고    scopus 로고
    • Integrin-syndecan cooperation governs the assembly of signalling complexes during cell spreading
    • discussion 188-192, 223-230
    • Humphries, M. J., Mostafavi-Pour, Z., Morgan, M. R., Deakin, N. O., Messent, A. J., and Bass, M. D. (2005) Integrin-syndecan cooperation governs the assembly of signalling complexes during cell spreading. Novartis Found. Symp. 269, 178-188; discussion 188-192, 223-230
    • (2005) Novartis Found. Symp. , vol.269 , pp. 178-188
    • Humphries, M.J.1    Mostafavi-Pour, Z.2    Morgan, M.R.3    Deakin, N.O.4    Messent, A.J.5    Bass, M.D.6
  • 17
    • 36448970493 scopus 로고    scopus 로고
    • Synergistic control of cell adhesion by integrins and syndecans
    • DOI 10.1038/nrm2289, PII NRM2289
    • Morgan, M. R., Humphries, M. J., and Bass, M. D. (2007) Synergistic control of cell adhesion by integrins and syndecans. Nat. Rev. Mol. Cell Biol. 8, 957-969 (Pubitemid 350174639)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.12 , pp. 957-969
    • Morgan, M.R.1    Humphries, M.J.2    Bass, M.D.3
  • 18
    • 0034729437 scopus 로고    scopus 로고
    • Syndecan-regulated receptor signaling
    • Rapraeger, A. C. (2000) Syndecan-regulated receptor signaling. J. Cell Biol. 149, 995-998
    • (2000) J. Cell Biol. , vol.149 , pp. 995-998
    • Rapraeger, A.C.1
  • 20
    • 0028106341 scopus 로고
    • The structure of a 38-kDa leucine-rich protein (chondroadherin) isolated from bovine cartilage
    • Neame, P. J., Sommarin, Y., Boynton, R. E., and Heinegård, D. (1994) The structure of a 38-kDa leucine-rich protein (chondroadherin) isolated from bovine cartilage. J. Biol. Chem. 269, 21547-21554 (Pubitemid 24274787)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.34 , pp. 21547-21554
    • Neame, P.J.1    Sommarin, Y.2    Boynton, R.E.3    Heinegard, D.4
  • 21
    • 70350366783 scopus 로고    scopus 로고
    • The tyrosine sulfate-rich domains of the LRR proteins fibromodulin and osteoadherin bind motifs of basic clusters in a variety of heparin-binding proteins including bioactive factors
    • Tillgren, V., Önnerfjord, P., Haglund, L., and Heinegård, D. (2009) The tyrosine sulfate-rich domains of the LRR proteins fibromodulin and osteoadherin bind motifs of basic clusters in a variety of heparin-binding proteins including bioactive factors. J. Biol. Chem. 284, 28543-28553
    • (2009) J. Biol. Chem. , vol.284 , pp. 28543-28553
    • Tillgren, V.1    Önnerfjord, P.2    Haglund, L.3    Heinegård, D.4
  • 23
    • 0030610917 scopus 로고    scopus 로고
    • Integrin α2β1 is a receptor for the cartilage matrix protein chondroadherin
    • Camper, L., Heinegârd, D., and Lundgren-Åkerlund, E. (1997) Integrin α2β1 is a receptor for the cartilage matrix protein chondroadherin. J. Cell Biol. 138, 1159-1167
    • (1997) J. Cell Biol. , vol.138 , pp. 1159-1167
    • Camper, L.1    Heinegârd, D.2    Lundgren-Åkerlund, E.3
  • 24
    • 79952787377 scopus 로고    scopus 로고
    • Identification and characterization of the integrin α2β1 binding motif in chondroadherin mediating cell attachment
    • Haglund, L., Tillgren, V., Addis, L., Wenglén, C., Recklies, A., and Heinegård, D. (2011) Identification and characterization of the integrin α2β1 binding motif in chondroadherin mediating cell attachment. J. Biol. Chem. 286, 3925-3934
    • (2011) J. Biol. Chem. , vol.286 , pp. 3925-3934
    • Haglund, L.1    Tillgren, V.2    Addis, L.3    Wenglén, C.4    Recklies, A.5    Heinegård, D.6
  • 25
    • 0024422641 scopus 로고
    • Chondrocyte-matrix interactions. Attachment to proteins isolated from cartilage
    • DOI 10.1016/0014-4827(89)90376-5
    • Sommarin, Y., Larsson, T., and Heinegård, D. (1989) Chondrocyte-matrix interactions. Attachment to proteins isolated from cartilage. Exp. Cell Res. 184, 181-192 (Pubitemid 19233398)
    • (1989) Experimental Cell Research , vol.184 , Issue.1 , pp. 181-192
    • Sommarin, Y.1    Larsson, T.2    Heinegard, D.3
  • 27
    • 0027079913 scopus 로고
    • Induction of synthesis and release of interleukin-8 from human articular chondrocytes and cartilage explants
    • DOI 10.1002/art.1780351215
    • Recklies, A. D., and Golds, E. E. (1992) Induction of synthesis and release of interleukin-8 from human articular chondrocytes and cartilage explants. Arthritis Rheum. 35, 1510-1519 (Pubitemid 23013659)
    • (1992) Arthritis and Rheumatism , vol.35 , Issue.12 , pp. 1510-1519
    • Recklies, A.D.1    Golds, E.E.2
  • 28
    • 0020619185 scopus 로고
    • Specific interaction between cartilage proteoglycans and hyaluronic acid at the chondrocyte cell surface
    • Sommarin, Y., and Heinegård, D. (1983) Specific interaction between cartilage proteoglycans and hyaluronic acid at the chondrocyte cell surface. Biochem. J. 214, 777-784
