메뉴 건너뛰기




Volumn 7, Issue 4, 1996, Pages 439-447

Integrin α2β1 in tumorigenic human osteosarcoma cell lines regulates cell adhesion, migration, and invasion by interaction with type I collagen

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGEN TYPE 1; INTEGRIN;

EID: 0029852955     PISSN: 10449523     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (59)

References (46)
  • 1
    • 0026903388 scopus 로고
    • Control of cell motility and tumor invasion by extracellular matrix interactions
    • Ruoslahti, E. Control of cell motility and tumor invasion by extracellular matrix interactions. Br. J. Cancer, 66: 239-242, 1992.
    • (1992) Br. J. Cancer , vol.66 , pp. 239-242
    • Ruoslahti, E.1
  • 2
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes, R. O. Integrins: versatility, modulation, and signaling in cell adhesion. Cell, 69: 11-25, 1992.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 3
    • 0028171068 scopus 로고
    • The integrin α9β1 mediates cell attachment to a non-RGD site in the third fibronectin type III repeat of tenascin
    • Yokosaki, Y., Palmer, E. L., Prieto, A. L., Crossin, K. L., Bourdon, M. A., Pylela, R , and Sheppard, D. The integrin α9β1 mediates cell attachment to a non-RGD site in the third fibronectin type III repeat of tenascin. J. Biol. Chem., 269: 26691-26696, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26691-26696
    • Yokosaki, Y.1    Palmer, E.L.2    Prieto, A.L.3    Crossin, K.L.4    Bourdon, M.A.5    Pylela, R.6    Sheppard, D.7
  • 5
    • 0025753821 scopus 로고
    • Human lung tumor-associated antigen identified as an extracellular matrix adhesion molecule
    • Chen, F A., Repasky, E. A., and Bankert, R. B. Human lung tumor-associated antigen identified as an extracellular matrix adhesion molecule. J. Exp. Med., 173: 1111-1115, 1991.
    • (1991) J. Exp. Med. , vol.173 , pp. 1111-1115
    • Chen, F.A.1    Repasky, E.A.2    Bankert, R.B.3
  • 6
    • 0026446816 scopus 로고
    • Expression and function of VLA-α2, -α3, -α5 and α6-integrin receptors in pancreatic carcinoma
    • Weinel, R. J., Rosendahl, A, Neumann, K., Chaloupka, B., Erb, D., Rothmund, M., and Santoso, S. Expression and function of VLA-α2, -α3, -α5 and α6-integrin receptors in pancreatic carcinoma. Int. J. Cancer, 52: 827-833, 1992.
    • (1992) Int. J. Cancer , vol.52 , pp. 827-833
    • Weinel, R.J.1    Rosendahl, A.2    Neumann, K.3    Chaloupka, B.4    Erb, D.5    Rothmund, M.6    Santoso, S.7
  • 7
    • 0025037292 scopus 로고
    • Decreased expression of integrin adhesive protein receptors in adenocarcinoma of the breast
    • Zutter, M. M., Mazoujian, G., and Santoro, S. A. Decreased expression of integrin adhesive protein receptors in adenocarcinoma of the breast. Am. J. Pathol., 137: 863-870, 1990.
    • (1990) Am. J. Pathol. , vol.137 , pp. 863-870
    • Zutter, M.M.1    Mazoujian, G.2    Santoro, S.A.3
  • 8
    • 0025213155 scopus 로고
    • Low expression of collagen receptors in moderate and poorly differentiated colorectal carcinomas
    • Pignatelli, M., Smith, M. E. F., and Bodmer, W. F. Low expression of collagen receptors in moderate and poorly differentiated colorectal carcinomas Br. J. Cancer, 61. 636-638, 1990.
    • (1990) Br. J. Cancer , vol.61 , pp. 636-638
    • Pignatelli, M.1    Smith, M.E.F.2    Bodmer, W.F.3
  • 9
    • 0024542439 scopus 로고
    • Identification of integrin collagen receptors on human melanoma cells
    • Kramer, R. H., and Marks, N. Identification of integrin collagen receptors on human melanoma cells. J. Biol. Chem., 264: 4684-4688, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4684-4688
    • Kramer, R.H.1    Marks, N.2
  • 10
    • 0025880917 scopus 로고
    • Integrin α2β1 is upregulated in fibroblasts and highly aggressive melanoma cells in three-dimensional collagen lattices and mediates the reorganization of collagen I fibrils
    • Klein, C E., Dressel, D., Steinmayer, T., Mauch, C., Eckes, B., Krieg, T., Bankert, R. B., and Weber, L. Integrin α2β1 is upregulated in fibroblasts and highly aggressive melanoma cells in three-dimensional collagen lattices and mediates the reorganization of collagen I fibrils. J. Cell Biol., 115: 1427-1436, 1991.
