Altered interaction of human granulation-tissue fibroblasts with fibronectin is regulated by α5β1 integrin
Granulation-tissue fibroblasts express an unique phenotype distinct from normal fibroblasts. Due to the importance of the cell-matrix interactions in the regulation of cell morphology and behavior, we have compared the cell adhesion apparatus, especially integrin-type receptors, in fibroblasts cultu...
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1994 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
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| Übergeordnetes Werk: |
in: Biochimica et Biophysica Acta (BBA)/Molecular Cell Research - Amsterdam : Elsevier, 1224(1994), 1, Seite 33-42 |
| Übergeordnetes Werk: |
volume:1224 ; year:1994 ; number:1 ; pages:33-42 |
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| 520 | |a Granulation-tissue fibroblasts express an unique phenotype distinct from normal fibroblasts. Due to the importance of the cell-matrix interactions in the regulation of cell morphology and behavior, we have compared the cell adhesion apparatus, especially integrin-type receptors, in fibroblasts cultured from healthy human periodontal connective tissues and from chronic and wound granulation tissues. The spreading of granulation-tissue cells on fibronectin, but not on type I collagen or laminin, was slower when compared with the normal fibroblasts. Cell spreading on fibronectin could be inhibited by RGD-containing peptide, suggesting integrin-mediated interaction. Both cell types expressed β1 integrin subunit, which associated with several integrin α subunits, namely α1, α2, α3, α5 and αv. In addition to β1 subunit, αv chain formed heterodimers with β3 and β5 subunits. Thus, these cells have multiple putative fibronectin, laminin, collagen, and vitronectin receptors. Cell spreading of both cell types on fibronectin was inhibited with anti-β1 and anti-α5 antibodies, but antibodies against other putative FN-binding integrins (α3, αv, and αvβ3) had no effects. Furthermore, granulation-tissue fibroblasts showed delayed spreading on substrates coated with anti-β1 or anti-α5 integrin antibodies. On substrates coated with anti-α3 antibody, both cell types spread equally well. By FACS analysis, the amount of β1 and α5 integrin subunits expressed on the cell surfaces was slightly elevated in GTFs compared with HGFs. Thus, the findings in this study indicate that the weakened interaction of granulation-tissue fibroblasts with fibronectin is regulated by altered function of α5β1 integrin. | ||
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(DE-627)NLEJ186877579 (DE-599)GBVNLZ186877579 DE-627 ger DE-627 rakwb eng Altered interaction of human granulation-tissue fibroblasts with fibronectin is regulated by α5β1 integrin 1994 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Granulation-tissue fibroblasts express an unique phenotype distinct from normal fibroblasts. Due to the importance of the cell-matrix interactions in the regulation of cell morphology and behavior, we have compared the cell adhesion apparatus, especially integrin-type receptors, in fibroblasts cultured from healthy human periodontal connective tissues and from chronic and wound granulation tissues. The spreading of granulation-tissue cells on fibronectin, but not on type I collagen or laminin, was slower when compared with the normal fibroblasts. Cell spreading on fibronectin could be inhibited by RGD-containing peptide, suggesting integrin-mediated interaction. Both cell types expressed β1 integrin subunit, which associated with several integrin α subunits, namely α1, α2, α3, α5 and αv. In addition to β1 subunit, αv chain formed heterodimers with β3 and β5 subunits. Thus, these cells have multiple putative fibronectin, laminin, collagen, and vitronectin receptors. Cell spreading of both cell types on fibronectin was inhibited with anti-β1 and anti-α5 antibodies, but antibodies against other putative FN-binding integrins (α3, αv, and αvβ3) had no effects. Furthermore, granulation-tissue fibroblasts showed delayed spreading on substrates coated with anti-β1 or anti-α5 integrin antibodies. On substrates coated with anti-α3 antibody, both cell types spread equally well. By FACS analysis, the amount of β1 and α5 integrin subunits expressed on the cell surfaces was slightly elevated in GTFs compared with HGFs. Thus, the findings in this study indicate that the weakened interaction of granulation-tissue fibroblasts with fibronectin is regulated by altered function of α5β1 integrin. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Hakkinen, L. oth Heino, J. oth Koivisto, L. oth Larjava, H. oth in Biochimica et Biophysica Acta (BBA)/Molecular Cell Research Amsterdam : Elsevier 1224(1994), 1, Seite 33-42 (DE-627)NLEJ186863756 (DE-600)2209512-3 0167-4889 nnns volume:1224 year:1994 number:1 pages:33-42 http://linkinghub.elsevier.com/retrieve/pii/0167-4889(94)90110-4 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 1224 1994 1 33-42 |
