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Volumn 291, Issue 6, 2006, Pages

Pathological shear stress directly regulates platelet α IIbβ3 signaling

Author keywords

Integrin; Mechanoreceptor; Platelets; Shear stress; Signal transduction

Indexed keywords

ADAPTOR PROTEIN; ALPHA ACTININ; GLYCOPROTEIN IB; INTEGRIN; INTEGRIN ALPHA2B BETA3; MYOSIN HEAVY CHAIN; PROTEIN KINASE SYK; PROTEIN SH2; PROTEIN SLP 76; TYROSINE; VON WILLEBRAND FACTOR;

EID: 33845332376     PISSN: 03636143     EISSN: 15221563     Source Type: Journal    
DOI: 10.1152/ajpcell.00559.2005     Document Type: Article
Times cited : (34)

References (52)
  • 2
    • 0034762491 scopus 로고    scopus 로고
    • Activation of αvβ3-vitronectin binding is a multistage process in which increases in bond strength are dependent on Y747 and Y759 in the cytoplasmic domain of β3
    • Boettiger D, Huber F, Lynch L, and Blystone S. Activation of αvβ3-vitronectin binding is a multistage process in which increases in bond strength are dependent on Y747 and Y759 in the cytoplasmic domain of β3. Mol Biol Cell 12: 1227-1237, 2001.
    • (2001) Mol Biol Cell , vol.12 , pp. 1227-1237
    • Boettiger, D.1    Huber, F.2    Lynch, L.3    Blystone, S.4
  • 3
    • 0026766487 scopus 로고
    • Shear stress-induced von Willebrand factor binding to platelet glycoprotein Ib initiates calcium influx associated with aggregation
    • Chow TW, Hellums JD, Moake JL, and Kroll MH. Shear stress-induced von Willebrand factor binding to platelet glycoprotein Ib initiates calcium influx associated with aggregation. Blood 80: 113-120, 1992.
    • (1992) Blood , vol.80 , pp. 113-120
    • Chow, T.W.1    Hellums, J.D.2    Moake, J.L.3    Kroll, M.H.4
  • 4
    • 0035871241 scopus 로고    scopus 로고
    • Glycoprotein Ib/IX/V binding to the membrane skeleton maintains shear-induced platelets aggregation
    • Christodoulides N, Feng S, Resendiz JC, Berndt MC, and Kroll MH. Glycoprotein Ib/IX/V binding to the membrane skeleton maintains shear-induced platelets aggregation. Thromb Res 102: 133-142, 2001.
    • (2001) Thromb Res , vol.102 , pp. 133-142
    • Christodoulides, N.1    Feng, S.2    Resendiz, J.C.3    Berndt, M.C.4    Kroll, M.H.5
  • 5
    • 2442602269 scopus 로고    scopus 로고
    • Proximal, selective and dynamic interactions between integrin αIIbβ3 and protein tyrosine kinases in living cells
    • de Virgilio M, Kiosses WB, and Shattil SJ. Proximal, selective and dynamic interactions between integrin αIIbβ3 and protein tyrosine kinases in living cells. J Cell Biol 165: 305-311, 2004.
    • (2004) J Cell Biol , vol.165 , pp. 305-311
    • De Virgilio, M.1    Kiosses, W.B.2    Shattil, S.J.3
  • 7
    • 0034624990 scopus 로고    scopus 로고
    • Phosphorylation of protein kinase N by phosphoinositide-dependent protein kinase-1 mediates insulin signals to the actin cytoskeleton
    • Dong LQ, Landa LR, Wick MJ, Zhu L, Mukai H, Ono Y, and Liu F. Phosphorylation of protein kinase N by phosphoinositide-dependent protein kinase-1 mediates insulin signals to the actin cytoskeleton. Proc Natl Acad Sci 97: 5089-5094, 2000.
    • (2000) Proc Natl Acad Sci , vol.97 , pp. 5089-5094
    • Dong, L.Q.1    Landa, L.R.2    Wick, M.J.3    Zhu, L.4    Mukai, H.5    Ono, Y.6    Liu, F.7
  • 8
    • 26844466783 scopus 로고    scopus 로고
    • Regulation of 14-3-3 protein binding to GpIb/IX/V by the cytoplasmic domains of GpIbα and GpIbβ
    • Feng S, Christodoulides N, Resendiz JC, Berndt MC, and Kroll MH. Regulation of 14-3-3 protein binding to GpIb/IX/V by the cytoplasmic domains of GpIbα and GpIbβ. Blood 95: 550-557, 2000.
