메뉴 건너뛰기




Volumn 47, Issue 3, 2010, Pages 227-234

Apoptotic Processes in Megakaryocytes and Platelets

Author keywords

[No Author keywords available]

Indexed keywords

ANTINEOPLASTIC AGENT; APOPTOTIC PROTEASE ACTIVATING FACTOR 1; BCL2 RELATED PROTEIN A1; BIM PROTEIN; CASPASE 3; CASPASE 7; CASPASE 8; CASPASE 9; CISPLATIN; CYTARABINE; PROTEIN BAD; PROTEIN BAK; PROTEIN BAX; PROTEIN BCL 2; PROTEIN BCL W; PROTEIN BCL XL; PROTEIN BID; PROTEIN KINASE B; PROTEIN MCL 1; VINCRISTINE;

EID: 77953891657     PISSN: 00371963     EISSN: None     Source Type: Journal    
DOI: 10.1053/j.seminhematol.2010.03.006     Document Type: Article
Times cited : (37)

References (75)
  • 1
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan D., Weinberg R.A. The hallmarks of cancer. Cell 2000, 100:57-70.
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 2
    • 1042303659 scopus 로고    scopus 로고
    • Deranged removal of apoptotic cells: its role in the genesis of lupus
    • Dieker J.W., van der Vlag J., Berden J.H. Deranged removal of apoptotic cells: its role in the genesis of lupus. Nephrol Dial Transplant 2004, 19:282-285.
    • (2004) Nephrol Dial Transplant , vol.19 , pp. 282-285
    • Dieker, J.W.1    van der Vlag, J.2    Berden, J.H.3
  • 3
    • 65549098614 scopus 로고    scopus 로고
    • Apoptotic mechanisms after cerebral ischemia
    • Broughton B.R., Reutens D.C., Sobey C.G. Apoptotic mechanisms after cerebral ischemia. Stroke 2009, 40:e331-e339.
    • (2009) Stroke , vol.40
    • Broughton, B.R.1    Reutens, D.C.2    Sobey, C.G.3
  • 4
    • 62449157200 scopus 로고    scopus 로고
    • Role of apoptosis in cardiovascular disease
    • Lee Y., Gustafsson A.B. Role of apoptosis in cardiovascular disease. Apoptosis 2009, 14:536-548.
    • (2009) Apoptosis , vol.14 , pp. 536-548
    • Lee, Y.1    Gustafsson, A.B.2
  • 6
    • 37549048249 scopus 로고    scopus 로고
    • The BCL-2 protein family: opposing activities that mediate cell death
    • Youle R.J., Strasser A. The BCL-2 protein family: opposing activities that mediate cell death. Nat Rev Mol Cell Biol 2008, 9:47-59.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 47-59
    • Youle, R.J.1    Strasser, A.2
  • 7
    • 0034508217 scopus 로고    scopus 로고
    • The combined functions of proapoptotic Bcl-2 family members Bak and Bax are essential for normal development of multiple tissues
    • Lindsten T., Ross A.J., King A., et al. The combined functions of proapoptotic Bcl-2 family members Bak and Bax are essential for normal development of multiple tissues. Mol Cell 2000, 6:1389-1399.
    • (2000) Mol Cell , vol.6 , pp. 1389-1399
    • Lindsten, T.1    Ross, A.J.2    King, A.3
  • 8
    • 0035957653 scopus 로고    scopus 로고
    • Proapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and death
    • 292727-30
    • Wei M.C., Zong W.X., Cheng E.H., et al. Proapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and death. Science 2001, 292727-30.
    • (2001) Science
    • Wei, M.C.1    Zong, W.X.2    Cheng, E.H.3
  • 9
    • 43049105074 scopus 로고    scopus 로고
    • To trigger apoptosis, Bak exposes its BH3 domain and homodimerizes via BH3:groove interactions
    • Dewson G., Kratina T., Sim H.W., et al. To trigger apoptosis, Bak exposes its BH3 domain and homodimerizes via BH3:groove interactions. Molecular cell 2008, 30(3):369-380.
    • (2008) Molecular cell , vol.30 , Issue.3 , pp. 369-380
    • Dewson, G.1    Kratina, T.2    Sim, H.W.3
  • 10
    • 0037459081 scopus 로고    scopus 로고
    • Mitochondria: releasing power for life and unleashing the machineries of death
    • Newmeyer D.D., Ferguson-Miller S. Mitochondria: releasing power for life and unleashing the machineries of death. Cell 2003, 112:481-490.