    • (1983) Biochem. J. , vol.214 , pp. 777-784
    • Sommarin, Y.1    Heinegård, D.2
  • 29
    • 0141621157 scopus 로고    scopus 로고
    • Type XIII collagen and some other transmembrane collagens contain two separate coiled-coil motifs, which may function as independent oligomerization domains
    • DOI 10.1074/jbc.M305974200
    • Latvanlehto, A., Snellman, A., Tu, H., and Pihlajaniemi, T. (2003) Type XIII collagen and some other transmembrane collagens contain two separate coiled-coil motifs, which may function as independent oligomerization domains. J. Biol. Chem. 278, 37590-37599 (Pubitemid 37175282)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.39 , pp. 37590-37599
    • Latvanlehto, A.1    Snellman, A.2    Tu, H.3    Pihlajaniemi, T.4
  • 30
    • 0021343351 scopus 로고
    • Measurement of cell numbers by means of the endogenous enzyme hexosaminidase. Applications to detection of lymphokines and cell surface antigens
    • Landegren, U. (1984) Measurement of cell numbers by means of the endogenous enzyme hexosaminidase. Applications to detection of lymphokines and cell surface antigens. J. Immunol. Methods 67, 379-388
    • (1984) J. Immunol. Methods , vol.67 , pp. 379-388
    • Landegren, U.1
  • 31
    • 0024584913 scopus 로고
    • Molecular modeling of proteinglycosaminoglycan interactions
    • Cardin, A. D., and Weintraub, H. J. (1989) Molecular modeling of proteinglycosaminoglycan interactions. Arteriosclerosis 9, 21-32
    • (1989) Arteriosclerosis , vol.9 , pp. 21-32
    • Cardin, A.D.1    Weintraub, H.J.2
  • 34
    • 0037968622 scopus 로고    scopus 로고
    • Syndecan-1 and -4 synthesized simultaneously by mouse mammary gland epithelial cells bear heparan sulfate chains that are apparently structurally indistinguishable
    • DOI 10.1074/jbc.M209658200
    • Zako, M., Dong, J., Goldberger, O., Bernfield, M., Gallagher, J. T., and Deakin, J. A. (2003) Syndecan-1 and -4 synthesized simultaneously by mouse mammary gland epithelial cells bear heparan sulfate chains that are apparently structurally indistinguishable. J. Biol. Chem. 278, 13561-13569 (Pubitemid 36800132)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.15 , pp. 13561-13569
    • Zako, M.1    Dong, J.2    Goldberger, O.3    Bernfield, M.4    Gallagher, J.T.5    Deakins, J.A.6
  • 37
    • 0024506757 scopus 로고
    • Phorbol ester modulation of integrin-mediated cell adhesion: A postreceptor event
    • DOI 10.1083/jcb.108.5.1925
    • Danilov, Y. N., and Juliano, R. L. (1989) Phorbol ester modulation of integrin-mediated cell adhesion: a postreceptor event. J. Cell Biol. 108, 1925-1933 (Pubitemid 19130525)
    • (1989) Journal of Cell Biology , vol.108 , Issue.5 , pp. 1925-1933
    • Danilov, Y.N.1    Juliano, R.L.2
  • 38
    • 0037031817 scopus 로고    scopus 로고
    • Syndecan-4 modulates focal adhesion kinase phosphorylation
    • DOI 10.1074/jbc.M201283200
    • Wilcox-Adelman, S. A., Denhez, F., and Goetinck, P. F. (2002) Syndecan-4 modulates focal adhesion kinase phosphorylation. J. Biol. Chem. 277, 32970-32977 (Pubitemid 34984811)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.36 , pp. 32970-32977
    • Wilcox-Adelman, S.A.1    Denhez, F.2    Goetinck, P.F.3
  • 39
    • 63449129028 scopus 로고    scopus 로고
    • Syndecan-1 regulates αvβ3 and αvβ5 integrin activation during angiogenesis and is blocked by synstatin, a novel peptide inhibitor
    • Beauvais, D. M., Ell, B. J., McWhorter, A. R., and Rapraeger, A. C. (2009) Syndecan-1 regulates αvβ3 and αvβ5 integrin activation during angiogenesis and is blocked by synstatin, a novel peptide inhibitor. J. Exp. Med. 206, 691-705
    • (2009) J. Exp. Med. , vol.206 , pp. 691-705
    • Beauvais, D.M.1    Ell, B.J.2    McWhorter, A.R.3    Rapraeger, A.C.4
  • 41
    • 0002352152 scopus 로고
    • Cartilage matrix proteins
    • (Kuettner, K. E., Schleyerbach, R., Peyron, J.G., and Hascall, V. C., eds) Raven Press, New York
    • Heinegård, D., and Pimentel, R. (1992) Cartilage matrix proteins. in Articular Cartilage and Osteoarthritis (Kuettner, K. E., Schleyerbach, R., Peyron, J.G., and Hascall, V. C., eds) pp, 95-111, Raven Press, New York
    • (1992) Articular Cartilage and Osteoarthritis , pp. 95-111
    • Heinegård, D.1    Pimentel, R.2
  • 42
    • 0015516429 scopus 로고
    • Structural studies on cartilage collagen employing limited cleavage and solubilization with pepsin
    • Miller, E. J. (1972) Structural studies on cartilage collagen employing limited cleavage and solubilization with pepsin. Biochemistry 11, 4903-4909
    • (1972) Biochemistry , vol.11 , pp. 4903-4909
    • Miller, E.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.