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Volumn 100, Issue 6, 1997, Pages 1647-1653

RGDN peptide interaction with endothelial α5β1 integrin causes sustained endothelin-dependent vasoconstriction of rat skeletal muscle arterioles

Author keywords

Arginine glycine aspartic acid (RGD); Microcirculation; Vascular smooth muscle; Vasoconstriction; (v) 3 integrin

Indexed keywords

ARGINYLGLYCYLASPARTIC ACID; CYCLO(DEXTRO TRYPTOPHYL DEXTRO ASPARTYLPROLYL DEXTRO VALYLLEUCYL); ENDOTHELIN; ENDOTHELIN A RECEPTOR; INTEGRIN;

EID: 0030808413     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI119689     Document Type: Article
Times cited : (57)

References (45)
  • 1
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation and signaling in cell adhesion
    • Hynes, R.O. 1992. Integrins: versatility, modulation and signaling in cell adhesion. Cell. 69:11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 2
    • 0027832390 scopus 로고
    • Integrins: A review of their structure and mechanisms of ligand binding
    • Tuckwell, D.S., S.A. Weston, and M.J. Humphries. 1993. Integrins: a review of their structure and mechanisms of ligand binding. Symp. Soc. Exp. Biol. 47:107-136.
    • (1993) Symp. Soc. Exp. Biol. , vol.47 , pp. 107-136
    • Tuckwell, D.S.1    Weston, S.A.2    Humphries, M.J.3
  • 5
    • 0030272735 scopus 로고    scopus 로고
    • Integrin cytoplasmic interactions and bidirectional transmembrane signalling
    • Dedhar, S., and G.E. Hannigan. 1996. Integrin cytoplasmic interactions and bidirectional transmembrane signalling. Curr. Opin. Cell Biol. 8:657-669.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 657-669
    • Dedhar, S.1    Hannigan, G.E.2
  • 6
    • 0028954797 scopus 로고
    • Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function
    • Miyamoto, S., S.K. Akiyama, and K.M. Yamada. 1995. Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function Science (Wash. DC). 267:885-885.
    • (1995) Science (Wash. DC) , vol.267 , pp. 885-885
    • Miyamoto, S.1    Akiyama, S.K.2    Yamada, K.M.3
  • 7
    • 0026535449 scopus 로고
    • Regulation of fibronectin receptor distribution
    • LaFlamme, S.E., S.K. Akiyama, and K.M. Yamada. 1992. Regulation of fibronectin receptor distribution. J. Cell Biol. 117:437-447.
    • (1992) J. Cell Biol. , vol.117 , pp. 437-447
    • LaFlamme, S.E.1    Akiyama, S.K.2    Yamada, K.M.3
  • 8
    • 0020491054 scopus 로고
    • The cell attachment domain of fibronectin. Determination of the primary structure
    • Pierschbacher, M.D., E. Ruoslahti, J. Sundelin, P. Lind, and P.A. Peterson. 1982. The cell attachment domain of fibronectin. Determination of the primary structure. J. Biol. Chem. 257:9593-9597.
    • (1982) J. Biol. Chem. , vol.257 , pp. 9593-9597
    • Pierschbacher, M.D.1    Ruoslahti, E.2    Sundelin, J.3    Lind, P.4    Peterson, P.A.5
  • 9
    • 0020631112 scopus 로고
    • Structure of a cDNa for the proa2 chain of human type I procollagen. Comparison with chick cDNa for proα2(I) identifies structurally conserved features of the protein and the gene
    • Bernard, M.P., J.C. Myers, M.L. Chu, F. Ramirez, E.F. Eikenberry and D.J. Prockop. 1983. Structure of a cDNA for the proa2 chain of human type I procollagen. Comparison with chick cDNA for proα2(I) identifies structurally conserved features of the protein and the gene. Biochemistry. 22:1139-1145.
    • (1983) Biochemistry , vol.22 , pp. 1139-1145
    • Bernard, M.P.1    Myers, J.C.2    Chu, M.L.3    Ramirez, F.4    Eikenberry, E.F.5    Prockop, D.J.6
  • 10
    • 0001588341 scopus 로고
    • Cloning and sequence analysis of rat bone sialoprotein (osteopontin) cDNA reveals an Arg-Gly-Asp cell-binding sequence