    • (1991) J. Cell Biol. , vol.115 , pp. 1427-1436
    • Klein, C.E.1    Dressel, D.2    Steinmayer, T.3    Mauch, C.4    Eckes, B.5    Krieg, T.6    Bankert, R.B.7    Weber, L.8
  • 12
    • 0028985257 scopus 로고
    • Transforming growth factor-β regulates collagen gel contraction by increasing α2β1 integrin expression in osteogenic cells
    • Riikonen, T., Koivisto, L, Vihinen, P., and Heino, J. Transforming growth factor-β regulates collagen gel contraction by increasing α2β1 integrin expression in osteogenic cells. J. Biol Chem., 270: 376-382, 1995.
    • (1995) J. Biol Chem. , vol.270 , pp. 376-382
    • Riikonen, T.1    Koivisto, L.2    Vihinen, P.3    Heino, J.4
  • 13
  • 14
    • 0027933588 scopus 로고
    • The role of the I domain in ligand binding of the human integrin α1β1
    • Kern, A., Briesewitz, R., Bank, I., and Marcantonio, E. E. The role of the I domain in ligand binding of the human integrin α1β1. J. Biol. Chem., 269: 22811-22816, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22811-22816
    • Kern, A.1    Briesewitz, R.2    Bank, I.3    Marcantonio, E.E.4
  • 15
    • 0028225987 scopus 로고
    • Identification of putative ligand binding sites within I domain of integrin α2β1 (VLA-2. CD49b/CD29)
    • Kamata, T., Puzon, W., and Takada, Y. Identification of putative ligand binding sites within I domain of integrin α2β1 (VLA-2. CD49b/CD29). J. Biol Chem., 269: 9659-9663, 1994.
    • (1994) J. Biol Chem. , vol.269 , pp. 9659-9663
    • Kamata, T.1    Puzon, W.2    Takada, Y.3
  • 16
    • 0026782146 scopus 로고
    • Analysis of α1β1, α2β1 and α3β1 integrins in cell-collagen interactions: Identification of conformation dependent α1β1 binding sites in collagen type I
    • Gullberg, D., Gehlsen, K. R., Turner, D. C , Åhlén, K., Zijenah, L. S., Barnes, M. J., and Rubin, K. Analysis of α1β1, α2β1 and α3β1 integrins in cell-collagen interactions: identification of conformation dependent α1β1 binding sites in collagen type I. EMBO J., 11: 3865-3873, 1992.
    • (1992) EMBO J. , vol.11 , pp. 3865-3873
    • Gullberg, D.1    Gehlsen, K.R.2    Turner, D.C.3    Åhlén, K.4    Zijenah, L.S.5    Barnes, M.J.6    Rubin, K.7
  • 17
    • 0028979348 scopus 로고
    • Integrin α2β1 is a positive regulator of collagenase (MMP-1) and collagen α1(I) gene expression
    • Riikonen, T., Westermarck, J., Koivisto, L., Broberg, A., Kähäri, V-M., and Heino, J. Integrin α2β1 is a positive regulator of collagenase (MMP-1) and collagen α1(I) gene expression. J. Biol. Chem., 270: 13548-13552, 1995
    • (1995) J. Biol. Chem. , vol.270 , pp. 13548-13552
    • Riikonen, T.1    Westermarck, J.2    Koivisto, L.3    Broberg, A.4    Kähäri, V.-M.5    Heino, J.6
  • 19
    • 0025159429 scopus 로고
    • α2β1 integrins from different cell types show different binding specificities
    • Kirchhofer, D., Languino, L. R., Ruoslahti, E., and Pierschbacher, M. D. α2β1 integrins from different cell types show different binding specificities. J. Biol. Chem., 265: 615-618, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 615-618
    • Kirchhofer, D.1    Languino, L.R.2    Ruoslahti, E.3    Pierschbacher, M.D.4
  • 20
    • 0027497502 scopus 로고
    • Multiple functional forms of the integrin VLA-2 can be derived from a single α2 cDNA clone: Interconversion of forms induced by an anti-β1 antibody
    • Chan, B. M. C., and Hemler, M. E. Multiple functional forms of the integrin VLA-2 can be derived from a single α2 cDNA clone: interconversion of forms induced by an anti-β1 antibody. J. Cell Biol., 120; 537-543, 1993.
    • (1993) J. Cell Biol. , vol.120 , pp. 537-543
    • Chan, B.M.C.1    Hemler, M.E.2
  • 21
    • 0027303968 scopus 로고
    • Endothelial cell attachment and spreading on human tenascin is mediated by α2β1 and αVβ3 integrins
    • Spiramarao, P., Mendler, M., and Bourdon, M. A. Endothelial cell attachment and spreading on human tenascin is mediated by α2β1 and αVβ3 integrins. J. Cell Sci., 105: 1001-1012, 1993.
