메뉴 건너뛰기




Volumn 144, Issue 5, 2008, Pages 625-633

Intercellular accumulation of type V collagen fibrils in accordance with cell aggregation

Author keywords

Accumulation of collagen fibrils; Cell cementing; Cell collagen interaction; Clump formation; Type V collagen fibrils

Indexed keywords

COLLAGEN FIBRIL; COLLAGEN TYPE 5;

EID: 55449084817     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvn109     Document Type: Article
Times cited : (10)

References (45)
  • 1
    • 0025792023 scopus 로고
    • Collagen family of proteins
    • van der Rest, M. and Garrone, R. (1991) Collagen family of proteins. FASEB J. 5, 2814-2823
    • (1991) FASEB J , vol.5 , pp. 2814-2823
    • van der Rest, M.1    Garrone, R.2
  • 2
    • 0028679665 scopus 로고
    • Extracellular matrix. 1: Fibril-forming collagens
    • Kadler, K. (1994) Extracellular matrix. 1: fibril-forming collagens. Prot. Profile 1, 519-638
    • (1994) Prot. Profile , vol.1 , pp. 519-638
    • Kadler, K.1
  • 3
    • 0347418197 scopus 로고    scopus 로고
    • Collagens, modifying enzymes and their mutations in humans, flies and worms
    • Myllyharju, J. and Kivirikko, K.I. (2004) Collagens, modifying enzymes and their mutations in humans, flies and worms. Trends Genet. 20, 33-43
    • (2004) Trends Genet , vol.20 , pp. 33-43
    • Myllyharju, J.1    Kivirikko, K.I.2
  • 4
    • 0021232602 scopus 로고
    • Localization of type V collagen and type IV collagen in human cornea, lung, and skin. Immunohistochemical evidence by anti-collagen antibodies characterized by immunoelectroblotting
    • Konomi, H., Hayashi, T., Nakayasu, K., and Arima, M. (1984) Localization of type V collagen and type IV collagen in human cornea, lung, and skin. Immunohistochemical evidence by anti-collagen antibodies characterized by immunoelectroblotting. Am. J. Pathol. 116, 417-426
    • (1984) Am. J. Pathol , vol.116 , pp. 417-426
    • Konomi, H.1    Hayashi, T.2    Nakayasu, K.3    Arima, M.4
  • 5
    • 0022605642 scopus 로고
    • In vitro formation of hybrid fibrils of type V collagen and type I collagen. Limited growth of type I collagen into thick fibrils by type V collagen
    • Adachi, E. and Hayashi, T. (1986) In vitro formation of hybrid fibrils of type V collagen and type I collagen. Limited growth of type I collagen into thick fibrils by type V collagen. Connect. Tissue Res. 14, 257-266
    • (1986) Connect. Tissue Res , vol.14 , pp. 257-266
    • Adachi, E.1    Hayashi, T.2
  • 6
    • 55449115200 scopus 로고    scopus 로고
    • Fessler, J.H. and Fessler, L.I. (1987) Type V collagen in Structure and Function of Collagen Types (Mayne, R. and Burgeson, R., eds.) pp. 81-103, Academic Press, New York.
    • Fessler, J.H. and Fessler, L.I. (1987) Type V collagen in Structure and Function of Collagen Types (Mayne, R. and Burgeson, R., eds.) pp. 81-103, Academic Press, New York.