    • (2003) Cell , vol.112 , pp. 481-490
    • Newmeyer, D.D.1    Ferguson-Miller, S.2
  • 11
    • 0032493870 scopus 로고    scopus 로고
    • Differential requirement for caspase 9 in apoptotic pathways in vivo
    • Hakem R., Hakem A., Duncan G.S., et al. Differential requirement for caspase 9 in apoptotic pathways in vivo. Cell 1998, 94:339-352.
    • (1998) Cell , vol.94 , pp. 339-352
    • Hakem, R.1    Hakem, A.2    Duncan, G.S.3
  • 12
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P.S., Nijhawan D., Budihardjo I., et al. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 1997, 91:479-489.
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.S.1    Nijhawan, D.2    Budihardjo, I.3
  • 13
    • 54549114986 scopus 로고    scopus 로고
    • BAX activation is initiated at a novel interaction site
    • Gavathiotis E., Suzuki M., Davis M.L., et al. BAX activation is initiated at a novel interaction site. Nature 2008, 455:1076-1081.
    • (2008) Nature , vol.455 , pp. 1076-1081
    • Gavathiotis, E.1    Suzuki, M.2    Davis, M.L.3
  • 14
    • 33846964621 scopus 로고    scopus 로고
    • Apoptosis initiated when BH3 ligands engage multiple Bcl-2 homologs, not Bax or Bak
    • Willis S.N., Fletcher J.I., Kaufmann T., et al. Apoptosis initiated when BH3 ligands engage multiple Bcl-2 homologs, not Bax or Bak. Science 2007, 315:856-859.
    • (2007) Science , vol.315 , pp. 856-859
    • Willis, S.N.1    Fletcher, J.I.2    Kaufmann, T.3
  • 15
    • 0027275490 scopus 로고
    • A novel domain within the 55 kd TNF receptor signals cell death
    • Tartaglia L.A., Ayres T.M., Wong G.H., Goeddel D.V. A novel domain within the 55 kd TNF receptor signals cell death. Cell 1993, 74:845-853.
    • (1993) Cell , vol.74 , pp. 845-853
    • Tartaglia, L.A.1    Ayres, T.M.2    Wong, G.H.3    Goeddel, D.V.4
  • 16
    • 0030011398 scopus 로고    scopus 로고
    • Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death
    • Boldin M.P., Goncharov T.M., Goltsev Y.V., Wallach D. Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death. Cell 1996, 85:803-815.
    • (1996) Cell , vol.85 , pp. 803-815
    • Boldin, M.P.1    Goncharov, T.M.2    Goltsev, Y.V.3    Wallach, D.4
  • 17
    • 15844412409 scopus 로고    scopus 로고
    • FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex
    • Muzio M., Chinnaiyan A.M., Kischkel F.C., et al. FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex. Cell 1996, 85:817-827.
    • (1996) Cell , vol.85 , pp. 817-827
    • Muzio, M.1    Chinnaiyan, A.M.2    Kischkel, F.C.3
  • 18
    • 0032817658 scopus 로고    scopus 로고
    • Increased activity of caspase 3 and caspase 8 in anti-Fas-induced apoptosis in lymphocytes from ageing humans
    • Aggarwal S., Gupta S. Increased activity of caspase 3 and caspase 8 in anti-Fas-induced apoptosis in lymphocytes from ageing humans. Clin Exp Immunol 1999, 117:285-290.
    • (1999) Clin Exp Immunol , vol.117 , pp. 285-290
    • Aggarwal, S.1    Gupta, S.2
  • 19
    • 0033534446 scopus 로고    scopus 로고
    • Caspase cleaved BID targets mitochondria and is required for cytochrome c release, while BCL-XL prevents this release but not tumor necrosis factor-R1/Fas death
    • Gross A., Yin X.M., Wang K., et al. Caspase cleaved BID targets mitochondria and is required for cytochrome c release, while BCL-XL prevents this release but not tumor necrosis factor-R1/Fas death. J Biol Chem 1999, 274:1156-1163.
    • (1999) J Biol Chem , vol.274 , pp. 1156-1163
    • Gross, A.1    Yin, X.M.2    Wang, K.3
  • 20
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • Li H., Zhu H., Xu C.J., Yuan J. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell 1998, 94:491-501.
