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Volumn 36, Issue 8, 1998, Pages 1087-1099

Full-spreading platelets induced by the recombinant rhodostomin are via binding to integrins and correlated with FAK phosphorylation

Author keywords

[No Author keywords available]

Indexed keywords

DISINTEGRIN; HYBRID PROTEIN; RECOMBINANT PROTEIN; SNAKE VENOM;

EID: 0031865984     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0041-0101(98)00088-9     Document Type: Article
Times cited : (27)

References (44)
  • 1
    • 0026350087 scopus 로고
    • Solution structure of kistrin, a potent platelet aggregation inhibitor and GP IIb-IIIa antagonist
    • Adler M., Lazarus R. A., Dennis M. S., Wagner G. Solution structure of kistrin, a potent platelet aggregation inhibitor and GP IIb-IIIa antagonist. Science. 253:1991;445-448.
    • (1991) Science , vol.253 , pp. 445-448
    • Adler, M.1    Lazarus, R.A.2    Dennis, M.S.3    Wagner, G.4
  • 3
    • 0026348765 scopus 로고
    • A common precursor for a putative hemorrhagic protein and rhodostomin, a platelet aggregation inhibitor of the venom of Calloselasma rhodosotma: Molecular cloning and sequence analysis
    • Au L. C., Huang Y. B., Huang T.-F., Teh G. W., Lin H. H., Choo K. B. A common precursor for a putative hemorrhagic protein and rhodostomin, a platelet aggregation inhibitor of the venom of Calloselasma rhodosotma: molecular cloning and sequence analysis. Biochem. Biophys. Res. Commun. 181:1991;585-593.
    • (1991) Biochem. Biophys. Res. Commun. , vol.181 , pp. 585-593
    • Au, L.C.1    Huang, Y.B.2    Huang, T.-F.3    Teh, G.W.4    Lin, H.H.5    Choo, K.B.6
  • 4
    • 0027229427 scopus 로고
    • Evidence for selective association of a subpopulation of GPIIb-IIIa with the actin cytoskeletons of thrombin-activated platelets
    • Bertagnolli M. E., Beckerle M. C. Evidence for selective association of a subpopulation of GPIIb-IIIa with the actin cytoskeletons of thrombin-activated platelets. J. Cell. Biol. 121:1993;1329-1342.
    • (1993) J. Cell. Biol. , vol.121 , pp. 1329-1342
    • Bertagnolli, M.E.1    Beckerle, M.C.2
  • 5
    • 0027182176 scopus 로고
    • Rhodosotmin, an RGD-containing peptide expressed from a synthetic gene in Escherichia coli, facilitates the attachment of human hepatoma cells
    • Chang H. H., Hu S. T., Huang T.-F., Chen S. H., Lee Y.-H. W., Lo S. J. Rhodosotmin, an RGD-containing peptide expressed from a synthetic gene in Escherichia coli, facilitates the attachment of human hepatoma cells. Biochem. Biophys. Res. Commun. 190:1993;242-249.
    • (1993) Biochem. Biophys. Res. Commun. , vol.190 , pp. 242-249
    • Chang, H.H.1    Hu, S.T.2    Huang, T.-F.3    Chen, S.H.4    Lee Y.-H., W.5    Lo, S.J.6
  • 6
    • 0031081687 scopus 로고    scopus 로고
    • Glutathione S-transferase-rhodostomin fusion protein inhibits platelet aggregation and induces platelet shape change
    • Chang H. H., Tsai W. J., Lo S. J. Glutathione S-transferase-rhodostomin fusion protein inhibits platelet aggregation and induces platelet shape change. Toxicon. 35:1997;195-204.
    • (1997) Toxicon , vol.35 , pp. 195-204
    • Chang, H.H.1    Tsai, W.J.2    Lo, S.J.3
  • 7
    • 0029120801 scopus 로고
    • Integrins and modulation of transmitter release from motor nerve terminals by stretch
    • Chen B.-M., Grinnell A. D. Integrins and modulation of transmitter release from motor nerve terminals by stretch. Science. 269:1995;1578-1580.
    • (1995) Science , vol.269 , pp. 1578-1580
    • Chen, B.-M.1    Grinnell, A.D.2
  • 8
    • 0030028743 scopus 로고    scopus 로고
