메뉴 건너뛰기




Volumn 385, Issue 3, 2009, Pages 902-911

Regulation of Collagen Fibrillogenesis by Cell-surface Expression of Kinase Dead DDR2

Author keywords

collagen; DDR2; fibrillogenesis; TEM

Indexed keywords

COLLAGEN FIBRIL; HYDROXYPROLINE; KINASE DEAD DISCOIDIN DOMAIN RECEPTOR 2; PROTEIN TYROSINE KINASE; UNCLASSIFIED DRUG;

EID: 58149105329     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.10.060     Document Type: Article
Times cited : (37)

References (37)
  • 1
    • 0026673475 scopus 로고
    • Collagen types. Molecular structure and tissue distribution
    • Burgeson R.E., and Nimni M.E. Collagen types. Molecular structure and tissue distribution. Clin. Orthop. Relat. Res. 282 (1992)
    • (1992) Clin. Orthop. Relat. Res. , vol.282
    • Burgeson, R.E.1    Nimni, M.E.2
  • 4
    • 34848851981 scopus 로고    scopus 로고
    • Fibromodulin binds collagen type I via Glu-353 and Lys-355 in leucine-rich repeat 11
    • Kalamajski S., and Oldberg A. Fibromodulin binds collagen type I via Glu-353 and Lys-355 in leucine-rich repeat 11. J. Biol. Chem. 282 (2007) 26740-26745
    • (2007) J. Biol. Chem. , vol.282 , pp. 26740-26745
    • Kalamajski, S.1    Oldberg, A.2
  • 5
    • 34547575826 scopus 로고    scopus 로고
    • SPARC regulates processing of procollagen I and collagen fibrillogenesis in dermal fibroblasts
    • Rentz T.J., Poobalarahi F., Bornstein P., Sage E.H., and Bradshaw A.D. SPARC regulates processing of procollagen I and collagen fibrillogenesis in dermal fibroblasts. J. Biol. Chem. 282 (2007) 22062-22071
    • (2007) J. Biol. Chem. , vol.282 , pp. 22062-22071
    • Rentz, T.J.1    Poobalarahi, F.2    Bornstein, P.3    Sage, E.H.4    Bradshaw, A.D.5
  • 6
    • 34547573300 scopus 로고    scopus 로고
    • Abnormal collagen fibrils in cartilage of matrilin-1/matrilin-3-deficient mice
    • Nicolae C., Ko Y.P., Miosge N., Niehoff A., Studer D., Enggist L., et al. Abnormal collagen fibrils in cartilage of matrilin-1/matrilin-3-deficient mice. J. Biol. Chem. 282 (2007) 22163-22175
    • (2007) J. Biol. Chem. , vol.282 , pp. 22163-22175
    • Nicolae, C.1    Ko, Y.P.2    Miosge, N.3    Niehoff, A.4    Studer, D.5    Enggist, L.6
  • 7
    • 0031309902 scopus 로고    scopus 로고
    • The discoidin domain receptor tyrosine kinases are activated by collagen
    • Vogel W., Gish G.D., Alves F., and Pawson T. The discoidin domain receptor tyrosine kinases are activated by collagen. Mol. Cell 1 (1997) 13-23
    • (1997) Mol. Cell , vol.1 , pp. 13-23
    • Vogel, W.1    Gish, G.D.2    Alves, F.3    Pawson, T.4
  • 8
    • 0031310941 scopus 로고    scopus 로고
    • An orphan receptor tyrosine kinase family whose members serve as nonintegrin collagen receptors
    • Shrivastava A., Radziejewski C., Campbell E., Kovac L., McGlynn M., Ryan T.E., et al. An orphan receptor tyrosine kinase family whose members serve as nonintegrin collagen receptors. Mol. Cell 1 (1997) 25-34
    • (1997) Mol. Cell , vol.1 , pp. 25-34
    • Shrivastava, A.1    Radziejewski, C.2    Campbell, E.3    Kovac, L.4    McGlynn, M.5    Ryan, T.E.6
  • 9
    • 33749189559 scopus 로고    scopus 로고
    • Identification of expressed genes characterizing long-term survival in malignant glioma patients
    • Yamanaka R., Arao T., Yajima N., Tsuchiya N., Homma J., Tanaka R., et al. Identification of expressed genes characterizing long-term survival in malignant glioma patients. Oncogene 25 (2006) 5994-6002