    • (1998) Cell , vol.94 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.J.3    Yuan, J.4
  • 21
    • 0032555716 scopus 로고    scopus 로고
    • Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors
    • Luo X., Budihardjo I., Zou H., Slaughter C., Wang X. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell 1998, 94:481-490.
    • (1998) Cell , vol.94 , pp. 481-490
    • Luo, X.1    Budihardjo, I.2    Zou, H.3    Slaughter, C.4    Wang, X.5
  • 22
    • 0034663829 scopus 로고    scopus 로고
    • TBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c
    • Wei M.C., Lindsten T., Mootha V.K., et al. tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c. Genes Dev 2000, 14:2060-2071.
    • (2000) Genes Dev , vol.14 , pp. 2060-2071
    • Wei, M.C.1    Lindsten, T.2    Mootha, V.K.3
  • 23
    • 60549096096 scopus 로고    scopus 로고
    • Management of chemotherapy-induced thrombocytopenia: current status of thrombopoietic agents
    • Vadhan-Raj S. Management of chemotherapy-induced thrombocytopenia: current status of thrombopoietic agents. Semin Hematol 2009, 46(Suppl 2):S26-S32.
    • (2009) Semin Hematol , vol.46 , Issue.2 SUPPL
    • Vadhan-Raj, S.1
  • 24
    • 0035525733 scopus 로고    scopus 로고
    • Cellular stress response and apoptosis in cancer therapy
    • Herr I., Debatin K.M. Cellular stress response and apoptosis in cancer therapy. Blood 2001, 98:2603-2614.
    • (2001) Blood , vol.98 , pp. 2603-2614
    • Herr, I.1    Debatin, K.M.2
  • 25
    • 0023218341 scopus 로고
    • Mechanisms of thrombocytopenia in chronic autoimmune thrombocytopenic purpura. Evidence of both impaired platelet production and increased platelet clearance
    • Ballem P.J., Segal G.M., Stratton J.R., Gernsheimer T., Adamson J.W., Slichter S.J. Mechanisms of thrombocytopenia in chronic autoimmune thrombocytopenic purpura. Evidence of both impaired platelet production and increased platelet clearance. J Clin Invest 1987, 80:33-40.
    • (1987) J Clin Invest , vol.80 , pp. 33-40
    • Ballem, P.J.1    Segal, G.M.2    Stratton, J.R.3    Gernsheimer, T.4    Adamson, J.W.5    Slichter, S.J.6
  • 26
    • 0043245959 scopus 로고    scopus 로고
    • Immune thrombocytopenic purpura (ITP) plasma and purified ITP monoclonal autoantibodies inhibit megakaryocytopoiesis in vitro
    • Chang M., Nakagawa P.A., Williams S.A., et al. Immune thrombocytopenic purpura (ITP) plasma and purified ITP monoclonal autoantibodies inhibit megakaryocytopoiesis in vitro. Blood 2003, 102:887-895.
    • (2003) Blood , vol.102 , pp. 887-895
    • Chang, M.1    Nakagawa, P.A.2    Williams, S.A.3
  • 27
    • 0942287736 scopus 로고    scopus 로고
    • Ultrastructural study shows morphologic features of apoptosis and para-apoptosis in megakaryocytes from patients with idiopathic thrombocytopenic purpura
    • Houwerzijl E.J., Blom N.R., van der Want J.J., et al. Ultrastructural study shows morphologic features of apoptosis and para-apoptosis in megakaryocytes from patients with idiopathic thrombocytopenic purpura. Blood 2004, 103:500-506.
    • (2004) Blood , vol.103 , pp. 500-506
    • Houwerzijl, E.J.1    Blom, N.R.2    van der Want, J.J.3
  • 28
    • 13944266670 scopus 로고    scopus 로고
    • The effect of antiplatelet autoantibodies on megakaryocytopoiesis
    • McMillan R., Nugent D. The effect of antiplatelet autoantibodies on megakaryocytopoiesis. Int J Hematol 2005, 81:94-99.
    • (2005) Int J Hematol , vol.81 , pp. 94-99
    • McMillan, R.1    Nugent, D.2
  • 29
    • 0029986406 scopus 로고    scopus 로고
    • Impaired survival of bone marrow GPIIb/IIa+ megakaryocytic cells as an additional pathogenetic mechanism of HIV-1-related thrombocytopenia
    • Zauli G., Catani L., Gibellini D., et al. Impaired survival of bone marrow GPIIb/IIa+ megakaryocytic cells as an additional pathogenetic mechanism of HIV-1-related thrombocytopenia. Br J Haematol 1996, 92:711-717.