  • 7
    • 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.P., Doane, K.J., and Linsenmayer, T.F. (1990) Collagen fibrillogenesis in vitro: interaction of types I and V collagen regulates fibril diameter. J. Cell Sci. 95, 649-657
    • (1990) J. Cell Sci , vol.95 , pp. 649-657
    • Birk, D.E.1    Fitch, J.M.2    Babiarz, J.P.3    Doane, K.J.4    Linsenmayer, T.F.5
  • 8
    • 0029067216 scopus 로고
    • Another look at collagen V and XI molecules
    • Fichard, A., Kleman, J.P., and Ruggiero, F. (1995) Another look at collagen V and XI molecules. Matrix Biol. 14, 515-531
    • (1995) Matrix Biol , vol.14 , pp. 515-531
    • Fichard, A.1    Kleman, J.P.2    Ruggiero, F.3
  • 10
    • 84966163623 scopus 로고
    • Targeted mutation in the col5a2 gene reveals a regulatory role for type V collagen during matrix assembly
    • Andrikopoulos, K., Liu, X., Keene, D.R., Jaenisch, R., and Ramirez, F. (1995) Targeted mutation in the col5a2 gene reveals a regulatory role for type V collagen during matrix assembly. Nat. Genet. 9, 31-36
    • (1995) Nat. Genet , vol.9 , pp. 31-36
    • Andrikopoulos, K.1    Liu, X.2    Keene, D.R.3    Jaenisch, R.4    Ramirez, F.5
  • 11
    • 0001297636 scopus 로고
    • Production of a tissue-like structure by contraction of collagen lattices by human fibroblasts of different proliferative potential in vitro
    • Bell, E., Ivarsson, B., and Merrill, C. (1979) Production of a tissue-like structure by contraction of collagen lattices by human fibroblasts of different proliferative potential in vitro. Proc. Natl Acad. Sci. USA 76, 1274-1278
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 1274-1278
    • Bell, E.1    Ivarsson, B.2    Merrill, C.3
  • 12
    • 55449100316 scopus 로고    scopus 로고
    • Hayashi, T., Nishiyama, T., and Adachi, E. (1991) Collagen as a potent regulator for cellular activity in Fundamental Investigations on the Creation of Biofunctional Materials (Okamura, S., Tsuruta, T., Imanishi, Y., and Sunamoto, J., eds.) pp. 55-64, Kagaku-Dojin, Kyoto
    • Hayashi, T., Nishiyama, T., and Adachi, E. (1991) Collagen as a potent regulator for cellular activity in Fundamental Investigations on the Creation of Biofunctional Materials (Okamura, S., Tsuruta, T., Imanishi, Y., and Sunamoto, J., eds.) pp. 55-64, Kagaku-Dojin, Kyoto
  • 13
    • 0028702908 scopus 로고
    • Extracellular matrix regulates cell morphology, proliferation, and tissue formation
    • Senoo, H. and Hata, R. (1994) Extracellular matrix regulates cell morphology, proliferation, and tissue formation. Kaibogaku Zasshi 69, 719-733
    • (1994) Kaibogaku Zasshi , vol.69 , pp. 719-733
    • Senoo, H.1    Hata, R.2
  • 14
    • 0032783534 scopus 로고    scopus 로고
    • Restoration to a quiescent and contractile phenotype from a proliferative phenotype of myofibroblast-like human aortic smooth muscle cells by culture on type IV collagen gels
    • Hirose, M., Kosugi, H., Nakazato, K., and Hayashi, T. (1999) Restoration to a quiescent and contractile phenotype from a proliferative phenotype of myofibroblast-like human aortic smooth muscle cells by culture on type IV collagen gels. J. Biochem. 125, 991-1000
    • (1999) J. Biochem , vol.125 , pp. 991-1000
    • Hirose, M.1    Kosugi, H.2    Nakazato, K.3    Hayashi, T.4
  • 15
    • 0030742897 scopus 로고    scopus 로고
    • Platelet receptors for collagen