    • (1993) J. Cell Sci. , vol.105 , pp. 1001-1012
    • Spiramarao, P.1    Mendler, M.2    Bourdon, M.A.3
  • 23
    • 0024534130 scopus 로고
    • Regulation of cell adhesion receptors by transforming growth factor-β
    • Heino, J., Ignotz, R. A., Hemler, M. E., Crouse, C., and Massagué, J Regulation of cell adhesion receptors by transforming growth factor-β. J. Biol. Chem., 264: 380-388, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 380-388
    • Heino, J.1    Ignotz, R.A.2    Hemler, M.E.3    Crouse, C.4    Massagué, J.5
  • 24
    • 0026343904 scopus 로고
    • Regulation of integrin-type cell adhesion receptors by cytokines
    • Santala, P., and Heino, J. Regulation of integrin-type cell adhesion receptors by cytokines. J. Biol. Chem., 266: 23505-23509, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23505-23509
    • Santala, P.1    Heino, J.2
  • 26
    • 0028987656 scopus 로고
    • Antibody against human α1β1 integrin inhibits HELA cell adhesion to laminin and to type I, IV, and V collagens
    • Riikonen, T., Vihinen, P., Potila, M., Rettig, W , and Heino, J. Antibody against human α1β1 integrin inhibits HELA cell adhesion to laminin and to type I, IV, and V collagens. Biochem. Biophys. Res. Commun., 209. 205-212, 1995.
    • (1995) Biochem. Biophys. Res. Commun. , vol.209 , pp. 205-212
    • Riikonen, T.1    Vihinen, P.2    Potila, M.3    Rettig, W.4    Heino, J.5
  • 27
    • 0028057470 scopus 로고
    • Suppressed collagen gene expression and induction of α2β1 integrin-type collagen receptor in tumorigenic derivatives of human osteogenic sarcoma (HOS) cell line
    • Santala, P., Larjava, H , Nissinen, L., Rukonen, T., Määttä, A., and Heino, J. Suppressed collagen gene expression and induction of α2β1 integrin-type collagen receptor in tumorigenic derivatives of human osteogenic sarcoma (HOS) cell line. J. Biol. Chem., 269: 1276-1283, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1276-1283
    • Santala, P.1    Larjava, H.2    Nissinen, L.3    Rukonen, T.4    Määttä, A.5    Heino, J.6
  • 28
    • 0024382716 scopus 로고
    • The primary structure of the VLA-2/ collagen receptor α2 subunit (platelet GP la): Homology to other integrins and the presence of a possible collagen-binding domain
    • Takada, Y., and Hemler, M. E. The primary structure of the VLA-2/ collagen receptor α2 subunit (platelet GP la): homology to other integrins and the presence of a possible collagen-binding domain. J. Cell Biol , 109: 397-407, 1989.
    • (1989) J. Cell Biol , vol.109 , pp. 397-407
    • Takada, Y.1    Hemler, M.E.2
  • 30
    • 0024534377 scopus 로고
    • Changes in integrin receptors on oncogenically transformed cells
    • Plantefaber, L C., and Hynes, R. O. Changes in integrin receptors on oncogenically transformed cells. Cell, 56: 281-290, 1989.
    • (1989) Cell , vol.56 , pp. 281-290
    • Plantefaber, L.C.1    Hynes, R.O.2
  • 31
    • 0025138216 scopus 로고
    • Alterations in integrin expression on chemically transformed human cells: Specific enhancement of laminin and collagen receptor complexes
    • Dedhar, S , and Saulnier, R. J. Alterations in integrin expression on chemically transformed human cells: specific enhancement of laminin and collagen receptor complexes. J. Cell Biol., 110: 481-489, 1990.
    • (1990) J. Cell Biol. , vol.110 , pp. 481-489
    • Dedhar, S.1    Saulnier, R.J.2
  • 33
    • 0026786361 scopus 로고
    • Integrin subunit expression by human osteoblasts and osteoclasts in situ and in culture
    • Clover, J., Dodds, R. A., and Gowen, M Integrin subunit expression by human osteoblasts and osteoclasts in situ and in culture. J. Cell Sci., 103. 267-271, 1992.
    • (1992) J. Cell Sci. , vol.103 , pp. 267-271
    • Clover, J.1    Dodds, R.A.2    Gowen, M.3
  • 34
    • 0027483226 scopus 로고
    • A novel divalent cation-binding site in the A domain of the β2 integrin CR3 (CD11b/CD18) is essential for ligand binding
    • Michishita, M., Videm, V., and Arnaout, M. A. A novel divalent cation-binding site in the A domain of the β2 integrin CR3 (CD11b/CD18) is essential for ligand binding. Cell, 72: 857-867, 1993.