    • (1996) Br J Haematol , vol.92 , pp. 711-717
    • Zauli, G.1    Catani, L.2    Gibellini, D.3
  • 30
    • 0024344474 scopus 로고
    • Structural changes in the megakaryocytes of patients infected with the human immune deficiency virus (HIV-1)
    • Zucker-Franklin D., Termin C.S., Cooper M.C. Structural changes in the megakaryocytes of patients infected with the human immune deficiency virus (HIV-1). Am J Pathol 1989, 134:1295-1303.
    • (1989) Am J Pathol , vol.134 , pp. 1295-1303
    • Zucker-Franklin, D.1    Termin, C.S.2    Cooper, M.C.3
  • 31
    • 34250373620 scopus 로고    scopus 로고
    • Chemotherapy-induced thrombocytopenia derives from the selective death of megakaryocyte progenitors and can be rescued by stem cell factor
    • Zeuner A., Signore M., Martinetti D., Bartucci M., Peschle C., De Maria R. Chemotherapy-induced thrombocytopenia derives from the selective death of megakaryocyte progenitors and can be rescued by stem cell factor. Cancer Res 2007, 67:4767-4773.
    • (2007) Cancer Res , vol.67 , pp. 4767-4773
    • Zeuner, A.1    Signore, M.2    Martinetti, D.3    Bartucci, M.4    Peschle, C.5    De Maria, R.6
  • 32
    • 0034981504 scopus 로고    scopus 로고
    • Antiapoptotic protein Bcl-x(L) is up-regulated during megakaryocytic differentiation of CD34(+) progenitors but is absent from senescent megakaryocytes
    • Sanz C., Benet I., Richard C., et al. Antiapoptotic protein Bcl-x(L) is up-regulated during megakaryocytic differentiation of CD34(+) progenitors but is absent from senescent megakaryocytes. Exp Hematol 2001, 29:728-735.
    • (2001) Exp Hematol , vol.29 , pp. 728-735
    • Sanz, C.1    Benet, I.2    Richard, C.3
  • 33
    • 34250183122 scopus 로고    scopus 로고
    • Continuous expression of Bcl-xL protein during megakaryopoiesis is post-translationally regulated by thrombopoietin-mediated Akt activation, which prevents the cleavage of Bcl-xL
    • Kozuma Y., Kojima H., Yuki S., Suzuki H., Nagasawa T. Continuous expression of Bcl-xL protein during megakaryopoiesis is post-translationally regulated by thrombopoietin-mediated Akt activation, which prevents the cleavage of Bcl-xL. J Thromb Haemost 2007, 5:1274-1282.
    • (2007) J Thromb Haemost , vol.5 , pp. 1274-1282
    • Kozuma, Y.1    Kojima, H.2    Yuki, S.3    Suzuki, H.4    Nagasawa, T.5
  • 34
    • 40549087266 scopus 로고    scopus 로고
    • PI3K/Akt/FOXO3a pathway contributes to thrombopoietin-induced proliferation of primary megakaryocytes in vitro and in vivo via modulation of p27(Kip1)
    • Nakao T., Geddis A.E., Fox N.E., Kaushansky K. PI3K/Akt/FOXO3a pathway contributes to thrombopoietin-induced proliferation of primary megakaryocytes in vitro and in vivo via modulation of p27(Kip1). Cell Cycle 2008, 7:257-266.
    • (2008) Cell Cycle , vol.7 , pp. 257-266
    • Nakao, T.1    Geddis, A.E.2    Fox, N.E.3    Kaushansky, K.4
  • 35
    • 0033635616 scopus 로고    scopus 로고
    • Conditional deletion of the Bcl-x gene from erythroid cells results in hemolytic anemia and profound splenomegaly
    • Wagner K.U., Claudio E., Rucker E.B., et al. Conditional deletion of the Bcl-x gene from erythroid cells results in hemolytic anemia and profound splenomegaly. Development 2000, 127:4949-4958.
    • (2000) Development , vol.127 , pp. 4949-4958
    • Wagner, K.U.1    Claudio, E.2    Rucker, E.B.3
  • 36
    • 70350070333 scopus 로고    scopus 로고
    • Mcl-1 and Bcl-xL cooperatively maintain integrity of hepatocytes in developing and adult murine liver
    • Hikita H., Takehara T., Shimizu S., et al. Mcl-1 and Bcl-xL cooperatively maintain integrity of hepatocytes in developing and adult murine liver. Hepatology 2009, 50:1217-1226.