    • Moroi, M. and Jung, S.M. (1997) Platelet receptors for collagen. Thromb. Haemost. 78, 439-444
    • (1997) Thromb. Haemost , vol.78 , pp. 439-444
    • Moroi, M.1    Jung, S.M.2
  • 16
    • 0032921366 scopus 로고    scopus 로고
    • Discoidin domain receptors: Structural relations and functional implications
    • Vogel, W. (1999) Discoidin domain receptors: structural relations and functional implications. FASEB J. 13 (supplement), S77-S82
    • (1999) FASEB J , vol.13 , Issue.SUPPL.EMENT
    • Vogel, W.1
  • 17
    • 0034254009 scopus 로고    scopus 로고
    • The collagen receptor integrins have distinct ligand recognition and signaling functions
    • Heino, J. (2000) The collagen receptor integrins have distinct ligand recognition and signaling functions. Matrix Biol. 19, 319-323
    • (2000) Matrix Biol , vol.19 , pp. 319-323
    • Heino, J.1
  • 18
    • 0022638743 scopus 로고    scopus 로고
    • Nakayasu, K., Tanaka, M., Konomi, H., and Hayashi, T. (1986) Distribution of types I, II, III, IV and V collagen in normal and keratoconus corneas. Ophthalmic Res. 18, 1-10
    • Nakayasu, K., Tanaka, M., Konomi, H., and Hayashi, T. (1986) Distribution of types I, II, III, IV and V collagen in normal and keratoconus corneas. Ophthalmic Res. 18, 1-10
  • 19
    • 0023066810 scopus 로고
    • Type V collagen in splenic reticular fibers of the macaque monkey
    • Adachi, E., Hayashi, T., and Hashimoto, P.H. (1987) Type V collagen in splenic reticular fibers of the macaque monkey. Acta Anat. 29, 169-175
    • (1987) Acta Anat , vol.29 , pp. 169-175
    • Adachi, E.1    Hayashi, T.2    Hashimoto, P.H.3
  • 20
    • 0023873382 scopus 로고
    • Collagen type I and type V are present in the same fibril in the avian corneal stroma
    • Birk, D.E., Fitch, J.M., Babiarz, J.P., and Linsenmayer, T.F. (1988) Collagen type I and type V are present in the same fibril in the avian corneal stroma. J. Cell Biol. 106, 999-1008
    • (1988) J. Cell Biol , vol.106 , pp. 999-1008
    • Birk, D.E.1    Fitch, J.M.2    Babiarz, J.P.3    Linsenmayer, T.F.4
  • 21
    • 0020701286 scopus 로고
    • Monoclonal antibodies against chicken type V collagen: Production, specificity, and use for immunocytochemical localization in embryonic cornea and other organs
    • Linsenmayer, T.F., Fitch, J.M., Schmid, T.M., Zak, N.B., Gibney, E., Sanderson, R.D., and Mayne, R. (1983) Monoclonal antibodies against chicken type V collagen: production, specificity, and use for immunocytochemical localization in embryonic cornea and other organs. J. Cell Biol. 96, 124-132
    • (1983) J. Cell Biol , vol.96 , pp. 124-132
    • Linsenmayer, T.F.1    Fitch, J.M.2    Schmid, T.M.3    Zak, N.B.4    Gibney, E.5    Sanderson, R.D.6    Mayne, R.7
  • 22
    • 0021274101 scopus 로고
    • Organization of collagen types I and V in the embryonic chicken cornea: Monoclonal antibody studies
    • Fitch, J.M., Gross, J., Mayne, R., Johnson-Wint, B., and Linsenmayer, T.F. (1984) Organization of collagen types I and V in the embryonic chicken cornea: monoclonal antibody studies. Proc. Natl Acad. Sci. USA 81, 2791-2795
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 2791-2795
    • Fitch, J.M.1    Gross, J.2    Mayne, R.3    Johnson-Wint, B.4    Linsenmayer, T.F.5
  • 23
    • 0035219340 scopus 로고    scopus 로고