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(DE-627)NLEJ186877579 (DE-599)GBVNLZ186877579 DE-627 ger DE-627 rakwb eng Altered interaction of human granulation-tissue fibroblasts with fibronectin is regulated by α5β1 integrin 1994 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Granulation-tissue fibroblasts express an unique phenotype distinct from normal fibroblasts. Due to the importance of the cell-matrix interactions in the regulation of cell morphology and behavior, we have compared the cell adhesion apparatus, especially integrin-type receptors, in fibroblasts cultured from healthy human periodontal connective tissues and from chronic and wound granulation tissues. The spreading of granulation-tissue cells on fibronectin, but not on type I collagen or laminin, was slower when compared with the normal fibroblasts. Cell spreading on fibronectin could be inhibited by RGD-containing peptide, suggesting integrin-mediated interaction. Both cell types expressed β1 integrin subunit, which associated with several integrin α subunits, namely α1, α2, α3, α5 and αv. In addition to β1 subunit, αv chain formed heterodimers with β3 and β5 subunits. Thus, these cells have multiple putative fibronectin, laminin, collagen, and vitronectin receptors. Cell spreading of both cell types on fibronectin was inhibited with anti-β1 and anti-α5 antibodies, but antibodies against other putative FN-binding integrins (α3, αv, and αvβ3) had no effects. Furthermore, granulation-tissue fibroblasts showed delayed spreading on substrates coated with anti-β1 or anti-α5 integrin antibodies. On substrates coated with anti-α3 antibody, both cell types spread equally well. By FACS analysis, the amount of β1 and α5 integrin subunits expressed on the cell surfaces was slightly elevated in GTFs compared with HGFs. Thus, the findings in this study indicate that the weakened interaction of granulation-tissue fibroblasts with fibronectin is regulated by altered function of α5β1 integrin. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Hakkinen, L. oth Heino, J. oth Koivisto, L. oth Larjava, H. oth in Biochimica et Biophysica Acta (BBA)/Molecular Cell Research Amsterdam : Elsevier 1224(1994), 1, Seite 33-42 (DE-627)NLEJ186863756 (DE-600)2209512-3 0167-4889 nnns volume:1224 year:1994 number:1 pages:33-42 http://linkinghub.elsevier.com/retrieve/pii/0167-4889(94)90110-4 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 1224 1994 1 33-42 |
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(DE-627)NLEJ186877579 (DE-599)GBVNLZ186877579 DE-627 ger DE-627 rakwb eng Altered interaction of human granulation-tissue fibroblasts with fibronectin is regulated by α5β1 integrin 1994 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Granulation-tissue fibroblasts express an unique phenotype distinct from normal fibroblasts. Due to the importance of the cell-matrix interactions in the regulation of cell morphology and behavior, we have compared the cell adhesion apparatus, especially integrin-type receptors, in fibroblasts cultured from healthy human periodontal connective tissues and from chronic and wound granulation tissues. The spreading of granulation-tissue cells on fibronectin, but not on type I collagen or laminin, was slower when compared with the normal fibroblasts. Cell spreading on fibronectin could be inhibited by RGD-containing peptide, suggesting integrin-mediated interaction. Both cell types expressed β1 integrin subunit, which associated with several integrin α subunits, namely α1, α2, α3, α5 and αv. In addition to β1 subunit, αv chain formed heterodimers with β3 and β5 subunits. Thus, these cells have multiple putative fibronectin, laminin, collagen, and vitronectin receptors. Cell spreading of both cell types on fibronectin was inhibited with anti-β1 and anti-α5 antibodies, but antibodies against other putative FN-binding integrins (α3, αv, and αvβ3) had no effects. Furthermore, granulation-tissue fibroblasts showed delayed spreading on substrates coated with anti-β1 or anti-α5 integrin antibodies. On substrates coated with anti-α3 antibody, both cell types spread equally well. By FACS analysis, the amount of β1 and α5 integrin subunits expressed on the cell surfaces was slightly elevated in GTFs compared with HGFs. Thus, the findings in this study indicate that the weakened interaction of granulation-tissue fibroblasts with fibronectin is regulated by altered function of α5β1 integrin. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Hakkinen, L. oth Heino, J. oth Koivisto, L. oth Larjava, H. oth in Biochimica et Biophysica Acta (BBA)/Molecular Cell Research Amsterdam : Elsevier 1224(1994), 1, Seite 33-42 (DE-627)NLEJ186863756 (DE-600)2209512-3 0167-4889 nnns volume:1224 year:1994 number:1 pages:33-42 http://linkinghub.elsevier.com/retrieve/pii/0167-4889(94)90110-4 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 1224 1994 1 33-42 |