    • (2006) Oncogene , vol.25 , pp. 5994-6002
    • Yamanaka, R.1    Arao, T.2    Yajima, N.3    Tsuchiya, N.4    Homma, J.5    Tanaka, R.6
  • 10
    • 20544449915 scopus 로고    scopus 로고
    • Expression analysis of genes involved in brain tumor progression driven by retroviral insertional mutagenesis in mice
    • Johansson F.K., Goransson H., and Westermark B. Expression analysis of genes involved in brain tumor progression driven by retroviral insertional mutagenesis in mice. Oncogene 24 (2005) 3896-3905
    • (2005) Oncogene , vol.24 , pp. 3896-3905
    • Johansson, F.K.1    Goransson, H.2    Westermark, B.3
  • 11
    • 33847701326 scopus 로고    scopus 로고
    • Expression and mutation analysis of the discoidin domain receptors 1 and 2 in non-small cell lung carcinoma
    • Ford C.E., Lau S.K., Zhu C.Q., Andersson T., Tsao M.S., and Vogel W.F. Expression and mutation analysis of the discoidin domain receptors 1 and 2 in non-small cell lung carcinoma. Br. J. Cancer 96 (2007) 808-814
    • (2007) Br. J. Cancer , vol.96 , pp. 808-814
    • Ford, C.E.1    Lau, S.K.2    Zhu, C.Q.3    Andersson, T.4    Tsao, M.S.5    Vogel, W.F.6
  • 12
    • 42549099331 scopus 로고    scopus 로고
    • Upregulation of discoidin domain receptor 2 in nasopharyngeal carcinoma
    • Chua H.H., Yeh T.H., Wang Y.P., Huang Y.T., Sheen T.S., Lo Y.C., et al. Upregulation of discoidin domain receptor 2 in nasopharyngeal carcinoma. Head Neck 30 (2008) 427-436
    • (2008) Head Neck , vol.30 , pp. 427-436
    • Chua, H.H.1    Yeh, T.H.2    Wang, Y.P.3    Huang, Y.T.4    Sheen, T.S.5    Lo, Y.C.6
  • 13
    • 0036274730 scopus 로고    scopus 로고
    • Collagens, integrins, and the discoidin domain receptors in arterial occlusive disease
    • Franco C., Hou G., and Bendeck M. Collagens, integrins, and the discoidin domain receptors in arterial occlusive disease. Trends Cardiovasc. Med. 12 (2002) 143-148
    • (2002) Trends Cardiovasc. Med. , vol.12 , pp. 143-148
    • Franco, C.1    Hou, G.2    Bendeck, M.3
  • 14
    • 1942469341 scopus 로고    scopus 로고
    • Role of Discoidin domain receptors 1 and 2 in human smooth muscle cell-mediated collagen remodeling: potential implications in atherosclerosis and lymphangioleiomyomatosis
    • Ferri N., Carragher N.O., and Raines E.W. Role of Discoidin domain receptors 1 and 2 in human smooth muscle cell-mediated collagen remodeling: potential implications in atherosclerosis and lymphangioleiomyomatosis. Am. J. Pathol. 164 (2004) 1575-1585
    • (2004) Am. J. Pathol. , vol.164 , pp. 1575-1585
    • Ferri, N.1    Carragher, N.O.2    Raines, E.W.3
  • 15
    • 23044491502 scopus 로고    scopus 로고
    • Regular expression of discoidin domain receptor 2 in the improved adjuvant-induced animal model for rheumatoid arthritis
    • Li W., Zhang Y.Q., Liu X.P., Yao L.B., and Sun L. Regular expression of discoidin domain receptor 2 in the improved adjuvant-induced animal model for rheumatoid arthritis. Clin. Med. Sci. J. 20 (2005) 133-137
    • (2005) Clin. Med. Sci. J. , vol.20 , pp. 133-137
    • Li, W.1    Zhang, Y.Q.2    Liu, X.P.3    Yao, L.B.4    Sun, L.5
  • 16
    • 12844287561 scopus 로고    scopus 로고
    • Activation of the discoidin domain receptor 2 induces expression of matrix metalloproteinase 13 associated with osteoarthritis in mice