    • Oldberg, A., A. Franzen, and D. Heinegard. 1986. Cloning and sequence analysis of rat bone sialoprotein (osteopontin) cDNA reveals an Arg-Gly-Asp cell-binding sequence. Proc. Natl. Acad Sci. USA. 83:8819-8823
    • (1986) Proc. Natl. Acad Sci. USA , vol.83 , pp. 8819-8823
    • Oldberg, A.1    Franzen, A.2    Heinegard, D.3
  • 11
    • 0022133419 scopus 로고
    • Complete amino acid sequence of human vitronectin deduced from cDNA. Similarity of cell attachment sites in vitronectin and fibronectin
    • Suzuki, S., A. Oldberg, E.G. Hayman, M.D. Pierschbacher, and E. Ruoslahti. 1985. Complete amino acid sequence of human vitronectin deduced from cDNA. Similarity of cell attachment sites in vitronectin and fibronectin. EMBO J. 4:2519-2524.
    • (1985) EMBO J. , vol.4 , pp. 2519-2524
    • Suzuki, S.1    Oldberg, A.2    Hayman, E.G.3    Pierschbacher, M.D.4    Ruoslahti, E.5
  • 13
    • 0021271957 scopus 로고
    • Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule
    • Picrsehbacher, M.D., and E. Ruoslahti. 1984. Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule. Nature (Lond.). 309:30-33.
    • (1984) Nature (Lond.) , vol.309 , pp. 30-33
    • Picrsehbacher, M.D.1    Ruoslahti, E.2
  • 14
    • 0023920076 scopus 로고
    • Fibronectin and its receptors
    • Ruoslahti, E. 1988. Fibronectin and its receptors. Ann. Rev. Biochem. 57:375-413.
    • (1988) Ann. Rev. Biochem. , vol.57 , pp. 375-413
    • Ruoslahti, E.1
  • 17
    • 0022502048 scopus 로고
    • Platelet membrane glycoprotcin IIb/IIIa: Member of a family of Arg-Gly-Asp-specific adhesion receptors
    • Pytela, R., M.D. Pierschbacher, M.H. Ginsberg, E.F. Plow, and E. Ruoslahti. 1986. Platelet membrane glycoprotcin IIb/IIIa: member of a family of Arg-Gly-Asp-specific adhesion receptors. Science (Wash. DC). 231:1559-1562.
    • (1986) Science (Wash. DC) , vol.231 , pp. 1559-1562
    • Pytela, R.1    Pierschbacher, M.D.2    Ginsberg, M.H.3    Plow, E.F.4    Ruoslahti, E.5
  • 18
    • 0023609864 scopus 로고
    • Influence of stereochemistry of the sequence Arg-Gly-Asp-Xaa on binding specificity in cell adhesion
    • Pierschbacher, M.D., and E. Ruoslahti. 1987. Influence of stereochemistry of the sequence Arg-Gly-Asp-Xaa on binding specificity in cell adhesion. J. Biol. Chem. 262:17294-17298.
    • (1987) J. Biol. Chem. , vol.262 , pp. 17294-17298
    • Pierschbacher, M.D.1    Ruoslahti, E.2
  • 21
    • 0028925423 scopus 로고
    • Function and receptor specificity of a minimal 20 kilodalton cell adhesive fragment of fibronectin
    • Akiyama, S.K., S. Aota, and K.M. Yamada. 1995. Function and receptor specificity of a minimal 20 kilodalton cell adhesive fragment of fibronectin. Cell Adhesion and Comm. 3:13-25.
    • (1995) Cell Adhesion and Comm. , vol.3 , pp. 13-25
    • Akiyama, S.K.1    Aota, S.2    Yamada, K.M.3
  • 22
    • 0029958940 scopus 로고    scopus 로고
    • VLA-3-mediated interaction with fibronectin induces cytokine production by human chondrocytes
    • Yonezawa, I., K. Kato, H. Yagita, Y. Yamauchi, and K. Okumura. 1996. VLA-3-mediated interaction with fibronectin induces cytokine production by human chondrocytes. Biochem. Biophys. Res. Comm. 219:261-265.
    • (1996) Biochem. Biophys. Res. Comm. , vol.219 , pp. 261-265
    • Yonezawa, I.1    Kato, K.2    Yagita, H.3    Yamauchi, Y.4    Okumura, K.5
  • 23
    • 0028987190 scopus 로고
    • Cooperative signaling by alpha 5 beta 1 and alpha 4 beta 1 integrins regulates metalloproteinase gene expression in fibroblasts adhering to fibronectin
    • Huhtala, P., M.J. Humphries, J.B. McCarthy, P.M. Tremble, Z. Werb, and C.H. Damsky. 1995. Cooperative signaling by alpha 5 beta 1 and alpha 4 beta 1 integrins regulates metalloproteinase gene expression in fibroblasts adhering to fibronectin. J. Cell Biol. 129:867-879.
    • (1995) J. Cell Biol. , vol.129 , pp. 867-879
