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Volumn 288, Issue 42, 2013, Pages 30672-30681

Mitochondrially mediated integrin αiIbβ3 protein inactivation limits thrombus growth

Author keywords

[No Author keywords available]

Indexed keywords

BINDING AFFINITIES; CALPAINS; INTEGRINS; MITOCHONDRIAL PERMEABILITY TRANSITION PORE; PLATELET AGGREGATION; PROTEOLYTIC CLEAVAGE;

EID: 84886912940     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.472688     Document Type: Article
Times cited : (32)

References (47)
  • 1
    • 0037050027 scopus 로고    scopus 로고
    • Stimulated platelets use serotonin to enhance their retention of procoagulant proteins on the cell surface
    • Dale, G. L., Friese, P., Batar, P., Hamilton, S. F., Reed, G. L., Jackson, K. W., Clemetson, K. J., and Alberio, L. (2002) Stimulated platelets use serotonin to enhance their retention of procoagulant proteins on the cell surface. Nature 415, 175-179
    • (2002) Nature , vol.415 , pp. 175-179
    • Dale, G.L.1    Friese, P.2    Batar, P.3    Hamilton, S.F.4    Reed, G.L.5    Jackson, K.W.6    Clemetson, K.J.7    Alberio, L.8
  • 3
    • 0034161567 scopus 로고    scopus 로고
    • Surface expression and functional characterization of -granule factor v in human platelets. Effects of ionophore A23187, thrombin, collagen, and convulxin
    • Alberio, L., Safa, O., Clemetson, K. J., Esmon, C. T., and Dale, G. L. (2000) Surface expression and functional characterization of -granule factor V in human platelets. Effects of ionophore A23187, thrombin, collagen, and convulxin. Blood 95, 1694-1702
    • (2000) Blood , vol.95 , pp. 1694-1702
    • Alberio, L.1    Safa, O.2    Clemetson, K.J.3    Esmon, C.T.4    Dale, G.L.5
  • 4
    • 28444436585 scopus 로고    scopus 로고
    • Coated-platelets. An emerging component of the procoagulant response
    • Dale, G. L. (2005) Coated-platelets. An emerging component of the procoagulant response. J. Thromb. Haemost 3, 2185-2192
    • (2005) J. Thromb. Haemost , vol.3 , pp. 2185-2192
    • Dale, G.L.1
  • 5
    • 0030845821 scopus 로고    scopus 로고
    • Collagen but not fibrinogen surfaces induce bleb formation, exposure of phosphatidylserine, and procoagulant activity of adherent platelets. Evidence for regulation by protein tyrosine kinase-dependent Ca2 responses
    • Heemskerk, J. W., Vuist, W. M., Feijge, M. A., Reutelingsperger, C. P., and Lindhout, T. (1997) Collagen but not fibrinogen surfaces induce bleb formation, exposure of phosphatidylserine, and procoagulant activity of adherent platelets. Evidence for regulation by protein tyrosine kinase-dependent Ca2 responses. Blood 90, 2615-2625
    • (1997) Blood , vol.90 , pp. 2615-2625
    • Heemskerk, J.W.1    Vuist, W.M.2    Feijge, M.A.3    Reutelingsperger, C.P.4    Lindhout, T.5
  • 6
    • 0035001103 scopus 로고    scopus 로고
    • Procoagulant platelet balloons. Evidence from cryopreparation and electron microscopy
    • Hess, M. W., and Siljander, P. (2001) Procoagulant platelet balloons. Evidence from cryopreparation and electron microscopy. Histochem. Cell Biol. 115, 439-443
    • (2001) Histochem. Cell Biol. , vol.115 , pp. 439-443
    • Hess, M.W.1    Siljander, P.2
  • 7
    • 3142674975 scopus 로고    scopus 로고
    • Platelet factor XIII and calpain negatively regulate integrin IIb 3 adhesive function and thrombus growth
    • Kulkarni, S., and Jackson, S. P. (2004) Platelet factor XIII and calpain negatively regulate integrin IIb 3 adhesive function and thrombus growth. J. Biol. Chem. 279, 30697-30706
    • (2004) J. Biol. Chem. , vol.279 , pp. 30697-30706
    • Kulkarni, S.1    Jackson, S.P.2
  • 8
    • 38949218420 scopus 로고    scopus 로고