    • (2000) Blood , vol.95 , pp. 550-557
    • Feng, S.1    Christodoulides, N.2    Resendiz, J.C.3    Berndt, M.C.4    Kroll, M.H.5
  • 9
    • 0037192123 scopus 로고    scopus 로고
    • Pathological shear stress stimulates the tyrosine phosphorylation of α-actinin associated with the glycoprotein Ib-IX complex
    • Feng S, Reséndiz JC, Christodoulides N, Lu X, Arboleda D, Berndt MC, and Kroll MH. Pathological shear stress stimulates the tyrosine phosphorylation of α-actinin associated with the glycoprotein Ib-IX complex. Biochemistry 41: 1100-1108, 2002.
    • (2002) Biochemistry , vol.41 , pp. 1100-1108
    • Feng, S.1    Reséndiz, J.C.2    Christodoulides, N.3    Lu, X.4    Arboleda, D.5    Berndt, M.C.6    Kroll, M.H.7
  • 10
    • 0141679000 scopus 로고    scopus 로고
    • Filamin A binding to the cytoplasmic tail of glycoprotein Ibα regulates von Willebrand factor-induced platelet activation
    • Feng S, Reséndiz JC, Lu X, and Kroll MH. Filamin A binding to the cytoplasmic tail of glycoprotein Ibα regulates von Willebrand factor-induced platelet activation. Blood 102: 2122-2129, 2003.
    • (2003) Blood , vol.102 , pp. 2122-2129
    • Feng, S.1    Reséndiz, J.C.2    Lu, X.3    Kroll, M.H.4
  • 11
    • 0037178784 scopus 로고    scopus 로고
    • Exploring the neighborhood: Adhesion-coupled cell mechanosensors
    • Geiger B and Bershadsky A. Exploring the neighborhood: adhesion-coupled cell mechanosensors. Cell 110: 139-142, 2002.
    • (2002) Cell , vol.110 , pp. 139-142
    • Geiger, B.1    Bershadsky, A.2
  • 12
    • 0242361579 scopus 로고    scopus 로고
    • Talin1 is critical for force-dependent reinforcement of initial integrin-cytoskeletal bonds but not tyrosine kinase activation
    • Giannone G, Jiang G, Sutton DH, Critchley DR, and Sheetz MP. Talin1 is critical for force-dependent reinforcement of initial integrin-cytoskeletal bonds but not tyrosine kinase activation. J Cell Biol 163: 409-419, 2003.
    • (2003) J Cell Biol , vol.163 , pp. 409-419
    • Giannone, G.1    Jiang, G.2    Sutton, D.H.3    Critchley, D.R.4    Sheetz, M.P.5
  • 13
    • 4444260266 scopus 로고    scopus 로고
    • Platelet adhesion signaling and the regulation of thrombus formation
    • Gibbons JM. Platelet adhesion signaling and the regulation of thrombus formation. J Cell Sci 117: 3415-3425, 2004.
    • (2004) J Cell Sci , vol.117 , pp. 3415-3425
    • Gibbons, J.M.1
  • 14
    • 17644372407 scopus 로고    scopus 로고
    • Importance of temporal flow gradients and integrin αIIbβ3 mechanotransduction for shear-activation of platelets
    • Goncalves I, Nesbitt WS, Yuan Y, and Jackson SP. Importance of temporal flow gradients and integrin αIIbβ3 mechanotransduction for shear-activation of platelets. J Biol Chem 280: 15430-15437, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 15430-15437
    • Goncalves, I.1    Nesbitt, W.S.2    Yuan, Y.3    Jackson, S.P.4
  • 15
    • 1042274928 scopus 로고    scopus 로고
    • Different effects of various anti-GPIIb-IIIa agents on shear-induced platelet activation
    • Goto S, Tamura N, Li M, Handa M, Ikeda Y, Handa S, and Ruggeri ZM. Different effects of various anti-GPIIb-IIIa agents on shear-induced platelet activation. J Thromb Haemost 1: 2022-2030, 2003.
    • (2003) J Thromb Haemost , vol.1 , pp. 2022-2030
    • Goto, S.1    Tamura, N.2    Li, M.3    Handa, M.4    Ikeda, Y.5    Handa, S.6    Ruggeri, Z.M.7
  • 16
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional allosteric signaling machines
    • Hynes RO. Integrins: bidirectional allosteric signaling machines. Cell 110: 673-687, 2002.