    • Type V collagen: Heterotypic type I/V collagen interactions in the regulation of fibril assembly
    • Birk, D.E. (2001) Type V collagen: heterotypic type I/V collagen interactions in the regulation of fibril assembly. Micron 32, 223-237
    • (2001) Micron , vol.32 , pp. 223-237
    • Birk, D.E.1
  • 24
    • 0142249313 scopus 로고    scopus 로고
    • Preferential liberation of type V collagen from bovine corneal stroma by limited treatment with protease
    • Takemura, Y., Mizuno, K., Imamura, Y., and Hayashi, T. (2003) Preferential liberation of type V collagen from bovine corneal stroma by limited treatment with protease. Connect. Tissue 35, 133-139
    • (2003) Connect. Tissue , vol.35 , pp. 133-139
    • Takemura, Y.1    Mizuno, K.2    Imamura, Y.3    Hayashi, T.4
  • 25
    • 0025196230 scopus 로고
    • Adhesion, growth and cytoskeletal characteristics of 8701-BC breast carcinoma cells cultured in the presence of type V collagen
    • Luparello, C., Schillaci, R., Pucci-Minafra, I., and Minafra, S. (1990) Adhesion, growth and cytoskeletal characteristics of 8701-BC breast carcinoma cells cultured in the presence of type V collagen. Eur. J. Cancer 26, 231-240
    • (1990) Eur. J. Cancer , vol.26 , pp. 231-240
    • Luparello, C.1    Schillaci, R.2    Pucci-Minafra, I.3    Minafra, S.4
  • 26
    • 0027215624 scopus 로고
    • Inhibition of cell adhesion by proteolytic fragments of type V collagen
    • Hatai, M., Hashi, H., Kato, I., and Yaoi, Y. (1993) Inhibition of cell adhesion by proteolytic fragments of type V collagen. Cell Struct. Funct. 18, 53-60
    • (1993) Cell Struct. Funct , vol.18 , pp. 53-60
    • Hatai, M.1    Hashi, H.2    Kato, I.3    Yaoi, Y.4
  • 28
    • 0026688923 scopus 로고
    • Disassembly of F-actin filaments in human endothelial cells cultured on type V collagen
    • Yamamoto, K., Yamamoto, M., and Noumura, T. (1992) Disassembly of F-actin filaments in human endothelial cells cultured on type V collagen. Exp. Cell Res. 201, 55-63
    • (1992) Exp. Cell Res , vol.201 , pp. 55-63
    • Yamamoto, K.1    Yamamoto, M.2    Noumura, T.3
  • 29
    • 8744287709 scopus 로고    scopus 로고
    • Reconstituted type V collagen fibrils as cementing materials in the formation of cell clumps in culture
    • Kihara, T., Takemura, Y., Imamura, Y., Mizuno, K., and Hayashi, T. (2004) Reconstituted type V collagen fibrils as cementing materials in the formation of cell clumps in culture. Cell Tissue Res. 318, 343-352
    • (2004) Cell Tissue Res , vol.318 , pp. 343-352
    • Kihara, T.1    Takemura, Y.2    Imamura, Y.3    Mizuno, K.4    Hayashi, T.5
  • 30
    • 0035218501 scopus 로고    scopus 로고
    • The fibril structure of type V collagen triple-helical domain
    • Mizuno, K., Adachi, E., Imamura, Y., Katsumata, O., and Hayashi, T. (2001) The fibril structure of type V collagen triple-helical domain. Micron 32, 317-323
    • (2001) Micron , vol.32 , pp. 317-323
    • Mizuno, K.1    Adachi, E.2    Imamura, Y.3    Katsumata, O.4    Hayashi, T.5
  • 32
    • 0024006111 scopus 로고
    • Quantitative evaluation of the factors affecting the process of fibroblast-mediated collagen gel contraction by separating the process into three phases
    • Nishiyama, T., Tominaga, N., Nakajima, K., and Hayashi, T. (1988) Quantitative evaluation of the factors affecting the process of fibroblast-mediated collagen gel contraction by separating the process into three phases. Coll. Relat. Res. 8, 259-273