    • Xu L., Peng H., Wu D., Hu K., Goldring M.B., Olsen B.R., and Li Y. Activation of the discoidin domain receptor 2 induces expression of matrix metalloproteinase 13 associated with osteoarthritis in mice. J. Biol. Chem. 280 (2005) 548-555
    • (2005) J. Biol. Chem. , vol.280 , pp. 548-555
    • Xu, L.1    Peng, H.2    Wu, D.3    Hu, K.4    Goldring, M.B.5    Olsen, B.R.6    Li, Y.7
  • 17
    • 0032921366 scopus 로고    scopus 로고
    • Discoidin domain receptors: structural relations and functional implications
    • Vogel W. Discoidin domain receptors: structural relations and functional implications. FASEB J. 13 (1999) S77-S82
    • (1999) FASEB J. , vol.13
    • Vogel, W.1
  • 18
    • 33746901276 scopus 로고    scopus 로고
    • Discoidin domain receptor 2 inhibits fibrillogenesis of collagen type I
    • Mihai C., Iscru D.F., Druhan L.J., Elton T.S., and Agarwal G. Discoidin domain receptor 2 inhibits fibrillogenesis of collagen type I. J. Mol. Biol. 361 (2006) 864-876
    • (2006) J. Mol. Biol. , vol.361 , pp. 864-876
    • Mihai, C.1    Iscru, D.F.2    Druhan, L.J.3    Elton, T.S.4    Agarwal, G.5
  • 19
    • 33847122893 scopus 로고    scopus 로고
    • Interaction of discoidin domain receptor 1 with collagen type 1
    • Agarwal G., Mihai C., and Iscru D.F. Interaction of discoidin domain receptor 1 with collagen type 1. J. Mol. Biol. 367 (2007) 443-455
    • (2007) J. Mol. Biol. , vol.367 , pp. 443-455
    • Agarwal, G.1    Mihai, C.2    Iscru, D.F.3
  • 20
    • 21644439471 scopus 로고    scopus 로고
    • Overexpression of lysyl hydroxylase-2b leads to defective collagen fibrillogenesis and matrix mineralization
    • Pornprasertsuk S., Duarte W.R., Mochida Y., and Yamauchi M. Overexpression of lysyl hydroxylase-2b leads to defective collagen fibrillogenesis and matrix mineralization. J. Bone Miner. Res. 20 (2005) 81-87
    • (2005) J. Bone Miner. Res. , vol.20 , pp. 81-87
    • Pornprasertsuk, S.1    Duarte, W.R.2    Mochida, Y.3    Yamauchi, M.4
  • 21
    • 0035344510 scopus 로고    scopus 로고
    • Identification of two novel, kinase-deficient variants of discoidin domain receptor 1: differential expression in human colon cancer cell lines
    • Alves F., Saupe S., Ledwon M., Schaub F., Hiddemann W., and Vogel W.F. Identification of two novel, kinase-deficient variants of discoidin domain receptor 1: differential expression in human colon cancer cell lines. FASEB J. 15 (2001) 1321-1323
    • (2001) FASEB J. , vol.15 , pp. 1321-1323
    • Alves, F.1    Saupe, S.2    Ledwon, M.3    Schaub, F.4    Hiddemann, W.5    Vogel, W.F.6
  • 22
    • 0028799694 scopus 로고
    • Distinct structural characteristics of discoidin I subfamily receptor tyrosine kinases and complementary expression in human cancer
    • Alves F., Vogel W., Mossie K., Millauer B., Hofler H., and Ullrich A. Distinct structural characteristics of discoidin I subfamily receptor tyrosine kinases and complementary expression in human cancer. Oncogene 10 (1995) 609-618
    • (1995) Oncogene , vol.10 , pp. 609-618
    • Alves, F.1    Vogel, W.2    Mossie, K.3    Millauer, B.4    Hofler, H.5    Ullrich, A.6
  • 23
    • 0027442939 scopus 로고
    • Structure, expression and chromosomal mapping of TKT from man and mouse: a new subclass of receptor tyrosine kinases with a factor VIII-like domain