    • Critical role for the mitochondrial permeability transition pore and cyclophilinDin platelet activation and thrombosis
    • Jobe, S. M., Wilson, K. M., Leo, L., Raimondi, A., Molkentin, J. D., Lentz, S. R., and Di Paola, J. (2008) Critical role for the mitochondrial permeability transition pore and cyclophilinDin platelet activation and thrombosis. Blood 111, 1257-1265
    • (2008) Blood , vol.111 , pp. 1257-1265
    • Jobe, S.M.1    Wilson, K.M.2    Leo, L.3    Raimondi, A.4    Molkentin, J.D.5    Lentz, S.R.6    Di Paola, J.7
  • 9
    • 0344151494 scopus 로고    scopus 로고
    • Von Willebrand factor stimulates thrombin-induced exposure of procoagulant phospholipids on the surface of fibrinadherent platelets
    • Briedé, J. J., Wielders, S. J., Heemskerk, J. W., Baruch, D., Hemker, H. C., and Lindhout, T. (2003) Von Willebrand factor stimulates thrombin-induced exposure of procoagulant phospholipids on the surface of fibrinadherent platelets. J. Thromb. Haemost. 1, 559-565
    • (2003) J. Thromb. Haemost. , vol.1 , pp. 559-565
    • Briedé, J.J.1    Wielders, S.J.2    Heemskerk, J.W.3    Baruch, D.4    Hemker, H.C.5    Lindhout, T.6
  • 10
  • 14
    • 84861108468 scopus 로고    scopus 로고
    • Identification of different proaggregatory abilities of activated platelet subpopulations
    • Yakimenko, A. O., Verholomova, F. Y., Kotova, Y. N., Ataullakhanov, F. I., and Panteleev, M. A. (2012) Identification of different proaggregatory abilities of activated platelet subpopulations. Biophys. J. 102, 2261-2269
    • (2012) Biophys. J. , vol.102 , pp. 2261-2269
    • Yakimenko, A.O.1    Verholomova, F.Y.2    Kotova, Y.N.3    Ataullakhanov, F.I.4    Panteleev, M.A.5
  • 15
    • 13244283340 scopus 로고    scopus 로고
    • Role of mitochondrial permeability transition pore in coated-platelet formation
    • Remenyi, G., Szasz, R., Friese, P., and Dale, G. L. (2005) Role of mitochondrial permeability transition pore in coated-platelet formation. Arterioscler. Thromb. Vasc. Biol. 25, 467-471
    • (2005) Arterioscler. Thromb. Vasc. Biol. , vol.25 , pp. 467-471
    • Remenyi, G.1    Szasz, R.2    Friese, P.3    Dale, G.L.4
  • 16
    • 67349117275 scopus 로고    scopus 로고
    • What is the mitochondrial permeability transition pore
    • Halestrap, A. P. (2009) What is the mitochondrial permeability transition pore? J. Mol. Cell Cardiol. 46, 821-831
    • (2009) J. Mol. Cell Cardiol. , vol.46 , pp. 821-831
    • Halestrap, A.P.1
  • 18
    • 0035958967 scopus 로고    scopus 로고
    • Calpain cleavage promotes talin binding to the 3 integrin cytoplasmic domain
    • Yan, B., Calderwood, D. A., Yaspan, B., and Ginsberg, M. H. (2001) Calpain cleavage promotes talin binding to the 3 integrin cytoplasmic domain. J. Biol. Chem. 276, 28164-28170
    • (2001) J. Biol. Chem. , vol.276 , pp. 28164-28170
    • Yan, B.1    Calderwood, D.A.2    Yaspan, B.3    Ginsberg, M.H.4
  • 19
    • 0042672885 scopus 로고    scopus 로고
    • Critical roles for the COOH-terminal NITY and RGT sequences of the integrin 3 cytoplasmic domain in inside-out and outside-in signaling
    • Xi, X., Bodnar, R. J., Li, Z., Lam, S. C., and Du, X. (2003) Critical roles for the COOH-terminal NITY and RGT sequences of the integrin 3 cytoplasmic domain in inside-out and outside-in signaling. J. Cell Biol. 162, 329-339
    • (2003) J. Cell Biol. , vol.162 , pp. 329-339
    • Xi, X.1    Bodnar, R.J.2    Li, Z.3    Lam, S.C.4    Du, X.5
  • 21
    • 0037108427 scopus 로고    scopus 로고
    • Role of the adapter protein SLP-76 in GPVI-dependent platelet procoagulant responses to collagen
    • Leo, L., Di Paola, J., Judd, B. A., Koretzky, G. A., and Lentz, S. R. (2002) Role of the adapter protein SLP-76 in GPVI-dependent platelet procoagulant responses to collagen. Blood 100, 2839-2844