    • (2009) Hepatology , vol.50 , pp. 1217-1226
    • Hikita, H.1    Takehara, T.2    Shimizu, S.3
  • 37
    • 20444486559 scopus 로고    scopus 로고
    • An inhibitor of Bcl-2 family proteins induces regression of solid tumours
    • Oltersdorf T., Elmore S., Shoemaker A., et al. An inhibitor of Bcl-2 family proteins induces regression of solid tumours. Nature 2005, 435:677-681.
    • (2005) Nature , vol.435 , pp. 677-681
    • Oltersdorf, T.1    Elmore, S.2    Shoemaker, A.3
  • 38
    • 44849112219 scopus 로고    scopus 로고
    • ABT-263: a potent and orally bioavailable Bcl-2 family inhibitor
    • Tse C., Shoemaker A.R., Adickes J., et al. ABT-263: a potent and orally bioavailable Bcl-2 family inhibitor. Cancer Res 2008, 68:3421-3428.
    • (2008) Cancer Res , vol.68 , pp. 3421-3428
    • Tse, C.1    Shoemaker, A.R.2    Adickes, J.3
  • 39
    • 0030801895 scopus 로고    scopus 로고
    • In vitro senescence and apoptotic cell death of human megakaryocytes
    • Zauli G., Vitale M., Falcieri E., et al. In vitro senescence and apoptotic cell death of human megakaryocytes. Blood 1997, 90:2234-2243.
    • (1997) Blood , vol.90 , pp. 2234-2243
    • Zauli, G.1    Vitale, M.2    Falcieri, E.3
  • 40
    • 0033986362 scopus 로고    scopus 로고
    • Ultrastructural characterization of maturation, platelet release, and senescence of human cultured megakaryocytes
    • Falcieri E., Bassini A., Pierpaoli S., et al. Ultrastructural characterization of maturation, platelet release, and senescence of human cultured megakaryocytes. Anat Rec 2000, 258:90-99.
    • (2000) Anat Rec , vol.258 , pp. 90-99
    • Falcieri, E.1    Bassini, A.2    Pierpaoli, S.3
  • 41
    • 0033607506 scopus 로고    scopus 로고
    • Proapoptotic Bcl-2 relative Bim required for certain apoptotic responses, leukocyte homeostasis, and to preclude autoimmunity
    • Bouillet P., Metcalf D., Huang D.C., et al. Proapoptotic Bcl-2 relative Bim required for certain apoptotic responses, leukocyte homeostasis, and to preclude autoimmunity. Science 1999, 286:1735-1738.
    • (1999) Science , vol.286 , pp. 1735-1738
    • Bouillet, P.1    Metcalf, D.2    Huang, D.C.3
  • 42
    • 0033593038 scopus 로고    scopus 로고
    • Constitutive Bcl-2 expression throughout the hematopoietic compartment affects multiple lineages and enhances progenitor cell survival
    • Ogilvy S., Metcalf D., Print C.G., Bath M.L., Harris A.W., Adams J.M. Constitutive Bcl-2 expression throughout the hematopoietic compartment affects multiple lineages and enhances progenitor cell survival. Proc Natl Acad Sci U S A 1999, 96:14943-14948.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 14943-14948
    • Ogilvy, S.1    Metcalf, D.2    Print, C.G.3    Bath, M.L.4    Harris, A.W.5    Adams, J.M.6
  • 43
    • 0036721472 scopus 로고    scopus 로고
    • BclxL overexpression in megakaryocytes leads to impaired platelet fragmentation
    • Kaluzhny Y., Yu G., Sun S., et al. BclxL overexpression in megakaryocytes leads to impaired platelet fragmentation. Blood 2002, 100:1670-1678.
    • (2002) Blood , vol.100 , pp. 1670-1678
    • Kaluzhny, Y.1    Yu, G.2    Sun, S.3
  • 44
    • 0037103295 scopus 로고    scopus 로고
    • Platelet formation is the consequence of caspase activation within megakaryocytes
    • De Botton S., Sabri S., Daugas E., et al. Platelet formation is the consequence of caspase activation within megakaryocytes. Blood 2002, 100:1310-1317.