    • Karn T., Holtrich U., Brauninger A., Bohme B., Wolf G., Rubsamen-Waigmann H., and Strebhardt K. Structure, expression and chromosomal mapping of TKT from man and mouse: a new subclass of receptor tyrosine kinases with a factor VIII-like domain. Oncogene 8 (1993) 3433-3440
    • (1993) Oncogene , vol.8 , pp. 3433-3440
    • Karn, T.1    Holtrich, U.2    Brauninger, A.3    Bohme, B.4    Wolf, G.5    Rubsamen-Waigmann, H.6    Strebhardt, K.7
  • 24
    • 0027955470 scopus 로고
    • Structure and expression of the Tyro 10 receptor tyrosine kinase
    • Lai C., and Lemke G. Structure and expression of the Tyro 10 receptor tyrosine kinase. Oncogene 9 (1994) 877-883
    • (1994) Oncogene , vol.9 , pp. 877-883
    • Lai, C.1    Lemke, G.2
  • 26
    • 0037125948 scopus 로고    scopus 로고
    • Binding of discoidin domain receptor 2 to collagen I: an atomic force microscopy investigation
    • Agarwal G., Kovac L., Radziejewski C., and Samuelsson S. Binding of discoidin domain receptor 2 to collagen I: an atomic force microscopy investigation. Biochemistry 41 (2002) 11091-11098
    • (2002) Biochemistry , vol.41 , pp. 11091-11098
    • Agarwal, G.1    Kovac, L.2    Radziejewski, C.3    Samuelsson, S.4
  • 27
    • 42449119742 scopus 로고    scopus 로고
    • Characterization of high affinity binding motifs for the discoidin domain recptor DDR2 in collagen
    • Konitsiotis A.D., Raynal N., Bihan D., Hohenester E., Farndale R.W., and Leitinger B. Characterization of high affinity binding motifs for the discoidin domain recptor DDR2 in collagen. J. Biol. Chem. 283 (2008) 6861-6868
    • (2008) J. Biol. Chem. , vol.283 , pp. 6861-6868
    • Konitsiotis, A.D.1    Raynal, N.2    Bihan, D.3    Hohenester, E.4    Farndale, R.W.5    Leitinger, B.6
  • 28
    • 0037040286 scopus 로고    scopus 로고
    • Mapping the ligand-binding sites and disease-associated mutations on the most abundant protein in the human, type I collagen
    • Di Lullo G.A., Sweeney S.M., Korkko J., Ala-Kokko L., and San Antonio J.D. Mapping the ligand-binding sites and disease-associated mutations on the most abundant protein in the human, type I collagen. J. Biol. Chem. 277 (2002) 4223-4231
    • (2002) J. Biol. Chem. , vol.277 , pp. 4223-4231
    • Di Lullo, G.A.1    Sweeney, S.M.2    Korkko, J.3    Ala-Kokko, L.4    San Antonio, J.D.5
  • 29
    • 0027154689 scopus 로고
    • Regulation of corneal collagen fibrillogenesis in vitro by corneal proteoglycan (lumican and decorin) core proteins
    • Rada J.A., Cornuet P.K., and Hassell J.R. Regulation of corneal collagen fibrillogenesis in vitro by corneal proteoglycan (lumican and decorin) core proteins. Exp. Eye Res. 56 (1993) 635-648
    • (1993) Exp. Eye Res. , vol.56 , pp. 635-648
    • Rada, J.A.1    Cornuet, P.K.2    Hassell, J.R.3
  • 30
    • 34547796856 scopus 로고    scopus 로고
    • The glycosaminoglycan chain of decorin plays an important role in collagen fibril formation at the early stages of fibrillogenesis
    • Rühland C., Schönherr E., Robenek H., Hansen U., Iozzo R.V., Bruckner P., and Seidler D.G. The glycosaminoglycan chain of decorin plays an important role in collagen fibril formation at the early stages of fibrillogenesis. FEBS J. 274 (2007) 4246-4255
    • (2007) FEBS J. , vol.274 , pp. 4246-4255
    • Rühland, C.1    Schönherr, E.2    Robenek, H.3    Hansen, U.4    Iozzo, R.V.5    Bruckner, P.6    Seidler, D.G.7
  • 31
    • 0033605648 scopus 로고    scopus 로고