    • (2002) Blood , vol.100 , pp. 2839-2844
    • Leo, L.1    Di Paola, J.2    Judd, B.A.3    Koretzky, G.A.4    Lentz, S.R.5
  • 22
    • 56749092145 scopus 로고    scopus 로고
    • Microfluidic focal thrombosis model for measuring murine platelet deposition and stability. PAR4 signaling enhances shear-resistance of platelet aggregates
    • Neeves, K. B., Maloney, S. F., Fong, K. P., Schmaier, A. A., Kahn, M. L., Brass, L. F., and Diamond, S. L. (2008) Microfluidic focal thrombosis model for measuring murine platelet deposition and stability. PAR4 signaling enhances shear-resistance of platelet aggregates. J. Thromb. Haemost. 6, 2193-2201
    • (2008) J. Thromb. Haemost. , vol.6 , pp. 2193-2201
    • Neeves, K.B.1    Maloney, S.F.2    Fong, K.P.3    Schmaier, A.A.4    Kahn, M.L.5    Brass, L.F.6    Diamond, S.L.7
  • 24
    • 0031028205 scopus 로고    scopus 로고
    • Calpain cleavage of focal adhesion proteins regulates the cytoskeletal attachment of integrin IIb 3 (platelet glycoprotein IIb/IIIa) and the cellular retraction of fibrin clots
    • Schoenwaelder, S. M., Yuan, Y., Cooray, P., Salem, H. H., and Jackson, S. P. (1997) Calpain cleavage of focal adhesion proteins regulates the cytoskeletal attachment of integrin IIb 3 (platelet glycoprotein IIb/IIIa) and the cellular retraction of fibrin clots. J. Biol. Chem. 272, 1694-1702
    • (1997) J. Biol. Chem. , vol.272 , pp. 1694-1702
    • Schoenwaelder, S.M.1    Yuan, Y.2    Cooray, P.3    Salem, H.H.4    Jackson, S.P.5
  • 25
    • 21244446551 scopus 로고    scopus 로고
    • Properties of the permeability transition pore in mitochondria devoid of cyclophilin D
    • Basso, E., Fante, L., Fowlkes, J., Petronilli, V., Forte, M. A., and Bernardi, P. (2005) Properties of the permeability transition pore in mitochondria devoid of cyclophilin D. J. Biol. Chem. 280, 18558-18561
    • (2005) J. Biol. Chem. , vol.280 , pp. 18558-18561
    • Basso, E.1    Fante, L.2    Fowlkes, J.3    Petronilli, V.4    Forte, M.A.5    Bernardi, P.6
  • 26
    • 84870061461 scopus 로고    scopus 로고
    • Mitochondrial calcium and reactive oxygen species regulate agonist-initiated platelet phosphatidylserine exposure
    • Choo, H. J., Saafir, T. B., Mkumba, L., Wagner, M. B., and Jobe, S. M. (2012) Mitochondrial calcium and reactive oxygen species regulate agonist-initiated platelet phosphatidylserine exposure. Arterioscler. Thromb. Vasc. Biol. 32, 2946-2955
    • (2012) Arterioscler. Thromb. Vasc. Biol. , vol.32 , pp. 2946-2955
    • Choo, H.J.1    Saafir, T.B.2    Mkumba, L.3    Wagner, M.B.4    Jobe, S.M.5
  • 28
    • 0032496059 scopus 로고    scopus 로고
    • PH dependency of -calpain and m-calpain activity assayed by casein zymography following traumatic brain injury in the rat
    • Zhao, X., Newcomb, J. K., Posmantur, R. M., Wang, K. K., Pike, B. R., and Hayes, R. L. (1998) pH dependency of -calpain and m-calpain activity assayed by casein zymography following traumatic brain injury in the rat. Neurosci Lett. 247, 53-57
    • (1998) Neurosci Lett. , vol.247 , pp. 53-57
    • Zhao, X.1    Newcomb, J.K.2    Posmantur, R.M.3    Wang, K.K.4    Pike, B.R.5    Hayes, R.L.6
  • 29
    • 0019825086 scopus 로고
    • Changes in cytoplasmic pH and in membrane potential in thrombin-stimulated human platelets
    • Horne, W. C., Norman, N. E., Schwartz, D. B., and Simons, E. R. (1981) Changes in cytoplasmic pH and in membrane potential in thrombin-stimulated human platelets. Eur. J. Biochem. 120, 295-302
    • (1981) Eur. J. Biochem. , vol.120 , pp. 295-302
    • Horne, W.C.1    Norman, N.E.2    Schwartz, D.B.3    Simons, E.R.4
  • 30
    • 0014690129 scopus 로고
    • Clot retraction and energy metabolism of platelets. Effect and mechanism of inhibitors