    • Huhtala, P.1    Humphries, M.J.2    McCarthy, J.B.3    Tremble, P.M.4    Werb, Z.5    Damsky, C.H.6
  • 24
    • 0028979701 scopus 로고
    • Integrin alpha 5 beta 1 expression negatively regulates cell growth: Reversal by attachment to fibronectin
    • Varner, J.A., D.A. Emerson, and R.L. Juliano. 1995. Integrin alpha 5 beta 1 expression negatively regulates cell growth: reversal by attachment to fibronectin. Mol. Biol. Cell. 6:725-740.
    • (1995) Mol. Biol. Cell. , vol.6 , pp. 725-740
    • Varner, J.A.1    Emerson, D.A.2    Juliano, R.L.3
  • 25
    • 0000779060 scopus 로고
    • Un calibreur video simple pour l'utilisation en microscopic video
    • Goodman, A.M. 1989. Un calibreur video simple pour l'utilisation en microscopic video. Innov. Tech. Biol. Med. 9:350-356.
    • (1989) Innov. Tech. Biol. Med. , vol.9 , pp. 350-356
    • Goodman, A.M.1
  • 26
    • 0025969557 scopus 로고
    • Endothelial independence of myogenic response in isolated skeletal muscle arterioles
    • Falcone. J.C., M.J. Davis, and G.A. Meininger. 1991. Endothelial independence of myogenic response in isolated skeletal muscle arterioles. Am. J. Physiol. 260:H130-H135.
    • (1991) Am. J. Physiol. , vol.260
    • Falcone, J.C.1    Davis, M.J.2    Meininger, G.A.3
  • 27
    • 0028987030 scopus 로고
    • Endothelin ETA and ETB mRNA and receptors expressed by smooth muscle in the human vasculature: Majority of the ETA sub-type
    • Davenport, A.P., G. O'Reilly, and R.E. Kuc. 1995. Endothelin ETA and ETB mRNA and receptors expressed by smooth muscle in the human vasculature: majority of the ETA sub-type. Br. J. Pharmacol. 114:1110-1116.
    • (1995) Br. J. Pharmacol. , vol.114 , pp. 1110-1116
    • Davenport, A.P.1    O'Reilly, G.2    Kuc, R.E.3
  • 28
    • 0028950986 scopus 로고
    • Endothelin receptor subtypes in resistance arteries from humans and rats
    • Deng, L.-Y., J.-S. Li, and E.L. Schiffin. 1995. Endothelin receptor subtypes in resistance arteries from humans and rats. Cardiovasc. Res. 29:532-535.
    • (1995) Cardiovasc. Res. , vol.29 , pp. 532-535
    • Deng, L.-Y.1    Li, J.-S.2    Schiffin, E.L.3
  • 33
    • 0027993937 scopus 로고
    • Clustering of vitronectin and RGD peptides on microspheres leads to engagement of integrins on the luminal aspect of endothelial cell membrane
    • Zanetti, A., G. Conforti, S. Hess, I. Martin-Padura, E. Ghibaudi, K.T. Preissner, and E. Dejana. 1994. Clustering of vitronectin and RGD peptides on microspheres leads to engagement of integrins on the luminal aspect of endothelial cell membrane. Blood. 84:1116-1123.
    • (1994) Blood , vol.84 , pp. 1116-1123
    • Zanetti, A.1    Conforti, G.2    Hess, S.3    Martin-Padura, I.4    Ghibaudi, E.5    Preissner, K.T.6    Dejana, E.7
  • 34
    • 0029861687 scopus 로고    scopus 로고
    • Macromolecular composition of stress fiber-plasma membrane attachment sites in endothelial cells in situ
    • Kano, Y., K. Katoh, M. Masuda, and K. Fujiwara. 1996. Macromolecular composition of stress fiber-plasma membrane attachment sites in endothelial cells in situ. Circ. Res. 79:1000-1006.
    • (1996) Circ. Res. , vol.79 , pp. 1000-1006
    • Kano, Y.1    Katoh, K.2    Masuda, M.3    Fujiwara, K.4
  • 35
    • 0001023374 scopus 로고
    • A 125/115-kDa cell surface receptor specific for vitronectin interacts with the arginine-glycine-aspartic acid adhesion sequence derived from tibronectin
    • Pytela, R., M.D. Pierschbacher, and E. Ruoslahti. 1985. A 125/115-kDa cell surface receptor specific for vitronectin interacts with the arginine-glycine-aspartic acid adhesion sequence derived from tibronectin. Proc. Natl. Acad. Sci. USA. 82:5766-5770.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 5766-5770
    • Pytela, R.1    Pierschbacher, M.D.2    Ruoslahti, E.3