    • Recombinant human type II collagens with low and high levels of hydroxylysine and its glycosylated forms show marked differences in fibrillgenesis in vitro
    • Notbohm H., Nokelainen M., Myllyharju J., Fietzek P.P., Müller P.K., and Kivirikko K.I. Recombinant human type II collagens with low and high levels of hydroxylysine and its glycosylated forms show marked differences in fibrillgenesis in vitro. J. Biol. Chem. 274 (1999) 8988-8992
    • (1999) J. Biol. Chem. , vol.274 , pp. 8988-8992
    • Notbohm, H.1    Nokelainen, M.2    Myllyharju, J.3    Fietzek, P.P.4    Müller, P.K.5    Kivirikko, K.I.6
  • 32
    • 50249101041 scopus 로고    scopus 로고
    • Non-enzymatic glycation of type I collagen diminishes collagen-proteoglycan binding and weakens cell adhesion
    • Reigle K.L., Di Lullo G., Turner K.R., Last J.A., Chervoneva I., Birk D.E., et al. Non-enzymatic glycation of type I collagen diminishes collagen-proteoglycan binding and weakens cell adhesion. J. Cell Biochem. 104 (2008) 1684-1698
    • (2008) J. Cell Biochem. , vol.104 , pp. 1684-1698
    • Reigle, K.L.1    Di Lullo, G.2    Turner, K.R.3    Last, J.A.4    Chervoneva, I.5    Birk, D.E.6
  • 33
    • 0027337717 scopus 로고
    • Collagen fibrillogenesis in a three-dimensional fibroblast cell culture system
    • Contard P., Lloydstone J., Perlish J.S., and Fleischmajer R. Collagen fibrillogenesis in a three-dimensional fibroblast cell culture system. Cell Tissue Res. 273 (1993) 571-575
    • (1993) Cell Tissue Res. , vol.273 , pp. 571-575
    • Contard, P.1    Lloydstone, J.2    Perlish, J.S.3    Fleischmajer, R.4
  • 34
    • 0025343595 scopus 로고
    • Collagen Fibrillogenesis in vitro: interaction of types I and V collagen regulates fibril diameter
    • Birk D.E., Fitch J.M., Babiarz J.M., Doane K.J., and Linesenmayer T.F. Collagen Fibrillogenesis in vitro: interaction of types I and V collagen regulates fibril diameter. J. Cell Sci. 95 (1990) 649-657
    • (1990) J. Cell Sci. , vol.95 , pp. 649-657
    • Birk, D.E.1    Fitch, J.M.2    Babiarz, J.M.3    Doane, K.J.4    Linesenmayer, T.F.5
  • 35
    • 0034988084 scopus 로고    scopus 로고
    • The collagen receptor DDR2 regulates proliferation and its elimination leads to dwarfism
    • Labrador J.P., Azcoitia V., Tuckermann J., Lin C., Olaso E., Mañes S., et al. The collagen receptor DDR2 regulates proliferation and its elimination leads to dwarfism. EMBO Rep. 2 (2001) 446-452
    • (2001) EMBO Rep. , vol.2 , pp. 446-452
    • Labrador, J.P.1    Azcoitia, V.2    Tuckermann, J.3    Lin, C.4    Olaso, E.5    Mañes, S.6
  • 36
    • 21044458339 scopus 로고    scopus 로고
    • Expression of discoidin domain receptor 2 (DDR2) in the developing heart
    • Morales M.O., Price R.L., and Goldsmith E.C. Expression of discoidin domain receptor 2 (DDR2) in the developing heart. Microsc. Microanal. 11 (2005) 260-267
    • (2005) Microsc. Microanal. , vol.11 , pp. 260-267
    • Morales, M.O.1    Price, R.L.2    Goldsmith, E.C.3
  • 37
    • 0029881336 scopus 로고    scopus 로고
    • A simplified method for the analysis of hydroxyproline in biological tissues
    • Reddy G.K., and Enwemeka C.S. A simplified method for the analysis of hydroxyproline in biological tissues. Clin. Biochem. 29 (1996) 225-229
    • (1996) Clin. Biochem. , vol.29 , pp. 225-229
    • Reddy, G.K.1    Enwemeka, C.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.