    • (2002) Blood , vol.100 , pp. 1310-1317
    • De Botton, S.1    Sabri, S.2    Daugas, E.3
  • 45
    • 0037450786 scopus 로고    scopus 로고
    • Compartmentalized megakaryocyte death generates functional platelets committed to caspase-independent death
    • Clarke M.C., Savill J., Jones D.B., Noble B.S., Brown S.B. Compartmentalized megakaryocyte death generates functional platelets committed to caspase-independent death. J Cell Biol 2003, 160:577-587.
    • (2003) J Cell Biol , vol.160 , pp. 577-587
    • Clarke, M.C.1    Savill, J.2    Jones, D.B.3    Noble, B.S.4    Brown, S.B.5
  • 48
    • 67349153739 scopus 로고    scopus 로고
    • Caspase activation is involved in early megakaryocyte differentiation but not in platelet production from megakaryocytes
    • Kozuma Y., Yuki S., Ninomiya H., Nagasawa T., Kojima H. Caspase activation is involved in early megakaryocyte differentiation but not in platelet production from megakaryocytes. Leukemia 2009, 23:1080-1086.
    • (2009) Leukemia , vol.23 , pp. 1080-1086
    • Kozuma, Y.1    Yuki, S.2    Ninomiya, H.3    Nagasawa, T.4    Kojima, H.5
  • 49
    • 41349097770 scopus 로고    scopus 로고
    • A mutation of human cytochrome c enhances the intrinsic apoptotic pathway but causes only thrombocytopenia
    • Morison I.M., Borde E.M., Cheesman E.J., et al. A mutation of human cytochrome c enhances the intrinsic apoptotic pathway but causes only thrombocytopenia. Nat Genet 2008, 40:387-389.
    • (2008) Nat Genet , vol.40 , pp. 387-389
    • Morison, I.M.1    Borde, E.M.2    Cheesman, E.J.3
  • 50
    • 0010980106 scopus 로고
    • Determination of the life of human blood platelets using labelled diisopropylfluorophosphanate
    • Leeksma C.H., Cohen J.A. Determination of the life of human blood platelets using labelled diisopropylfluorophosphanate. Nature 1955, 175:552-553.
    • (1955) Nature , vol.175 , pp. 552-553
    • Leeksma, C.H.1    Cohen, J.A.2
  • 51
    • 0029127976 scopus 로고
    • In vivo biotinylation demonstrates that reticulated platelets are the youngest platelets in circulation
    • Ault K.A., Knowles C. In vivo biotinylation demonstrates that reticulated platelets are the youngest platelets in circulation. Exp Hematol 1995, 23:996-1001.
    • (1995) Exp Hematol , vol.23 , pp. 996-1001
    • Ault, K.A.1    Knowles, C.2
  • 52
    • 0031457994 scopus 로고    scopus 로고
    • Alterations in Bcl-2/Bax protein levels in platelets form part of an ionomycin-induced process that resembles apoptosis
    • Vanags D.M., Orrenius S., Aguilar-Santelises M. Alterations in Bcl-2/Bax protein levels in platelets form part of an ionomycin-induced process that resembles apoptosis. Br J Haematol 1997, 99:824-831.
    • (1997) Br J Haematol , vol.99 , pp. 824-831
    • Vanags, D.M.1    Orrenius, S.2    Aguilar-Santelises, M.3
  • 53
    • 33947227522 scopus 로고    scopus 로고
    • Programmed anuclear cell death delimits platelet life span
    • Mason K.D., Carpinelli M.R., Fletcher J.I., et al. Programmed anuclear cell death delimits platelet life span. Cell 2007, 128:1173-1186.
    • (2007) Cell , vol.128 , pp. 1173-1186
    • Mason, K.D.1    Carpinelli, M.R.2    Fletcher, J.I.3
  • 54
    • 33947223337 scopus 로고    scopus 로고
    • Bcl-2 family proteins are essential for platelet survival
    • Zhang H., Nimmer P.M., Tahir S.K., et al. Bcl-2 family proteins are essential for platelet survival. Cell Death Differ 2007, 14:943-951.
    • (2007) Cell Death Differ , vol.14 , pp. 943-951
    • Zhang, H.1    Nimmer, P.M.2    Tahir, S.K.3
  • 56
    • 0038646211 scopus 로고    scopus 로고
    • Apoptotic markers are increased in platelets stored at 37 degrees C
    • Bertino A.M., Qi X.Q., Li J., Xia Y., Kuter D.J. Apoptotic markers are increased in platelets stored at 37 degrees C. Transfusion 2003, 43:857-866.