    • Signaling through chemoattractant receptors in Dictyostelium
    • Chen M.-Y., Insall R. H., Devreotes P. N. Signaling through chemoattractant receptors in Dictyostelium. Trends Genet. 12:1996;52-57.
    • (1996) Trends Genet. , vol.12 , pp. 52-57
    • Chen, M.-Y.1    Insall, R.H.2    Devreotes, P.N.3
  • 9
    • 0030272735 scopus 로고    scopus 로고
    • Integrin cytoplasmic interactions and bidirectional transmembrane signalling
    • Dedhar S., Hannigan G. E. Integrin cytoplasmic interactions and bidirectional transmembrane signalling. Curr. Opin. Cell Biol. 8:1996;657-669.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 657-669
    • Dedhar, S.1    Hannigan, G.E.2
  • 13
  • 14
    • 0028337108 scopus 로고
    • CDNA sequences for four snake venom metalloproteinases: Structure, classification and their relationship to mammalian reproductive proteins
    • Hite L. A., Jia L. G., Bjarnason J. B., Fox J. W. cDNA sequences for four snake venom metalloproteinases: structure, classification and their relationship to mammalian reproductive proteins. Arch. Biochem. Biophys. 308:1994;182-191.
    • (1994) Arch. Biochem. Biophys. , vol.308 , pp. 182-191
    • Hite, L.A.1    Jia, L.G.2    Bjarnason, J.B.3    Fox, J.W.4
  • 15
    • 0028560391 scopus 로고
    • Disintegrins: The naturally-occurring antagonists of platelet fibrinogen receptor
    • Huang T.-F., Niewiarowski S. Disintegrins: the naturally-occurring antagonists of platelet fibrinogen receptor. J. Toxicol. Toxin Rev. 13:1994;253-273.
    • (1994) J. Toxicol. Toxin Rev. , vol.13 , pp. 253-273
    • Huang, T.-F.1    Niewiarowski, S.2
  • 16
    • 0029935373 scopus 로고    scopus 로고
    • Changes in cytosolic calcium concentrations and cell morphology in single platelets adhered to fibrinogen-coated surface under flow
    • Jen C. J., Chen H.-i., Lai K.-c., Usami S. Changes in cytosolic calcium concentrations and cell morphology in single platelets adhered to fibrinogen-coated surface under flow. Blood. 87:1996;3775-3782.
    • (1996) Blood , vol.87 , pp. 3775-3782
    • Jen, C.J.1    Chen, H.-i.2    Lai, K.-c.3    Usami, S.4
  • 17
    • 0040378974 scopus 로고
    • Search for relationship among the hemolytic, phosphorolytic and neurotoxic activities of snake venoms
    • Jeng T. W., Hendon R. A., Fraenkel-Conrat H. Search for relationship among the hemolytic, phosphorolytic and neurotoxic activities of snake venoms. Proc. Natl. Acad. Sci. U.S.A. 75:1978;600-604.
    • (1978) Proc. Natl. Acad. Sci. U.S.A. , vol.75 , pp. 600-604
    • Jeng, T.W.1    Hendon, R.A.2    Fraenkel-Conrat, H.3
  • 18
    • 0030273873 scopus 로고    scopus 로고
    • Snake venom metalloproteinases: Structure, function and relationship to the ADAMs family of proteins
    • Jia L. G., Shimokawa K., Bjarnason J. B., Fox J. W. Snake venom metalloproteinases: structure, function and relationship to the ADAMs family of proteins. Toxicon. 34:1996;1269-1276.
    • (1996) Toxicon , vol.34 , pp. 1269-1276
    • Jia, L.G.1    Shimokawa, K.2    Bjarnason, J.B.3    Fox, J.W.4
  • 19
    • 0001765604 scopus 로고
    • Chemistry of protein toxins in snake toxins
    • Karlsson E. Chemistry of protein toxins in snake toxins. Handb. Exp. Pharmacol. 52:1979;159-212.
    • (1979) Handb. Exp. Pharmacol. , vol.52 , pp. 159-212
    • Karlsson, E.1
  • 20
    • 0029016906 scopus 로고
    • The exchange of Arg-Gly-Asp (RGD) and Arg-Tyr-ASp (RYD) binding sequences in integrin alpha IIb beta 3 does not alter integrin recognition