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(DE-627)NLEJ186877579 (DE-599)GBVNLZ186877579 DE-627 ger DE-627 rakwb eng Altered interaction of human granulation-tissue fibroblasts with fibronectin is regulated by α5β1 integrin 1994 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Granulation-tissue fibroblasts express an unique phenotype distinct from normal fibroblasts. Due to the importance of the cell-matrix interactions in the regulation of cell morphology and behavior, we have compared the cell adhesion apparatus, especially integrin-type receptors, in fibroblasts cultured from healthy human periodontal connective tissues and from chronic and wound granulation tissues. The spreading of granulation-tissue cells on fibronectin, but not on type I collagen or laminin, was slower when compared with the normal fibroblasts. Cell spreading on fibronectin could be inhibited by RGD-containing peptide, suggesting integrin-mediated interaction. Both cell types expressed β1 integrin subunit, which associated with several integrin α subunits, namely α1, α2, α3, α5 and αv. In addition to β1 subunit, αv chain formed heterodimers with β3 and β5 subunits. Thus, these cells have multiple putative fibronectin, laminin, collagen, and vitronectin receptors. Cell spreading of both cell types on fibronectin was inhibited with anti-β1 and anti-α5 antibodies, but antibodies against other putative FN-binding integrins (α3, αv, and αvβ3) had no effects. Furthermore, granulation-tissue fibroblasts showed delayed spreading on substrates coated with anti-β1 or anti-α5 integrin antibodies. On substrates coated with anti-α3 antibody, both cell types spread equally well. By FACS analysis, the amount of β1 and α5 integrin subunits expressed on the cell surfaces was slightly elevated in GTFs compared with HGFs. Thus, the findings in this study indicate that the weakened interaction of granulation-tissue fibroblasts with fibronectin is regulated by altered function of α5β1 integrin. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Hakkinen, L. oth Heino, J. oth Koivisto, L. oth Larjava, H. oth in Biochimica et Biophysica Acta (BBA)/Molecular Cell Research Amsterdam : Elsevier 1224(1994), 1, Seite 33-42 (DE-627)NLEJ186863756 (DE-600)2209512-3 0167-4889 nnns volume:1224 year:1994 number:1 pages:33-42 http://linkinghub.elsevier.com/retrieve/pii/0167-4889(94)90110-4 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 1224 1994 1 33-42 |
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(DE-627)NLEJ186877579 (DE-599)GBVNLZ186877579 DE-627 ger DE-627 rakwb eng Altered interaction of human granulation-tissue fibroblasts with fibronectin is regulated by α5β1 integrin 1994 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Granulation-tissue fibroblasts express an unique phenotype distinct from normal fibroblasts. Due to the importance of the cell-matrix interactions in the regulation of cell morphology and behavior, we have compared the cell adhesion apparatus, especially integrin-type receptors, in fibroblasts cultured from healthy human periodontal connective tissues and from chronic and wound granulation tissues. The spreading of granulation-tissue cells on fibronectin, but not on type I collagen or laminin, was slower when compared with the normal fibroblasts. Cell spreading on fibronectin could be inhibited by RGD-containing peptide, suggesting integrin-mediated interaction. Both cell types expressed β1 integrin subunit, which associated with several integrin α subunits, namely α1, α2, α3, α5 and αv. In addition to β1 subunit, αv chain formed heterodimers with β3 and β5 subunits. Thus, these cells have multiple putative fibronectin, laminin, collagen, and vitronectin receptors. Cell spreading of both cell types on fibronectin was inhibited with anti-β1 and anti-α5 antibodies, but antibodies against other putative FN-binding integrins (α3, αv, and αvβ3) had no effects. Furthermore, granulation-tissue fibroblasts showed delayed spreading on substrates coated with anti-β1 or anti-α5 integrin antibodies. On substrates coated with anti-α3 antibody, both cell types spread equally well. By FACS analysis, the amount of β1 and α5 integrin subunits expressed on the cell surfaces was slightly elevated in GTFs compared with HGFs. Thus, the findings in this study indicate that the weakened interaction of granulation-tissue fibroblasts with fibronectin is regulated by altered function of α5β1 integrin. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Hakkinen, L. oth Heino, J. oth Koivisto, L. oth Larjava, H. oth in Biochimica et Biophysica Acta (BBA)/Molecular Cell Research Amsterdam : Elsevier 1224(1994), 1, Seite 33-42 (DE-627)NLEJ186863756 (DE-600)2209512-3 0167-4889 nnns volume:1224 year:1994 number:1 pages:33-42 http://linkinghub.elsevier.com/retrieve/pii/0167-4889(94)90110-4 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 1224 1994 1 33-42 |
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altered interaction of human granulation-tissue fibroblasts with fibronectin is regulated by α5β1 integrin |
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Altered interaction of human granulation-tissue fibroblasts with fibronectin is regulated by α5β1 integrin |
| abstract |