    • (1988) Coll. Relat. Res , vol.8 , pp. 259-273
    • Nishiyama, T.1    Tominaga, N.2    Nakajima, K.3    Hayashi, T.4
  • 33
    • 0020010851 scopus 로고
    • Preparation and characterization of the different types of collagen
    • Miller, E.J. and Rhodes, R.K. (1982) Preparation and characterization of the different types of collagen. Methods Enzymol. 82, 33-64
    • (1982) Methods Enzymol , vol.82 , pp. 33-64
    • Miller, E.J.1    Rhodes, R.K.2
  • 34
    • 0029820105 scopus 로고    scopus 로고
    • Separation of the subtypes of type V collagen molecules, [alpha 1(V)]2 alpha 2(V) and alpha 1(V) alpha 2(V) alpha 3(V), by chain composition-dependent affinity for heparin: Single alpha 1(V) chain shows intermediate heparin affinity between those of the type V collagen subtypes composed of [alpha 1(V)]2 alpha 2(V) and of alpha 1(V) alpha 2(V) alpha 3(V)
    • Mizuno, K. and Hayashi, T. (1996) Separation of the subtypes of type V collagen molecules, [alpha 1(V)]2 alpha 2(V) and alpha 1(V) alpha 2(V) alpha 3(V), by chain composition-dependent affinity for heparin: single alpha 1(V) chain shows intermediate heparin affinity between those of the type V collagen subtypes composed of [alpha 1(V)]2 alpha 2(V) and of alpha 1(V) alpha 2(V) alpha 3(V). J. Biochem. 120, 934-939
    • (1996) J. Biochem , vol.120 , pp. 934-939
    • Mizuno, K.1    Hayashi, T.2
  • 35
    • 0019824397 scopus 로고
    • Intracellular degradation of newly synthesized collagen is conformation-dependent
    • Steinmann, B., Rao, V.H., and Gitzelmann, R. (1981) Intracellular degradation of newly synthesized collagen is conformation-dependent. FEBS Lett. 133, 142-144
    • (1981) FEBS Lett , vol.133 , pp. 142-144
    • Steinmann, B.1    Rao, V.H.2    Gitzelmann, R.3
  • 36
    • 55449122635 scopus 로고    scopus 로고
    • Kielty, C.M., Hopkinson, I., and Grant, M.E. (1993) Collagen: the collagen family, structure, assembly and organization in the extracellular matrix in Connective Tissue and its Heritable Disorders (Royce, P.M. and Steinmann, B., eds.) pp. 103-147, Wiley-Liss, New York.
    • Kielty, C.M., Hopkinson, I., and Grant, M.E. (1993) Collagen: the collagen family, structure, assembly and organization in the extracellular matrix in Connective Tissue and its Heritable Disorders (Royce, P.M. and Steinmann, B., eds.) pp. 103-147, Wiley-Liss, New York.
  • 37
    • 0032711777 scopus 로고    scopus 로고
    • Serum-dependent secretion of nondisulfide-bonded and unfolded type IV collagen alpha chains by cultured fetal lung fibroblasts
    • Takahashi, S., Yoshikawa, K., Sasaki, T., Takeda, Y., Imamura, Y., Sado, Y., and Hayashi, T. (1999) Serum-dependent secretion of nondisulfide-bonded and unfolded type IV collagen alpha chains by cultured fetal lung fibroblasts. Connect. Tissue 31, 161-168
    • (1999) Connect. Tissue , vol.31 , pp. 161-168
    • Takahashi, S.1    Yoshikawa, K.2    Sasaki, T.3    Takeda, Y.4    Imamura, Y.5    Sado, Y.6    Hayashi, T.7
  • 38
    • 0034950492 scopus 로고    scopus 로고
    • Secretion of non-helical collagenous polypeptides of alpha1(IV) and alpha2(IV) chains upon depletion of ascorbate by cultured human cells
    • Yoshikawa, K., Takahashi, S., Imamura, Y., Sado, Y., and Hayashi, T. (2001) Secretion of non-helical collagenous polypeptides of alpha1(IV) and alpha2(IV) chains upon depletion of ascorbate by cultured human cells. J. Biochem. 129, 929-936
