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Volumn 347, Issue 1, 2006, Pages 100-108

Angiopoietin-related growth factor (AGF) supports adhesion, spreading, and migration of keratinocytes, fibroblasts, and endothelial cells through interaction with RGD-binding integrins

Author keywords

Angiopoietin related growth factor; Cell adhesion; Cell migration; Cell proliferation; Cell spreading; Endothelial cell; Fibroblast; Keratinocyte; RGD binding integrins

Indexed keywords

ANGIOPOIETIN RELATED GROWTH FACTOR; ARGINYLGLYCYLASPARTIC ACID; INTEGRIN; UNCLASSIFIED DRUG;

EID: 33745749345     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.06.053     Document Type: Article
Times cited : (21)

References (36)
  • 1
    • 3142738754 scopus 로고    scopus 로고
    • Angiopoietin-related/Angiopoietin-like proteins regulate angiogenesis
    • Oike Y., Yasunaga K., and Suda T. Angiopoietin-related/Angiopoietin-like proteins regulate angiogenesis. Int. J. Hematol. 80 (2004) 21-28
    • (2004) Int. J. Hematol. , vol.80 , pp. 21-28
    • Oike, Y.1    Yasunaga, K.2    Suda, T.3
  • 3
    • 0034666157 scopus 로고    scopus 로고
    • Characterization of the fasting-induced adipose factor FIAF, a novel peroxisome proliferator-activated receptor target gene
    • Kersten S., Mandard S., Tan N.S., Escher P., Metzger D., Chambon P., Gonzalez F.J., Desvergne B., and Wahli W. Characterization of the fasting-induced adipose factor FIAF, a novel peroxisome proliferator-activated receptor target gene. J. Biol. Chem. 275 (2000) 28488-28493
    • (2000) J. Biol. Chem. , vol.275 , pp. 28488-28493
    • Kersten, S.1    Mandard, S.2    Tan, N.S.3    Escher, P.4    Metzger, D.5    Chambon, P.6    Gonzalez, F.J.7    Desvergne, B.8    Wahli, W.9
  • 8
    • 0033137070 scopus 로고    scopus 로고
    • Extracellular matrix and integrin signaling: the shape of things to come
    • Boudreau N.J., and Jones P.L. Extracellular matrix and integrin signaling: the shape of things to come. Biochem. J. 339 (1999) 481-488
    • (1999) Biochem. J. , vol.339 , pp. 481-488
    • Boudreau, N.J.1    Jones, P.L.2
  • 10
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays
    • Mosmann T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J. Immunol. Methods 65 (1983) 55-63
    • (1983) J. Immunol. Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 13
    • 0036197618 scopus 로고    scopus 로고
    • 6 integrins, and CD9 in the interaction of the Fertilin β (ADAM2) disintegrin domain with the mouse egg membrane
    • 6 integrins, and CD9 in the interaction of the Fertilin β (ADAM2) disintegrin domain with the mouse egg membrane. Biol. Reprod. 66 (2002) 1193-1202
    • (2002) Biol. Reprod. , vol.66 , pp. 1193-1202
    • Zhu, X.1    Evans, J.P.2
  • 15
    • 0023609864 scopus 로고
    • Influence of stereochemistry of the sequence Arg-Gly-Asp-Xaa on binding specificity in cell adhesion
    • Pierschbacher M.D., and Ruoslahti E. Influence of stereochemistry of the sequence Arg-Gly-Asp-Xaa on binding specificity in cell adhesion. J. Biol. Chem. 262 (1987) 17294-17298
    • (1987) J. Biol. Chem. , vol.262 , pp. 17294-17298
    • Pierschbacher, M.D.1    Ruoslahti, E.2
  • 16
    • 0026647568 scopus 로고    scopus 로고
    • Mechanism of human keratinocyte migration on fibronectin: unique roles of RGD site and integrins
    • Kim J.P., Zhang K., Chen J.D., Wynn K.C., Kramer R.H., and Woodley D.T. Mechanism of human keratinocyte migration on fibronectin: unique roles of RGD site and integrins. J. Cell. Physiol. 151 (2005) 443-450
    • (2005) J. Cell. Physiol. , vol.151 , pp. 443-450
    • Kim, J.P.1    Zhang, K.2    Chen, J.D.3    Wynn, K.C.4    Kramer, R.H.5    Woodley, D.T.6
  • 17
    • 0019423313 scopus 로고
    • Induction of fibroblast chemotaxis by fibronectin. Localization of the chemotactic region to a 140,000-molecular weight non-gelatin-binding fragment
    • Postlethwaite A.E., Keski-Oja J., Balian G., and Kang A. Induction of fibroblast chemotaxis by fibronectin. Localization of the chemotactic region to a 140,000-molecular weight non-gelatin-binding fragment. J. Exp. Med. 153 (1981) 494-499
    • (1981) J. Exp. Med. , vol.153 , pp. 494-499