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 17
    • 0037452771 scopus 로고    scopus 로고
    • Mechanosensation through integrins: Cells act locally but think globally
    • Ingber DE. Mechanosensation through integrins: cells act locally but think globally. Proc Natl Acad Sci USA 100: 1472-1474, 2003.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 1472-1474
    • Ingber, D.E.1
  • 18
    • 0012796190 scopus 로고    scopus 로고
    • Tensegrity II. How structural networks influence cellular information processing networks
    • Ingber DE. Tensegrity II. How structural networks influence cellular information processing networks. J Cell Sci 116: 1397-1408, 2003.
    • (2003) J Cell Sci , vol.116 , pp. 1397-1408
    • Ingber, D.E.1
  • 20
    • 0041461882 scopus 로고    scopus 로고
    • Two piconewton slip bind between fibronectin and the cytoskeleton depends on talin
    • Jiang G, Giannone G, Critchley DR, Fukumoto E, and Sheetz MP. Two piconewton slip bind between fibronectin and the cytoskeleton depends on talin. Nature 424: 334-337, 2003.
    • (2003) Nature , vol.424 , pp. 334-337
    • Jiang, G.1    Giannone, G.2    Critchley, D.R.3    Fukumoto, E.4    Sheetz, M.P.5
  • 21
  • 23
    • 20444465227 scopus 로고    scopus 로고
    • Integrin activation and matrix binding mediate cellular response to mechanical stretch
    • Katsumi A, Naoe T, Matsushita T, Kaibuchi K, and Schwartz MA. Integrin activation and matrix binding mediate cellular response to mechanical stretch. J Biol Chem 280: 16546-16549, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 16546-16549
    • Katsumi, A.1    Naoe, T.2    Matsushita, T.3    Kaibuchi, K.4    Schwartz, M.A.5
  • 25
    • 0033566876 scopus 로고    scopus 로고
    • Cytosolic calcium changes in a process of platelet adhesion and cohesion on a von Willebrand factor-coated surface under flow conditions
    • Kuwahara M, Sugimoto M, Tsuji S, Miyata S, and Yoshioka A. Cytosolic calcium changes in a process of platelet adhesion and cohesion on a von Willebrand factor-coated surface under flow conditions. Blood 94: 1149-1155, 1999.
    • (1999) Blood , vol.94 , pp. 1149-1155
    • Kuwahara, M.1    Sugimoto, M.2    Tsuji, S.3    Miyata, S.4    Yoshioka, A.5
  • 26
    • 0033592610 scopus 로고    scopus 로고
    • Integrin cytoplasmic tyrosine motif is required for outside-in αIIbβ3 signalling and platelet function
    • Law DA, DeGuzman FR, Heiser P, Ministri-Madrid K, and Phillips DR. Integrin cytoplasmic tyrosine motif is required for outside-in αIIbβ3 signalling and platelet function. Nature 410: 808-811, 1999.
    • (1999) Nature , vol.410 , pp. 808-811
    • Law, D.A.1    DeGuzman, F.R.2    Heiser, P.3    Ministri-Madrid, K.4    Phillips, D.R.5
  • 30
    • 0030953445 scopus 로고    scopus 로고
    • Integrin-mediated activation of focal adhesion kinase is independent of focal adhesion formation or integrin activation
    • Lyman S, Gilmore A, Burridge K, Gidwitz S, and White GC III. Integrin-mediated activation of focal adhesion kinase is independent of focal adhesion formation or integrin activation. J Biol Chem 272: 22538-22547, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 22538-22547
    • Lyman, S.1    Gilmore, A.2    Burridge, K.3    Gidwitz, S.4    White III, G.C.5
  • 31
    • 0023908222 scopus 로고
    • Shear-induced platelet aggregation can be mediated by VWF released from platelets, as well as exogenous large or unusually large VWF multimers, requires adenosine diphosphate, and is resistant to aspirin
    • Moake JL, Turner NA, Stathopoulos NA, Nolasco LH, and Hellums JD. Shear-induced platelet aggregation can be mediated by VWF released from platelets, as well as exogenous large or unusually large VWF multimers, requires adenosine diphosphate, and is resistant to aspirin. Blood 71: 1366-1374, 1988.