    • Kunicki T. J., Ely K. R., Kunicki T. C., Tomilama Y., Amris D. S. The exchange of Arg-Gly-Asp (RGD) and Arg-Tyr-ASp (RYD) binding sequences in integrin alpha IIb beta 3 does not alter integrin recognition. J. Biol. Chem. 270:1995;16660-16665.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16660-16665
    • Kunicki, T.J.1    Ely, K.R.2    Kunicki, T.C.3    Tomilama, Y.4    Amris, D.S.5
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0015275403 scopus 로고
    • Chemistry and pharmacology of polypeptide toxins in snake venoms
    • Lee C. Y. Chemistry and pharmacology of polypeptide toxins in snake venoms. Ann. Rev. Pharmacol. 12:1972;265-286.
    • (1972) Ann. Rev. Pharmacol. , vol.12 , pp. 265-286
    • Lee, C.Y.1
  • 24
    • 0018386629 scopus 로고
    • ACTH-induced internalization of plasma membrane in xanthophores of the goldfish, Carassius auratus L.
    • Lo S. J., Taylor J. D., Tchen T. T. ACTH-induced internalization of plasma membrane in xanthophores of the goldfish, Carassius auratus L. Biochem. Biophys. Res. Commun. 86:1980;748-754.
    • (1980) Biochem. Biophys. Res. Commun. , vol.86 , pp. 748-754
    • Lo, S.J.1    Taylor, J.D.2    Tchen, T.T.3
  • 25
    • 0025365318 scopus 로고
    • Sequence of a cDNA encoding the platelet aggregation inhibitor trigramin
    • Neeper M. P., Jacobson M. A. Sequence of a cDNA encoding the platelet aggregation inhibitor trigramin. Nucl. Acids Res. 18:1990;4255-4265.
    • (1990) Nucl. Acids Res. , vol.18 , pp. 4255-4265
    • Neeper, M.P.1    Jacobson, M.A.2
  • 26
    • 0026451081 scopus 로고
    • Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C
    • Nishizuka Y. Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C. Science. 258:1992;607-614.
    • (1992) Science , vol.258 , pp. 607-614
    • Nishizuka, Y.1
  • 27
    • 0028961293 scopus 로고
    • Rho, rac and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia and filopodia
    • Nobes C. D., Hall A. Rho, rac and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia and filopodia. Cell. 81:1995;53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 28
    • 0027096622 scopus 로고
    • Signal transduction by the platelet integrin αiIbβ3: Induction of calcium oscillations required for protein-tyrosine phosphorylation and ligand-induced spreading of stably transfected cells
    • Pelletier A. J., Bodary S. C., Levinson A. D. Signal transduction by the platelet integrin αIIbβ3: induction of calcium oscillations required for protein-tyrosine phosphorylation and ligand-induced spreading of stably transfected cells. Mol. Biol. Cell. 3:1992;989-998.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 989-998
    • Pelletier, A.J.1    Bodary, S.C.2    Levinson, A.D.3
  • 29
  • 30
    • 0021027332 scopus 로고
    • Interaction of Ap2, a monoclonal antibody specific for the human platelet glycoprotein IIb-IIIa complex, with intact platelets
    • Pidard D., Montgomery R. R., Bennett J. S., Kunicki T. J. Interaction of Ap2, a monoclonal antibody specific for the human platelet glycoprotein IIb-IIIa complex, with intact platelets. J. Biol. Chem. 258:1983;12582-12586.
    • (1983) J. Biol. Chem. , vol.258 , pp. 12582-12586
    • Pidard, D.1    Montgomery, R.R.2    Bennett, J.S.3    Kunicki, T.J.4
  • 31
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley A. J., Hall A. The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell. 70:1992;389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 32
    • 0026654125 scopus 로고
    • The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
    • Ridley A. J., Paterson H. F., Johnston C. L., Diekmann D., Hall A. The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell. 70:1992;401-410.
    • (1992) Cell , vol.70 , pp. 401-410