    • (2003) Transfusion , vol.43 , pp. 857-866
    • Bertino, A.M.1    Qi, X.Q.2    Li, J.3    Xia, Y.4    Kuter, D.J.5
  • 57
    • 0034104294 scopus 로고    scopus 로고
    • Constitutive death of platelets leading to scavenger receptor-mediated phagocytosis. A caspase-independent cell clearance program
    • Brown S.B., Clarke M.C., Magowan L., Sanderson H., Savill J. Constitutive death of platelets leading to scavenger receptor-mediated phagocytosis. A caspase-independent cell clearance program. J Biol Chem 2000, 275:5987-5996.
    • (2000) J Biol Chem , vol.275 , pp. 5987-5996
    • Brown, S.B.1    Clarke, M.C.2    Magowan, L.3    Sanderson, H.4    Savill, J.5
  • 58
    • 0037410195 scopus 로고    scopus 로고
    • Platelet apoptosis in stored platelet concentrates and other models
    • Leytin V., Freedman J. Platelet apoptosis in stored platelet concentrates and other models. Transfus Apher Sci 2003, 28:285-295.
    • (2003) Transfus Apher Sci , vol.28 , pp. 285-295
    • Leytin, V.1    Freedman, J.2
  • 59
    • 0033725182 scopus 로고    scopus 로고
    • The mechanism of apoptosis in human platelets during storage
    • Li J., Xia Y., Bertino A.M., Coburn J.P., Kuter D.J. The mechanism of apoptosis in human platelets during storage. Transfusion 2000, 40:1320-1329.
    • (2000) Transfusion , vol.40 , pp. 1320-1329
    • Li, J.1    Xia, Y.2    Bertino, A.M.3    Coburn, J.P.4    Kuter, D.J.5
  • 60
  • 61
    • 0034777852 scopus 로고    scopus 로고
    • Early increase in DcR2 expression and late activation of caspases in the platelet storage lesion
    • Plenchette S., Moutet M., Benguella M., et al. Early increase in DcR2 expression and late activation of caspases in the platelet storage lesion. Leukemia 2001, 15:1572-1581.
    • (2001) Leukemia , vol.15 , pp. 1572-1581
    • Plenchette, S.1    Moutet, M.2    Benguella, M.3
  • 62
    • 0033564368 scopus 로고    scopus 로고
    • Role of caspase in a subset of human platelet activation responses
    • Shcherbina A., Remold-O'Donnell E. Role of caspase in a subset of human platelet activation responses. Blood 1999, 93:4222-4231.
    • (1999) Blood , vol.93 , pp. 4222-4231
    • Shcherbina, A.1    Remold-O'Donnell, E.2
  • 63
    • 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., et al. Calpain functions in a caspase-independent manner to promote apoptosis-like events during platelet activation. Blood 1999, 94:1683-1692.
    • (1999) Blood , vol.94 , pp. 1683-1692
    • Wolf, B.B.1    Goldstein, J.C.2    Stennicke, H.R.3
  • 64
    • 67649541305 scopus 로고    scopus 로고
    • Two distinct pathways regulate platelet phosphatidylserine exposure and procoagulant function
    • Schoenwaelder S.M., Yuan Y., Josefsson E.C., et al. Two distinct pathways regulate platelet phosphatidylserine exposure and procoagulant function. Blood 2009, 114:663-666.
    • (2009) Blood , vol.114 , pp. 663-666
    • Schoenwaelder, S.M.1    Yuan, Y.2    Josefsson, E.C.3
  • 65
    • 32444434664 scopus 로고    scopus 로고
    • Caspases 3 and 7: key mediators of mitochondrial events of apoptosis
    • Lakhani S.A., Masud A., Kuida K., et al. Caspases 3 and 7: key mediators of mitochondrial events of apoptosis. Science 2006, 311:847-851.
    • (2006) Science , vol.311 , pp. 847-851
    • Lakhani, S.A.1    Masud, A.2    Kuida, K.3
  • 66
    • 3042687605 scopus 로고    scopus 로고
    • Apaf-1 and caspase-9 accelerate apoptosis, but do not determine whether factor-deprived or drug-treated cells die
    • Ekert P.G., Read S.H., Silke J., et al. Apaf-1 and caspase-9 accelerate apoptosis, but do not determine whether factor-deprived or drug-treated cells die. J Cell Biol 2004, 165:835-842.