    • (1988) Blood , vol.71 , pp. 1366-1374
    • Moake, J.L.1    Turner, N.A.2    Stathopoulos, N.A.3    Nolasco, L.H.4    Hellums, J.D.5
  • 32
    • 0037283966 scopus 로고    scopus 로고
    • The structure and function of PKN, a protein kinase having a catalytic domain homologous to that of PKC
    • Mukai H. The structure and function of PKN, a protein kinase having a catalytic domain homologous to that of PKC. J Biochem 133: 17-27, 2003.
    • (2003) J Biochem , vol.133 , pp. 17-27
    • Mukai, H.1
  • 35
    • 0029023172 scopus 로고
    • Protein tyrosine phosphorylation in human platelets during shear stress-induced platelet aggregation is regulated by GpIb/IX as well as GpIIb-IIIa and requires intact cytoskeleton and endogenous ADP
    • Oda A, Yokoyama K, Murata M, Tokuhira M, Nakamura K, Handa M, Watanabe K, and Ikeda Y. Protein tyrosine phosphorylation in human platelets during shear stress-induced platelet aggregation is regulated by GpIb/IX as well as GpIIb-IIIa and requires intact cytoskeleton and endogenous ADP. Thromb Haemost 74: 736-742, 1995.
    • (1995) Thromb Haemost , vol.74 , pp. 736-742
    • Oda, A.1    Yokoyama, K.2    Murata, M.3    Tokuhira, M.4    Nakamura, K.5    Handa, M.6    Watanabe, K.7    Ikeda, Y.8
  • 37
    • 0028060528 scopus 로고
    • Shear stress-induced von Willebrand factor binding to platelets causes the activation of tyrosine kinase(s)
    • Razdan K, Hellums JD, and Kroll MH. Shear stress-induced von Willebrand factor binding to platelets causes the activation of tyrosine kinase(s). Biochem J 302: 681-686, 1994.
    • (1994) Biochem J , vol.302 , pp. 681-686
    • Razdan, K.1    Hellums, J.D.2    Kroll, M.H.3
  • 38
    • 0035958874 scopus 로고    scopus 로고
    • Dynamic modulation of cytoskeletal proteins linking integrins to signaling complexes in spreading cells
    • Reddy KB, Bialkowska K, and Fox JEB. Dynamic modulation of cytoskeletal proteins linking integrins to signaling complexes in spreading cells. J Biol Chem 276: 28300-28308, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 28300-28308
    • Reddy, K.B.1    Bialkowska, K.2    Fox, J.E.B.3
  • 39
    • 0037333465 scopus 로고    scopus 로고
    • Purinergic P2Y receptor blockade inhibits shear-induced platelet phosphatidylinositol 3-kinase activation
    • Reséndiz JC, Feng S, Ji G, Francis KA, Berndt MC, and Kroll MH. Purinergic P2Y receptor blockade inhibits shear-induced platelet phosphatidylinositol 3-kinase activation. Mol Pharmacol 63: 639-645, 2003.
    • (2003) Mol Pharmacol , vol.63 , pp. 639-645
    • Reséndiz, J.C.1    Feng, S.2    Ji, G.3    Francis, K.A.4    Berndt, M.C.5    Kroll, M.H.6
  • 40
    • 0036851876 scopus 로고    scopus 로고
    • Platelets in atherothrombosis
    • Ruggeri ZM. Platelets in atherothrombosis. Nat Med 8: 1227-1234, 2002.
    • (2002) Nat Med , vol.8 , pp. 1227-1234
    • Ruggeri, Z.M.1
  • 41
    • 0037119606 scopus 로고    scopus 로고
    • Contact-how platelets touch von Willebrand factor
    • Sadler JE. Contact-how platelets touch von Willebrand factor. Science 297: 1128-1129, 2002.
    • (2002) Science , vol.297 , pp. 1128-1129
    • Sadler, J.E.1
  • 42
    • 0033559816 scopus 로고    scopus 로고
    • Activation of integrin β3-associated Syk in platelets
    • Sarkar S, Rooney MM, and Lord ST. Activation of integrin β3-associated Syk in platelets. Biochem J 338: 677-680, 1999.
    • (1999) Biochem J , vol.338 , pp. 677-680
    • Sarkar, S.1    Rooney, M.M.2    Lord, S.T.3
  • 43
    • 0032483550 scopus 로고    scopus 로고
    • Specific synergy of multiple substrate-receptor interactions in platelet thrombus formation under flow
    • Savage B, Almus-Jacobs F, and Ruggeri ZM. Specific synergy of multiple substrate-receptor interactions in platelet thrombus formation under flow. Cell 94: 657-666, 1998.
