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Volumn 118, Issue 2, 2011, Pages 416-424

Protein kinase C mediates platelet secretion and thrombus formation through protein kinase D2

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA GRANULE PROTEIN; INTEGRIN ALPHA2BBETA3; MEMBRANE PROTEIN; PROTEIN KINASE C; PROTEIN KINASE D; PROTEIN KINASE D2; UNCLASSIFIED DRUG; VERY LATE ACTIVATION ANTIGEN 2;

EID: 79960504480     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2010-10-312199     Document Type: Article
Times cited : (44)

References (42)
  • 1
    • 75949128633 scopus 로고    scopus 로고
    • Antiplatelet therapies for the treatment of cardiovascular disease
    • Michelson AD. Antiplatelet therapies for the treatment of cardiovascular disease. Nat Rev Drug Discov. 2010;9(2):154-69.
    • (2010) Nat Rev Drug Discov , vol.9 , Issue.2 , pp. 154-169
    • Michelson, A.D.1
  • 2
    • 61749097572 scopus 로고    scopus 로고
    • PKCalpha regulates platelet granule secretion and thrombus formation in mice
    • Konopatskaya O, Gilio K, Harper MT, et al. PKCalpha regulates platelet granule secretion and thrombus formation in mice. J Clin Invest. 2009;119(2):399-407.
    • (2009) J Clin Invest , vol.119 , Issue.2 , pp. 399-407
    • Konopatskaya, O.1    Gilio, K.2    Harper, M.T.3
  • 4
    • 33645990604 scopus 로고    scopus 로고
    • A role for PKCtheta in outside-in alpha(IIb)beta3 signaling
    • Soriani A, Moran B, de Virgilio M, et al. A role for PKCtheta in outside-in alpha(IIb)beta3 signaling. J Thromb Haemost. 2006;4(3):648-655.
    • (2006) J Thromb Haemost , vol.4 , Issue.3 , pp. 648-655
    • Soriani, A.1    Moran, B.2    De Virgilio, M.3
  • 5
    • 65549123690 scopus 로고    scopus 로고
    • Protein kinase Cδ differentially regulates platelet functional responses
    • Chari R, Getz T, Nagy B Jr, et al. Protein kinase Cδ differentially regulates platelet functional responses. Arterioscler Thromb Vasc Biol. 2009;29(5):699-705.
    • (2009) Arterioscler Thromb Vasc Biol , vol.29 , Issue.5 , pp. 699-705
    • Chari, R.1    Getz, T.2    Nagy Jr., B.3
  • 6
    • 63849163448 scopus 로고    scopus 로고
    • Impaired activation of platelets lacking protein kinase C-theta isoform
    • Nagy B Jr., Bhavaraju K, Getz T, Bynagari YS, Kim S, Kunapuli SP. Impaired activation of platelets lacking protein kinase C-theta isoform. Blood. 2009;113(11):2557-2567.
    • (2009) Blood , vol.113 , Issue.11 , pp. 2557-2567
    • Nagy Jr., B.1    Bhavaraju, K.2    Getz, T.3    Bynagari, Y.S.4    Kim, S.5    Kunapuli, S.P.6
  • 7
    • 77954945985 scopus 로고    scopus 로고
    • Functional divergence of platelet protein kinase C (PKC) isoforms in thrombus formation on collagen
    • Gilio K, Harper MT, Cosemans JM, et al. Functional divergence of platelet protein kinase C (PKC) isoforms in thrombus formation on collagen. J Biol Chem. 2010;285(30):23410-23419.
    • (2010) J Biol Chem , vol.285 , Issue.30 , pp. 23410-23419
    • Gilio, K.1    Harper, M.T.2    Cosemans, J.M.3
  • 8
    • 33744926666 scopus 로고    scopus 로고
    • PKD at the crossroads of DAG and PKC signaling
    • DOI 10.1016/j.tips.2006.04.003, PII S0165614706001040
    • Wang QJ. PKD at the crossroads of DAG and PKC signaling. Trends Pharmacol Sci. 2006;27(6):317-323. (Pubitemid 43850003)
    • (2006) Trends in Pharmacological Sciences , vol.27 , Issue.6 , pp. 317-323
    • Wang, Q.J.1
  • 10
    • 45149095520 scopus 로고    scopus 로고
    • Sequential protein kinase C (PKC)-dependent and PKC-independent protein kinase D catalytic activation via Gq-coupled receptors: Differential regulation of activation loop Ser(744) and Ser(748) phosphorylation
    • Jacamo R, Sinnett-Smith J, Rey O, Waldron RT, Rozengurt E. Sequential protein kinase C (PKC)-dependent and PKC-independent protein kinase D catalytic activation via Gq-coupled receptors: differential regulation of activation loop Ser(744) and Ser(748) phosphorylation. J Biol Chem. 2008;283(19):12877-12887.