    • Postlethwaite, A.E.1    Keski-Oja, J.2    Balian, G.3    Kang, A.4
  • 21
    • 0029979757 scopus 로고    scopus 로고
    • Cell biology of wound healing
    • Shaffer C.J., and Nanney L.B. Cell biology of wound healing. Int. Rev. Cytol. 169 (1996) 151-181
    • (1996) Int. Rev. Cytol. , vol.169 , pp. 151-181
    • Shaffer, C.J.1    Nanney, L.B.2
  • 23
    • 0035860806 scopus 로고    scopus 로고
    • Angiopoietin-1, unlike angiopoietin-2, is incorporated into the extracellular matrix via its linker peptide region
    • Xu Y., and Yu Q. Angiopoietin-1, unlike angiopoietin-2, is incorporated into the extracellular matrix via its linker peptide region. J. Biol. Chem. 276 (2001) 34990-34998
    • (2001) J. Biol. Chem. , vol.276 , pp. 34990-34998
    • Xu, Y.1    Yu, Q.2
  • 24
    • 4644364673 scopus 로고    scopus 로고
    • Angiopoietin-3 is tethered on the cell surface via heparin sulfate proteoglycans
    • Xu Y., Liu Y.-j., and Yu Q. Angiopoietin-3 is tethered on the cell surface via heparin sulfate proteoglycans. J. Biol. Chem. 279 (2004) 41179-41188
    • (2004) J. Biol. Chem. , vol.279 , pp. 41179-41188
    • Xu, Y.1    Liu, Y.-j.2    Yu, Q.3
  • 25
    • 0014418101 scopus 로고
    • Anchorage and growth regulation in normal and virus-transformed cells
    • Stoker M., O'neill C., Berryman S., and Waxman V. Anchorage and growth regulation in normal and virus-transformed cells. Int. J. Cancer 3 (1968) 683-693
    • (1968) Int. J. Cancer , vol.3 , pp. 683-693
    • Stoker, M.1    O'neill, C.2    Berryman, S.3    Waxman, V.4
  • 26
    • 85006175167 scopus 로고
    • The pattern of epidermal cell migration during wound healing
    • Krawczyk W.S. The pattern of epidermal cell migration during wound healing. J. Cell. Biol. 49 (1971) 247-263
    • (1971) J. Cell. Biol. , vol.49 , pp. 247-263
    • Krawczyk, W.S.1
  • 27
    • 0142149188 scopus 로고    scopus 로고
    • Rac2 specificity in macrophage integrin signaling
    • Pradip D., Peng X., and Durden D.L. Rac2 specificity in macrophage integrin signaling. J. Biol. Chem. 278 (2003) 41661-41669
    • (2003) J. Biol. Chem. , vol.278 , pp. 41661-41669
    • Pradip, D.1    Peng, X.2    Durden, D.L.3
  • 30
    • 0029081442 scopus 로고
    • CD31/PECAM-1 is a ligand for alpha v beta 3 integrin involved in adhesion of leukocytes to endothelium
    • Piali L., Hammel P., Uherek C., Bachmann F., Gisler R.H., Dunon D., and Imhof B.A. CD31/PECAM-1 is a ligand for alpha v beta 3 integrin involved in adhesion of leukocytes to endothelium. J. Cell Biol. 130 (1995) 451-460
    • (1995) J. Cell Biol. , vol.130 , pp. 451-460
    • Piali, L.1    Hammel, P.2    Uherek, C.3    Bachmann, F.4    Gisler, R.H.5    Dunon, D.6    Imhof, B.A.7
  • 31
    • 0034050359 scopus 로고    scopus 로고
    • High affinity interaction of Coxsackievirus A9 with integrin alpahvbeta3 (CD51/61) require the CYDMKTTC sequence of beta3, but do not require the RGD sequence of the CAV-9 VP1 protein
    • Triantafilou M., Triantafilou K., Wilson K.M., Takada Y., and Fernandez N. High affinity interaction of Coxsackievirus A9 with integrin alpahvbeta3 (CD51/61) require the CYDMKTTC sequence of beta3, but do not require the RGD sequence of the CAV-9 VP1 protein. Hum. Immunol. 61 (2000) 453-459
    • (2000) Hum. Immunol. , vol.61 , pp. 453-459
    • Triantafilou, M.1    Triantafilou, K.2    Wilson, K.M.3    Takada, Y.4    Fernandez, N.5
  • 34
    • 0028307404 scopus 로고
    • Interactions between and collagen V molecules or single chains involve distinct mechanisms
    • Ruggiero F., Champliaud M.F., Garrone R., and Aumailley M. Interactions between and collagen V molecules or single chains involve distinct mechanisms. Exp. Cell. Res. 210 (1994) 215-223
    • (1994) Exp. Cell. Res. , vol.210 , pp. 215-223
    • Ruggiero, F.1    Champliaud, M.F.2    Garrone, R.3    Aumailley, M.4
  • 36
    • 0033626573 scopus 로고    scopus 로고
    • 3 integrins on smooth muscle cell spreading and migration in fibrin gels
    • 3 integrins on smooth muscle cell spreading and migration in fibrin gels. Thromb. Haemost. 84 (2000) 701-705
    • (2000) Thromb. Haemost. , vol.84 , pp. 701-705
    • Ikari, Y.1    Yee, K.O.2    Schwartz, S.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.