    • (2004) J Cell Biol , vol.165 , pp. 835-842
    • Ekert, P.G.1    Read, S.H.2    Silke, J.3
  • 67
    • 33344456332 scopus 로고    scopus 로고
    • Apaf-1 and caspase-9 are required for cytokine withdrawal-induced apoptosis of mast cells but dispensable for their functional and clonogenic death
    • Marsden V.S., Kaufmann T., O'Reilly L.A., Adams J.M., Strasser A. Apaf-1 and caspase-9 are required for cytokine withdrawal-induced apoptosis of mast cells but dispensable for their functional and clonogenic death. Blood 2006, 107:1872-1877.
    • (2006) Blood , vol.107 , pp. 1872-1877
    • Marsden, V.S.1    Kaufmann, T.2    O'Reilly, L.A.3    Adams, J.M.4    Strasser, A.5
  • 68
    • 0345688868 scopus 로고    scopus 로고
    • Metalloproteinase inhibitors improve the recovery and hemostatic function of in vitro-aged or -injured mouse platelets
    • Bergmeier W., Burger P.C., Piffath C.L., et al. Metalloproteinase inhibitors improve the recovery and hemostatic function of in vitro-aged or -injured mouse platelets. Blood 2003, 102:4229-4235.
    • (2003) Blood , vol.102 , pp. 4229-4235
    • Bergmeier, W.1    Burger, P.C.2    Piffath, C.L.3
  • 69
    • 0021047734 scopus 로고
    • Changes in membrane phospholipid distribution during platelet activation
    • Bevers E.M., Comfurius P., Zwaal R.F. Changes in membrane phospholipid distribution during platelet activation. Biochim Biophys Acta 1983, 736:57-66.
    • (1983) Biochim Biophys Acta , vol.736 , pp. 57-66
    • Bevers, E.M.1    Comfurius, P.2    Zwaal, R.F.3
  • 71
    • 38949218420 scopus 로고    scopus 로고
    • Critical role for the mitochondrial permeability transition pore and cyclophilin D in platelet activation and thrombosis
    • Jobe S.M., Wilson K.M., Leo L., et al. Critical role for the mitochondrial permeability transition pore and cyclophilin D in platelet activation and thrombosis. Blood 2008, 111:1257-1265.
    • (2008) Blood , vol.111 , pp. 1257-1265
    • Jobe, S.M.1    Wilson, K.M.2    Leo, L.3
  • 72
    • 73949144549 scopus 로고    scopus 로고
    • Rapid procoagulant phosphatidylserine exposure relies on high cytosolic calcium rather than on mitochondrial depolarization
    • Arachiche A., Kerbiriou-Nabias D., Garcin I., Letellier T., Dachary-Prigent J. Rapid procoagulant phosphatidylserine exposure relies on high cytosolic calcium rather than on mitochondrial depolarization. Arterioscler Thromb Vasc Biol 2009, 29:1883-1889.
    • (2009) Arterioscler Thromb Vasc Biol , vol.29 , pp. 1883-1889
    • Arachiche, A.1    Kerbiriou-Nabias, D.2    Garcin, I.3    Letellier, T.4    Dachary-Prigent, J.5
  • 74
    • 67650230871 scopus 로고    scopus 로고
    • Mitochondrial clearance is regulated by Atg7-dependent and -independent mechanisms during reticulocyte maturation
    • Zhang J., Randall M.S., Loyd M.R., et al. Mitochondrial clearance is regulated by Atg7-dependent and -independent mechanisms during reticulocyte maturation. Blood 2009, 114:157-164.
    • (2009) Blood , vol.114 , pp. 157-164
    • Zhang, J.1    Randall, M.S.2    Loyd, M.R.3
  • 75
    • 33750353416 scopus 로고    scopus 로고
    • Megakaryocytic dysfunction in myelodysplastic syndromes and idiopathic thrombocytopenic purpura is in part due to different forms of cell death
    • Houwerzijl E.J., Blom N.R., van der Want J.J., Vellenga E., de Wolf J.T. Megakaryocytic dysfunction in myelodysplastic syndromes and idiopathic thrombocytopenic purpura is in part due to different forms of cell death. Leukemia 2006, 20:1937-1942.
    • (2006) Leukemia , vol.20 , pp. 1937-1942
    • Houwerzijl, E.J.1    Blom, N.R.2    van der Want, J.J.3    Vellenga, E.4    de Wolf, J.T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.