  • 37
    • 0026554217 scopus 로고
    • Affinity of integrins for damaged extracellular matrix: Alpha v beta 3 binds to denatured collagen type 1 through RGD sites
    • Davis, G.E. 1992. Affinity of integrins for damaged extracellular matrix: alpha v beta 3 binds to denatured collagen type 1 through RGD sites. Biochem. Biophys. Res. Commun. 182:1025-1031.
    • (1992) Biochem. Biophys. Res. Commun. , vol.182 , pp. 1025-1031
    • Davis, G.E.1
  • 38
    • 0024365390 scopus 로고
    • Arteriolar smooth muscle responses are modulated by an intramural diffusion barrier
    • Lew, M.J., R.J. Rivers, and B.R. Dialing. 1989. Arteriolar smooth muscle responses are modulated by an intramural diffusion barrier. Am. J. Physiol. 257:H10-H16.
    • (1989) Am. J. Physiol. , vol.257
    • Lew, M.J.1    Rivers, R.J.2    Dialing, B.R.3
  • 39
    • 0028586145 scopus 로고
    • New insights into the local regulation of blood How by perivascular nerves and endothelium
    • Burnstock, G., and V. Ralevic. 1994. New insights into the local regulation of blood How by perivascular nerves and endothelium. British J. Plast. Surg. 47:527-543.
    • (1994) British J. Plast. Surg. , vol.47 , pp. 527-543
    • Burnstock, G.1    Ralevic, V.2
  • 40
    • 0025605345 scopus 로고
    • Cloning and expression of a cDNa encoding an endothelin receptor
    • Arai, H., S. Hori, I. Aramori, H. Ohkubo, and S. Nakanishi. 1990. Cloning and expression of a cDNA encoding an endothelin receptor. Nature (Lond.). 348:730-732.
    • (1990) Nature (Lond.) , vol.348 , pp. 730-732
    • Arai, H.1    Hori, S.2    Aramori, I.3    Ohkubo, H.4    Nakanishi, S.5
  • 41
    • 0030272101 scopus 로고    scopus 로고
    • Integrin activation: The link between ligand binding and signal transduction
    • Humphries, M.J. 1996. Integrin activation: the link between ligand binding and signal transduction. Curr. Opin. Cell Biol. 8:632-640.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 632-640
    • Humphries, M.J.1
  • 42
    • 0021813717 scopus 로고
    • Detachment of cells from culture substrate by soluble fibronectin peptides
    • Hayman, E.G., M.D. Pierschbacher, and E. Ruoslahti. 1985. Detachment of cells from culture substrate by soluble fibronectin peptides. J. Cell Biol. 100:1948-1954.
    • (1985) J. Cell Biol. , vol.100 , pp. 1948-1954
    • Hayman, E.G.1    Pierschbacher, M.D.2    Ruoslahti, E.3
  • 43
    • 0025823869 scopus 로고
    • Reactivity of synthetic peptide analogs of adhesive proteins in regard to the interaction of human endothelial cells with extracellular matrix
    • Chen, C.S., and J. Hawiger. 1991. Reactivity of synthetic peptide analogs of adhesive proteins in regard to the interaction of human endothelial cells with extracellular matrix. Blood. 77:2200-2206.
    • (1991) Blood , vol.77 , pp. 2200-2206
    • Chen, C.S.1    Hawiger, J.2
  • 44
    • 0027395041 scopus 로고
    • Affinity modulation of integrin α5β1: Regulation of the functional response by soluble fibronectin
    • Faull, R.J., N.L. Kovach, J.M. Harlan, and M.H. Ginsberg. 1993. Affinity modulation of integrin α5β1: regulation of the functional response by soluble fibronectin. J. Cell. Biol. 121:155-162.
    • (1993) J. Cell. Biol. , vol.121 , pp. 155-162
    • Faull, R.J.1    Kovach, N.L.2    Harlan, J.M.3    Ginsberg, M.H.4
  • 45
    • 0023234612 scopus 로고
    • Effects of partial hepatectomy on plasma fibronectin concentrations in the rat Brit
    • Nilsson, T.K., Domellof, L., and L. Berghem. 1987. Effects of partial hepatectomy on plasma fibronectin concentrations in the rat Brit. J. Exp. Pathol. 68:421-425.
    • (1987) J. Exp. Pathol. , vol.68 , pp. 421-425
    • Nilsson, T.K.1    Domellof, L.2    Berghem, L.3


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