    • Ridley, A.J.1    Paterson, H.F.2    Johnston, C.L.3    Diekmann, D.4    Hall, A.5
  • 33
    • 0025267690 scopus 로고
    • Calcium signaling in human platelets
    • Rink T. J., Sage S. O. Calcium signaling in human platelets. Annu. Rev. Physiol. 52:1990;431-449.
    • (1990) Annu. Rev. Physiol. , vol.52 , pp. 431-449
    • Rink, T.J.1    Sage, S.O.2
  • 34
    • 0024467195 scopus 로고
    • Ligand inhibition of the platelet glycoprotein IIb-IIIa complex function as a calcium channel in liposomes
    • Rybak M. E. M., Renzulli L. A. Ligand inhibition of the platelet glycoprotein IIb-IIIa complex function as a calcium channel in liposomes. J. Biol. Chem. 264:1989;14617-14620.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14617-14620
    • Rybak, M.E.M.1    Renzulli, L.A.2
  • 36
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusion with glutathione S-transferase
    • Smith D. B., Johnson K. S. Single-step purification of polypeptides expressed in Escherichia coli as fusion with glutathione S-transferase. Gene. 67:1988;31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 37
    • 0025729301 scopus 로고
    • Inventory of exogenous inhibitors of platelet aggregation
    • Teng C.-M., Huang T.-F. Inventory of exogenous inhibitors of platelet aggregation. Thromb. Haemostas. 65:1991;624-626.
    • (1991) Thromb. Haemostas. , vol.65 , pp. 624-626
    • Teng, C.-M.1    Huang, T.-F.2
  • 38
    • 0025904530 scopus 로고
    • Snake venom constituents that affect platelet function
    • Teng C.-M., Huang T.-F. Snake venom constituents that affect platelet function. Platelets. 2:1991;77-87.
    • (1991) Platelets , vol.2 , pp. 77-87
    • Teng, C.-M.1    Huang, T.-F.2
  • 39
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H., Stachelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U.S.A. 76:1979;4350-4354.
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Stachelin, T.2    Gordon, J.3
  • 40
    • 0028355410 scopus 로고
    • A family of cellular proteins related to snake venom disintegrin
    • Weskamp G., Blobel C. P. A family of cellular proteins related to snake venom disintegrin. Proc. Natl. Acad. Sci. U.S.A. 91:1994;2748-2751.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 2748-2751
    • Weskamp, G.1    Blobel, C.P.2
  • 41
    • 0030049705 scopus 로고    scopus 로고
    • MDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domains
    • Weskamp G., Kratzschmar J., Reid M. S., Blobel C. P. MDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domains. J. Cell Biol. 132:1996;717-726.
    • (1996) J. Cell Biol. , vol.132 , pp. 717-726
    • Weskamp, G.1    Kratzschmar, J.2    Reid, M.S.3    Blobel, C.P.4
  • 42
    • 0028936855 scopus 로고
    • Mechanism of shape change in chilled human platelets
    • Winokur R., Hartwig J. H. Mechanism of shape change in chilled human platelets. Blood. 85:1995;1796-1804.
    • (1995) Blood , vol.85 , pp. 1796-1804
    • Winokur, R.1    Hartwig, J.H.2
  • 43
    • 0028820623 scopus 로고
    • ADAM, a novel family of membrane proteins containing a disintegrin and metalloprotease domain: Multipotential functions in cell-cell and cell-matrix interactions
    • Wolfsberg T. G., Primakoff P., Myles D. G., White J. M. ADAM, a novel family of membrane proteins containing a disintegrin and metalloprotease domain: multipotential functions in cell-cell and cell-matrix interactions. J. Cell Biol. 131:1995;275-278.
    • (1995) J. Cell Biol. , vol.131 , pp. 275-278
    • Wolfsberg, T.G.1    Primakoff, P.2    Myles, D.G.3    White, J.M.4


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