    • (1998) Cell , vol.94 , pp. 657-666
    • Savage, B.1    Almus-Jacobs, F.2    Ruggeri, Z.M.3
  • 44
    • 4444264392 scopus 로고    scopus 로고
    • Integrins: Dynamic scaffolds for adhesion and signaling in platelets
    • Shattil SJ and Newman PJ. Integrins: dynamic scaffolds for adhesion and signaling in platelets. Blood 104: 1606-1615, 2004.
    • (2004) Blood , vol.104 , pp. 1606-1615
    • Shattil, S.J.1    Newman, P.J.2
  • 45
    • 0142091359 scopus 로고    scopus 로고
    • Soluble CD40 ligand induces β3 integrin tyrosine phosphorylation and triggers platelet activation by outside-in signaling
    • Srinivasa Prasad KS, Andre P, He M, Bao M, Manganello J, and Phillips DR. Soluble CD40 ligand induces β3 integrin tyrosine phosphorylation and triggers platelet activation by outside-in signaling. Proc Natl Acad Sci USA 100: 12367-12371, 2003.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 12367-12371
    • Srinivasa Prasad, K.S.1    Andre, P.2    He, M.3    Bao, M.4    Manganello, J.5    Phillips, D.R.6
  • 46
    • 7744232293 scopus 로고    scopus 로고
    • Activation of a signaling cascade by cell stretch
    • Tamada M, Sheetz MP, and Sawada M. Activation of a signaling cascade by cell stretch. Dev Cell 7: 709-718, 2004.
    • (2004) Dev Cell , vol.7 , pp. 709-718
    • Tamada, M.1    Sheetz, M.P.2    Sawada, M.3
  • 48
    • 0030664425 scopus 로고    scopus 로고
    • Truncation of the cytoplasmic domain of β3 in a variant form of Glanzmann thrombasthenia abrogates signaling through the integrin αIIbβ3 complex
    • Wang R, Shattil SJ, Ambruso DR, and Newman PJ. Truncation of the cytoplasmic domain of β3 in a variant form of Glanzmann thrombasthenia abrogates signaling through the integrin αIIbβ3 complex. J Clin Invest 100: 2393-2403, 1997.
    • (1997) J Clin Invest , vol.100 , pp. 2393-2403
    • Wang, R.1    Shattil, S.J.2    Ambruso, D.R.3    Newman, P.J.4
  • 50
    • 0037131428 scopus 로고    scopus 로고
    • The N-terminal SH2 domains of Syk and ZAP-70 mediate phosphotyrosine- independent binding to integrin β cytoplasmic domains
    • Woodside DG, Obergfell A, Leng L, Talapatra A, Calderwood DA, Shattil SJ, and Ginsberg MH. The N-terminal SH2 domains of Syk and ZAP-70 mediate phosphotyrosine-independent binding to integrin β cytoplasmic domains. J Biol Chem 277: 39401-39408, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 39401-39408
    • Woodside, D.G.1    Obergfell, A.2    Leng, L.3    Talapatra, A.4    Calderwood, D.A.5    Shattil, S.J.6    Ginsberg, M.H.7
  • 51
    • 0042672885 scopus 로고    scopus 로고
    • Critical roles for the COOH-terminal NITY and RGT sequences of integrin β3 cytoplasmic domain in inside-out and outside-in signaling
    • Xi X, Bodnar RJ, Li Z, Lam SCT, and Du X. Critical roles for the COOH-terminal NITY and RGT sequences of integrin β3 cytoplasmic domain in inside-out and outside-in signaling. J Cell Biol 162: 329-339, 2003.
    • (2003) J Cell Biol , vol.162 , pp. 329-339
    • Xi, X.1    Bodnar, R.J.2    Li, Z.3    Lam, S.C.T.4    Du, X.5
  • 52
    • 0031568534 scopus 로고    scopus 로고
    • Protein tyrosine kinases Syk and Zap-70 display distinct requirements for Src family kinases in immune response receptor signal transduction
    • Zoller KE, MacNeil IA, and Brugge JS. Protein tyrosine kinases Syk and Zap-70 display distinct requirements for Src family kinases in immune response receptor signal transduction. J Immunol 158: 1650-1659, 1997.
    • (1997) J Immunol , vol.158 , pp. 1650-1659
    • Zoller, K.E.1    MacNeil, I.A.2    Brugge, J.S.3


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