    • Mürer, E. H. (1969) Clot retraction and energy metabolism of platelets. Effect and mechanism of inhibitors. Biochim. Biophys. Acta 172, 266-276
    • (1969) Biochim. Biophys. Acta , vol.172 , pp. 266-276
    • Mürer, E.H.1
  • 32
    • 40449133970 scopus 로고    scopus 로고
    • Kindlin-3 is essential for integrin activation and platelet aggregation
    • Moser, M., Nieswandt, B., Ussar, S., Pozgajova, M., and Fässler, R. (2008) Kindlin-3 is essential for integrin activation and platelet aggregation. Nat. Med. 14, 325-330
    • (2008) Nat. Med. , vol.14 , pp. 325-330
    • Moser, M.1    Nieswandt, B.2    Ussar, S.3    Pozgajova, M.4    Fässler, R.5
  • 33
    • 0029086557 scopus 로고
    • Phosphatidylserine exposure on the platelet plasma membrane during A23187-induced activation is independent of cytoskeleton reorganization
    • Gaffet, P., Bettache, N., and Bienvenüe, A. (1995) Phosphatidylserine exposure on the platelet plasma membrane during A23187-induced activation is independent of cytoskeleton reorganization. Eur. J. Cell Biol. 67, 336-345
    • (1995) Eur. J. Cell Biol. , vol.67 , pp. 336-345
    • Gaffet, P.1    Bettache, N.2    Bienvenüe, A.3
  • 34
    • 0033199115 scopus 로고    scopus 로고
    • Calpain functions in a caspase-independent manner to promote apoptosis-like events during platelet activation
    • Wolf, B. B., Goldstein, J. C., Stennicke, H. R., Beere, H., Amarante-Mendes, G. P., Salvesen, G. S., and Green, D. R. (1999) Calpain functions in a caspase-independent manner to promote apoptosis-like events during platelet activation. Blood 94, 1683-1692
    • (1999) Blood , vol.94 , pp. 1683-1692
    • Wolf, B.B.1    Goldstein, J.C.2    Stennicke, H.R.3    Beere, H.4    Amarante-Mendes, G.P.5    Salvesen, G.S.6    Green, D.R.7
  • 36
    • 45449083640 scopus 로고    scopus 로고
    • Living with death. The evolution of the mitochondrial pathway of apoptosis in animals
    • Oberst, A., Bender, C., and Green, D. R. (2008) Living with death. The evolution of the mitochondrial pathway of apoptosis in animals. Cell Death Differ. 15, 1139-1146
    • (2008) Cell Death Differ. , vol.15 , pp. 1139-1146
    • Oberst, A.1    Bender, C.2    Green, D.R.3
  • 37
    • 0032499784 scopus 로고    scopus 로고
    • Measurement of cytosolic, mitochondrial, and Golgi pH in single living cells with green fluorescent proteins
    • Llopis, J., McCaffery, J. M., Miyawaki, A., Farquhar, M. G., and Tsien, R. Y. (1998) Measurement of cytosolic, mitochondrial, and Golgi pH in single living cells with green fluorescent proteins. Proc. Natl. Acad. Sci. U.S.A. 95, 6803-6808
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 6803-6808
    • Llopis, J.1    McCaffery, J.M.2    Miyawaki, A.3    Farquhar, M.G.4    Tsien, R.Y.5
  • 38
    • 33645959522 scopus 로고    scopus 로고
    • Involvement of the Na/H exchanger in membrane phosphatidylserine exposure during human platelet activation
    • Bucki, R., Pastore, J. J., Giraud, F., Janmey, P. A., and Sulpice, J. C. (2006) Involvement of the Na/H exchanger in membrane phosphatidylserine exposure during human platelet activation. Biochim. Biophys. Acta 1761, 195-204
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 195-204
    • Bucki, R.1    Pastore, J.J.2    Giraud, F.3    Janmey, P.A.4    Sulpice, J.C.5
  • 39
    • 0035191089 scopus 로고    scopus 로고
    • The importance of Na/H exchanger for the generation of procoagulant activity by porcine blood platelets
    • Samson, J., Stelmach, H., and Tomasiak, M. (2001) The importance of Na/H exchanger for the generation of procoagulant activity by porcine blood platelets. Platelets 12, 436-442
    • (2001) Platelets , vol.12 , pp. 436-442