Granulation-tissue fibroblasts express an unique phenotype distinct from normal fibroblasts. Due to the importance of the cell-matrix interactions in the regulation of cell morphology and behavior, we have compared the cell adhesion apparatus, especially integrin-type receptors, in fibroblasts cultured from healthy human periodontal connective tissues and from chronic and wound granulation tissues. The spreading of granulation-tissue cells on fibronectin, but not on type I collagen or laminin, was slower when compared with the normal fibroblasts. Cell spreading on fibronectin could be inhibited by RGD-containing peptide, suggesting integrin-mediated interaction. Both cell types expressed β1 integrin subunit, which associated with several integrin α subunits, namely α1, α2, α3, α5 and αv. In addition to β1 subunit, αv chain formed heterodimers with β3 and β5 subunits. Thus, these cells have multiple putative fibronectin, laminin, collagen, and vitronectin receptors. Cell spreading of both cell types on fibronectin was inhibited with anti-β1 and anti-α5 antibodies, but antibodies against other putative FN-binding integrins (α3, αv, and αvβ3) had no effects. Furthermore, granulation-tissue fibroblasts showed delayed spreading on substrates coated with anti-β1 or anti-α5 integrin antibodies. On substrates coated with anti-α3 antibody, both cell types spread equally well. By FACS analysis, the amount of β1 and α5 integrin subunits expressed on the cell surfaces was slightly elevated in GTFs compared with HGFs. Thus, the findings in this study indicate that the weakened interaction of granulation-tissue fibroblasts with fibronectin is regulated by altered function of α5β1 integrin. |
| abstractGer |
Granulation-tissue fibroblasts express an unique phenotype distinct from normal fibroblasts. Due to the importance of the cell-matrix interactions in the regulation of cell morphology and behavior, we have compared the cell adhesion apparatus, especially integrin-type receptors, in fibroblasts cultured from healthy human periodontal connective tissues and from chronic and wound granulation tissues. The spreading of granulation-tissue cells on fibronectin, but not on type I collagen or laminin, was slower when compared with the normal fibroblasts. Cell spreading on fibronectin could be inhibited by RGD-containing peptide, suggesting integrin-mediated interaction. Both cell types expressed β1 integrin subunit, which associated with several integrin α subunits, namely α1, α2, α3, α5 and αv. In addition to β1 subunit, αv chain formed heterodimers with β3 and β5 subunits. Thus, these cells have multiple putative fibronectin, laminin, collagen, and vitronectin receptors. Cell spreading of both cell types on fibronectin was inhibited with anti-β1 and anti-α5 antibodies, but antibodies against other putative FN-binding integrins (α3, αv, and αvβ3) had no effects. Furthermore, granulation-tissue fibroblasts showed delayed spreading on substrates coated with anti-β1 or anti-α5 integrin antibodies. On substrates coated with anti-α3 antibody, both cell types spread equally well. By FACS analysis, the amount of β1 and α5 integrin subunits expressed on the cell surfaces was slightly elevated in GTFs compared with HGFs. Thus, the findings in this study indicate that the weakened interaction of granulation-tissue fibroblasts with fibronectin is regulated by altered function of α5β1 integrin. |
| abstract_unstemmed |
Granulation-tissue fibroblasts express an unique phenotype distinct from normal fibroblasts. Due to the importance of the cell-matrix interactions in the regulation of cell morphology and behavior, we have compared the cell adhesion apparatus, especially integrin-type receptors, in fibroblasts cultured from healthy human periodontal connective tissues and from chronic and wound granulation tissues. The spreading of granulation-tissue cells on fibronectin, but not on type I collagen or laminin, was slower when compared with the normal fibroblasts. Cell spreading on fibronectin could be inhibited by RGD-containing peptide, suggesting integrin-mediated interaction. Both cell types expressed β1 integrin subunit, which associated with several integrin α subunits, namely α1, α2, α3, α5 and αv. In addition to β1 subunit, αv chain formed heterodimers with β3 and β5 subunits. Thus, these cells have multiple putative fibronectin, laminin, collagen, and vitronectin receptors. Cell spreading of both cell types on fibronectin was inhibited with anti-β1 and anti-α5 antibodies, but antibodies against other putative FN-binding integrins (α3, αv, and αvβ3) had no effects. Furthermore, granulation-tissue fibroblasts showed delayed spreading on substrates coated with anti-β1 or anti-α5 integrin antibodies. On substrates coated with anti-α3 antibody, both cell types spread equally well. By FACS analysis, the amount of β1 and α5 integrin subunits expressed on the cell surfaces was slightly elevated in GTFs compared with HGFs. Thus, the findings in this study indicate that the weakened interaction of granulation-tissue fibroblasts with fibronectin is regulated by altered function of α5β1 integrin. |
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