    • (2008) J Biol Chem , vol.283 , Issue.19 , pp. 12877-12887
    • Jacamo, R.1    Sinnett-Smith, J.2    Rey, O.3    Waldron, R.T.4    Rozengurt, E.5
  • 12
    • 36148990584 scopus 로고    scopus 로고
    • Angiotensin II directly triggers endothelial exocytosis via protein kinase C-dependent protein kinase D2 activation
    • DOI 10.1254/jphs.FP0070858
    • Ge X, Low B, Liang M, Fu J. Angiotensin II directly triggers endothelial exocytosis via protein kinase C-dependent protein kinase D2 activation. J Pharmacol Sci. 2007;105(2):168-176. (Pubitemid 350106806)
    • (2007) Journal of Pharmacological Sciences , vol.105 , Issue.2 , pp. 168-176
    • Ge, X.1    Low, B.2    Liang, M.3    Fu, J.4
  • 13
    • 0037441763 scopus 로고    scopus 로고
    • PKD: A new protein kinase C-dependent pathway in platelets
    • DOI 10.1182/blood-2002-08-2384
    • Stafford MJ, Watson SP, Pears CJPKD: a new protein kinase C-dependent pathway in platelets. Blood. 2003;101(4):1392-1399. (Pubitemid 36182511)
    • (2003) Blood , vol.101 , Issue.4 , pp. 1392-1399
    • Stafford, M.J.1    Watson, S.P.2    Pears, C.J.3
  • 14
    • 66549084876 scopus 로고    scopus 로고
    • HaemAtlas: Characterizing gene expression in differentiated human blood cells
    • Watkins NA et al. HaemAtlas: characterizing gene expression in differentiated human blood cells. Blood. 2009;113(19):e1-9.
    • (2009) Blood , vol.113 , Issue.19
    • Watkins, N.A.1
  • 15
    • 33845512493 scopus 로고    scopus 로고
    • PKCdelta regulates collagen-induced platelet aggregation through inhibition of VASP-mediated filopodia formation
    • DOI 10.1182/blood-2006-05-023739
    • Pula G, Schuh K, Nakayama K, Nakayama KI, Walter U, Poole A. WPKCdelta regulates collagen-induced platelet aggregation through inhibition of VASP-mediated filopodia formation. Blood. 2006;108(13):4035-4044. (Pubitemid 44913272)
    • (2006) Blood , vol.108 , Issue.13 , pp. 4035-4044
    • Pula, G.1    Schuh, K.2    Nakayama, K.3    Nakayama, K.I.4    Walter, U.5    Poole, A.W.6
  • 16
    • 0037389469 scopus 로고    scopus 로고
    • Complementary roles of glycoprotein VI and alpha2beta1 integrin in collagen-induced thrombus formation in flowing whole blood ex vivo
    • Kuijpers MJE, Schulte V, Bergmeier W, et al. Complementary roles of glycoprotein VI and alpha2beta1 integrin in collagen-induced thrombus formation in flowing whole blood ex vivo. FASEB J. 2003;17(6):685-687.
    • (2003) FASEB J , vol.17 , Issue.6 , pp. 685-687
    • Kuijpers, M.J.E.1    Schulte, V.2    Bergmeier, W.3
  • 17
    • 68049086486 scopus 로고    scopus 로고
    • Protein kinase C{alpha}, but not PKC{beta} or PKC{gamma}, regulates contractility and heart failure susceptibility: Implications for ruboxistaurin as a novel therapeutic approach
    • Liu Q, Chen X, Macdonnell SM, et al. Protein kinase C{alpha}, but not PKC{beta} or PKC{gamma}, regulates contractility and heart failure susceptibility: implications for ruboxistaurin as a novel therapeutic approach. Circ Res. 2009;105(2):194-200.
    • (2009) Circ Res , vol.105 , Issue.2 , pp. 194-200
    • Liu, Q.1    Chen, X.2    Macdonnell, S.M.3
  • 18
    • 77949279691 scopus 로고    scopus 로고
    • Diverse functions of protein kinase C isoforms in platelet activation and thrombus formation
    • Harper MT, Poole AW. Diverse functions of protein kinase C isoforms in platelet activation and thrombus formation. J Thromb Haemost. 2010;8(3):454-462.