    • (1993) Cell , vol.72 , pp. 857-867
    • Michishita, M.1    Videm, V.2    Arnaout, M.A.3
  • 35
    • 0028986196 scopus 로고
    • Crystal structure of the A domain from the a subunit of integrin CR3 (CD11b/CD18)
    • Lee, J-O., Rieu, P., Arnaout, M. A., and Liddington, R. Crystal structure of the A domain from the a subunit of integrin CR3 (CD11b/CD18). Cell, 80: 631-638, 1995.
    • (1995) Cell , vol.80 , pp. 631-638
    • Lee, J.-O.1    Rieu, P.2    Arnaout, M.A.3    Liddington, R.4
  • 36
    • 0025214421 scopus 로고
    • Elevated levels of the α5β1 fibronectin receptor suppress the transformed phenotype of Chinese hamster ovary cells
    • Giancotti, F. G , and Ruoslahti, E. Elevated levels of the α5β1 fibronectin receptor suppress the transformed phenotype of Chinese hamster ovary cells. Cell, 60: 849-859, 1990.
    • (1990) Cell , vol.60 , pp. 849-859
    • Giancotti, F.G.1    Ruoslahti, E.2
  • 37
    • 0028175008 scopus 로고
    • Expression of the integrin α4β1 on melanoma cells can inhibit the invasive stage of metastasis formation
    • Qian, F., Vaux, D. L., and Weissman, I. L. Expression of the integrin α4β1 on melanoma cells can inhibit the invasive stage of metastasis formation. Cell, 77: 335-347, 1994.
    • (1994) Cell , vol.77 , pp. 335-347
    • Qian, F.1    Vaux, D.L.2    Weissman, I.L.3
  • 38
    • 0028221785 scopus 로고
    • The distribution of cellular adhesion molecules in pigmented skin lesions
    • Phila.
    • van Duinen, C. M., van den Broek, L. J. C. M., Vermeer, B J., Fleuren, G. J , and Bruijn, J. A. The distribution of cellular adhesion molecules in pigmented skin lesions. Cancer (Phila.), 73: 2131-2139, 1994.
    • (1994) Cancer , vol.73 , pp. 2131-2139
    • Van Duinen, C.M.1    Van Den Broek, L.J.C.M.2    Vermeer, B.J.3    Fleuren, G.J.4    Bruijn, J.A.5
  • 40
    • 0025806141 scopus 로고
    • In vitro and in vivo consequences of VLA-2 expression on rhabdomyosarcoma cells
    • Washington DC
    • Chan, B. M. C., Matsuura, N., Takada, Y., Zetter, B. R., and Hemler, M. E. In vitro and in vivo consequences of VLA-2 expression on rhabdomyosarcoma cells. Science (Washington DC). 251: 1600-1602, 1991.
    • (1991) Science , vol.251 , pp. 1600-1602
    • Chan, B.M.C.1    Matsuura, N.2    Takada, Y.3    Zetter, B.R.4    Hemler, M.E.5
  • 44
    • 0028670298 scopus 로고
    • Integrin αvβ3 rescues melanoma cells from apoptosis in three-dimensional dermal collagen
    • Montgomery, A M P., Reisfeld, R. A., and Cheresh, D. A Integrin αvβ3 rescues melanoma cells from apoptosis in three-dimensional dermal collagen. Proc. Natl. Acad. Sci. USA, 97: 8856-8860, 1994.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8856-8860
    • Montgomery, A.M.P.1    Reisfeld, R.A.2    Cheresh, D.A.3
  • 45
    • 0024335963 scopus 로고
    • Signal transduction through the fibronectin receptor induces collagenase and stromelysin gene expression
    • Werb, Z., Tremble, P. M., Behrendtsen, O., Crowley, E., and Damsky, C. H Signal transduction through the fibronectin receptor induces collagenase and stromelysin gene expression. J. Cell Biol, 109: 877-889, 1989.
    • (1989) J. Cell Biol , vol.109 , pp. 877-889
    • Werb, Z.1    Tremble, P.M.2    Behrendtsen, O.3    Crowley, E.4    Damsky, C.H.5
  • 46
    • 0023280134 scopus 로고
    • Use of the monoclonal antibody 12F1 to characterize the differentiation antigen VLA-2
    • Pischel, K D., Hemler, M. E., Huang, C., Bluestein, H. G., and Woods, V. L Use of the monoclonal antibody 12F1 to characterize the differentiation antigen VLA-2. J. Immunol, 138: 226-233, 1987.
    • (1987) J. Immunol , vol.138 , pp. 226-233
    • Pischel, K.D.1    Hemler, M.E.2    Huang, C.3    Bluestein, H.G.4    Woods, V.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.