    • Samson, J.1    Stelmach, H.2    Tomasiak, M.3
  • 41
    • 77952688395 scopus 로고    scopus 로고
    • Plasminogen on the surfaces of fibrin clots prevents adhesion of leukocytes and platelets
    • Lishko, V. K., Yermolenko, I. S., and Ugarova, T. P. (2010) Plasminogen on the surfaces of fibrin clots prevents adhesion of leukocytes and platelets. J. Thromb. Haemost 8, 799-807
    • (2010) J. Thromb. Haemost , vol.8 , pp. 799-807
    • Lishko, V.K.1    Yermolenko, I.S.2    Ugarova, T.P.3
  • 42
    • 0036530015 scopus 로고    scopus 로고
    • A hereditary bleeding disorder of dogs caused by a lack of platelet procoagulant activity
    • Brooks, M. B., Catalfamo, J. L., Brown, H. A., Ivanova, P., and Lovaglio, J. (2002) A hereditary bleeding disorder of dogs caused by a lack of platelet procoagulant activity. Blood 99, 2434-2441
    • (2002) Blood , vol.99 , pp. 2434-2441
    • Brooks, M.B.1    Catalfamo, J.L.2    Brown, H.A.3    Ivanova, P.4    Lovaglio, J.5
  • 43
    • 84871860558 scopus 로고    scopus 로고
    • TMEM16F forms a Ca2-activated cation channel required for lipid scrambling in platelets during blood coagulation
    • Yang, H., Kim, A., David, T., Palmer, D., Jin, T., Tien, J., Huang, F., Cheng, T., Coughlin, S. R., Jan, Y. N., and Jan, L. Y. (2012) TMEM16F forms a Ca2-activated cation channel required for lipid scrambling in platelets during blood coagulation. Cell 151, 111-122
    • (2012) Cell , vol.151 , pp. 111-122
    • Yang, H.1    Kim, A.2    David, T.3    Palmer, D.4    Jin, T.5    Tien, J.6    Huang, F.7    Cheng, T.8    Coughlin, S.R.9    Jan, Y.N.10    Jan, L.Y.11
  • 44
    • 2942637935 scopus 로고    scopus 로고
    • Scott syndrome, a bleeding disorder caused by defective scrambling of membrane phospholipids
    • Zwaal, R. F., Comfurius, P., and Bevers, E. M. (2004) Scott syndrome, a bleeding disorder caused by defective scrambling of membrane phospholipids. Biochim. Biophys. Acta 1636, 119-128
    • (2004) Biochim. Biophys. Acta , vol.1636 , pp. 119-128
    • Zwaal, R.F.1    Comfurius, P.2    Bevers, E.M.3
  • 45
    • 34548080000 scopus 로고    scopus 로고
    • Scott syndrome dogs have impaired coated-platelet formation and calcein-release but normal mitochondrial depolarization
    • Brooks, M. B., Catalfamo, J. L., Friese, P., and Dale, G. L. (2007) Scott syndrome dogs have impaired coated-platelet formation and calcein-release but normal mitochondrial depolarization. J. Thromb. Haemost. 5, 1972-1974
    • (2007) J. Thromb. Haemost. , vol.5 , pp. 1972-1974
    • Brooks, M.B.1    Catalfamo, J.L.2    Friese, P.3    Dale, G.L.4
  • 46
    • 84876516813 scopus 로고    scopus 로고
    • Both TMEM16F-dependent and TMEM16F-independent pathways contribute to phosphatidylserine exposure in platelet apoptosis and platelet activation
    • van Kruchten, R., Mattheij, N. J., Saunders, C., Feijge, M. A., Swieringa, F., Wolfs, J. L., Collins, P. W., Heemskerk, J. W., and Bevers, E. M. (2013) Both TMEM16F-dependent and TMEM16F-independent pathways contribute to phosphatidylserine exposure in platelet apoptosis and platelet activation. Blood 121, 1850-1857
    • (2013) Blood , vol.121 , pp. 1850-1857
    • Van Kruchten, R.1    Mattheij, N.J.2    Saunders, C.3    Feijge, M.A.4    Swieringa, F.5    Wolfs, J.L.6    Collins, P.W.7    Heemskerk, J.W.8    Bevers, E.M.9
  • 47
    • 82255195322 scopus 로고    scopus 로고
    • Immunophilins and thrombotic disorders
    • Lopez, E., Rosado, J. A., and Redondo, P. C. (2011) Immunophilins and thrombotic disorders. Curr. Med. Chem. 18, 5414-5423
    • (2011) Curr. Med. Chem. , vol.18 , pp. 5414-5423
    • Lopez, E.1    Rosado, J.A.2    Redondo, P.C.3


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