    • (2001) J. Biochem , vol.129 , pp. 929-936
    • Yoshikawa, K.1    Takahashi, S.2    Imamura, Y.3    Sado, Y.4    Hayashi, T.5
  • 39
    • 0029013320 scopus 로고
    • Condensation of collagen fibrils to the direct vicinity of fibroblasts as a cause of gel contraction
    • Yamato, M., Adachi, E., Yamamoto, K., and Hayashi, T. (1995) Condensation of collagen fibrils to the direct vicinity of fibroblasts as a cause of gel contraction. J. Biochem. 117, 940-946
    • (1995) J. Biochem , vol.117 , pp. 940-946
    • Yamato, M.1    Adachi, E.2    Yamamoto, K.3    Hayashi, T.4
  • 40
    • 13944265302 scopus 로고    scopus 로고
    • Basic mechanism of three-dimensional collagen fibre transport by fibroblasts
    • Meshel, A.S., Wei, Q., Adelstein, R.S., and Sheetz, M.P. (2005) Basic mechanism of three-dimensional collagen fibre transport by fibroblasts. Nat. Cell Biol. 7, 157-164
    • (2005) Nat. Cell Biol , vol.7 , pp. 157-164
    • Meshel, A.S.1    Wei, Q.2    Adelstein, R.S.3    Sheetz, M.P.4
  • 41
    • 0025823515 scopus 로고
    • Extracellular proteins that modulate cell-matrix interactions. SPARC, tenascin, and thrombospondin
    • Sage, E.H. and Bornstein, P. (1991) Extracellular proteins that modulate cell-matrix interactions. SPARC, tenascin, and thrombospondin. J. Biol. Chem. 266, 14831-14834
    • (1991) J. Biol. Chem , vol.266 , pp. 14831-14834
    • Sage, E.H.1    Bornstein, P.2
  • 42
    • 0028132870 scopus 로고
    • Repression of a malignant cell-substratum adhesion phenotype by inhibiting the production of the anti-adhesive proteoglycan, PG-M/ versican
    • Yamagata, M. and Kimata, K. (1994) Repression of a malignant cell-substratum adhesion phenotype by inhibiting the production of the anti-adhesive proteoglycan, PG-M/ versican. J. Cell Sci. 107, 2581-2590
    • (1994) J. Cell Sci , vol.107 , pp. 2581-2590
    • Yamagata, M.1    Kimata, K.2
  • 43
    • 0029909499 scopus 로고    scopus 로고
    • Cyclic GMP-dependent protein kinase is required for thrombospondin and tenascin mediated focal adhesion disassembly
    • Murphy-Ullrich, J.E., Pallero, M.A., Boerth, N., Greenwood, J.A., Lincoln, T.M., and Cornwell, T.L. (1996) Cyclic GMP-dependent protein kinase is required for thrombospondin and tenascin mediated focal adhesion disassembly. J. Cell Sci. 109, 2499-2508
    • (1996) J. Cell Sci , vol.109 , pp. 2499-2508
    • Murphy-Ullrich, J.E.1    Pallero, M.A.2    Boerth, N.3    Greenwood, J.A.4    Lincoln, T.M.5    Cornwell, T.L.6
  • 44
    • 0018852771 scopus 로고
    • Stereoscopic visualization of various morphological types of collagenous fibres
    • Rizk, N.N. (1980) Stereoscopic visualization of various morphological types of collagenous fibres. Acta Anat. 107, 424-429
    • (1980) Acta Anat , vol.107 , pp. 424-429
    • Rizk, N.N.1
  • 45
    • 0019499516 scopus 로고
    • Growth and development of collagen fibrils in immature tissues from rat and sheep
    • Craig, A.S. and Parry, D.A. (1981) Growth and development of collagen fibrils in immature tissues from rat and sheep. Proc. R. Soc. Lond. B. Biol. Sci. 212, 85-92
    • (1981) Proc. R. Soc. Lond. B. Biol. Sci , vol.212 , pp. 85-92
    • Craig, A.S.1    Parry, D.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.