    • (2010) J Thromb Haemost , vol.8 , Issue.3 , pp. 454-462
    • Harper, M.T.1    Poole, A.W.2
  • 19
    • 0029964752 scopus 로고    scopus 로고
    • Protein kinase D (PKD) activation in intact cells through a protein kinase C-dependent signal transduction pathway
    • Zugaza JL, Sinnett-Smith J, Van Lint J, Rozengurt E. Protein kinase D (PKD) activation in intact cells through a protein kinase C-dependent signal transduction pathway. EMBO J. 1996;15(22):6220-6230. (Pubitemid 26397895)
    • (1996) EMBO Journal , vol.15 , Issue.22 , pp. 6220-6230
    • Zugaza, J.L.1    Sinnett-Smith, J.2    Van Lint, J.3    Rozengurt, E.4
  • 20
    • 0030771317 scopus 로고    scopus 로고
    • Bombesin, vasopressin, endothelin, bradykinin, and platelet-derived growth factor rapidly activate protein kinase D through a protein kinase C- dependent signal transduction pathway
    • DOI 10.1074/jbc.272.38.23952
    • Zugaza JL, Waldron RT, Sinnett-Smith J, Rozengurt E. Bombesin, vasopressin, endothelin, bradykinin, and platelet-derived growth factor rapidly activate protein kinase D through a protein kinase C-dependent signal transduction pathway. J Biol Chem. 1997;272(38):23952-23960. (Pubitemid 27410978)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.38 , pp. 23952-23960
    • Zugaza, J.L.1    Waldron, R.T.2    Sinnett-Smith, J.3    Rozengurt, E.4
  • 21
    • 65649128229 scopus 로고    scopus 로고
    • Vascular endothelial growth factor induces protein kinase D-dependent production of proinflammatory cytokines in endothelial cells
    • Hao Q,Wang L, Tang H. Vascular endothelial growth factor induces protein kinase D-dependent production of proinflammatory cytokines in endothelial cells. Am J Physiol Cell Physiol. 2009;296(4):C821-C827.
    • (2009) Am J Physiol Cell Physiol , vol.296 , Issue.4
    • Hao, Q.1    Wang, L.2    Tang, H.3
  • 22
    • 25844484590 scopus 로고    scopus 로고
    • Protein kinase C-dependent protein kinase D activation modulates ERK signal pathway and endothelial cell proliferation by vascular endothelial growth factor
    • DOI 10.1074/jbc.M503198200
    • Wong C, Jin ZG. Protein kinase C-dependent protein kinase D activation modulates ERK signal pathway and endothelial cell proliferation by vascular endothelial growth factor. J Biol Chem. 2005;280(39):33262-33269. (Pubitemid 41397122)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.39 , pp. 33262-33269
    • Wong, C.1    Jin, Z.-G.2
  • 24
    • 77951771770 scopus 로고    scopus 로고
    • Novel protein kinase D inhibitors cause potent arrest in prostate cancer cell growth and motility
    • Lavalle CR, Bravo-Altamirano K, Giridhar KV, et al. Novel protein kinase D inhibitors cause potent arrest in prostate cancer cell growth and motility. BMC Chem Biol. 2010;10:5.
    • (2010) BMC Chem Biol , vol.10 , pp. 5
    • Lavalle, C.R.1    Bravo-Altamirano, K.2    Giridhar, K.V.3
  • 25
    • 57749100261 scopus 로고    scopus 로고
    • Potent and selective disruption of protein kinase D functionality by a benzoxoloazepinolone
    • Sharlow ER, Giridhar KV, LaValle CR, et al. Potent and selective disruption of protein kinase D functionality by a benzoxoloazepinolone. J Biol Chem. 2008;283(48):33516-33526.
    • (2008) J Biol Chem , vol.283 , Issue.48 , pp. 33516-33526
    • Sharlow, E.R.1    Giridhar, K.V.2    LaValle, C.R.3
  • 26
    • 73149089479 scopus 로고    scopus 로고
    • CID755673 enhances mitogenic signaling by phorbol esters, bombesin and EGF through a protein kinase D-independent pathway
    • Torres-Marquez E, Sinnett-Smith J, Guha S, et al. CID755673 enhances mitogenic signaling by phorbol esters, bombesin and EGF through a protein kinase D-independent pathway. Biochem Biophys Res Commun. 2010;391(1):63-68.
    • (2010) Biochem Biophys Res Commun , vol.391 , Issue.1 , pp. 63-68
    • Torres-Marquez, E.1    Sinnett-Smith, J.2    Guha, S.3
  • 27
    • 74249106877 scopus 로고    scopus 로고
    • A novel kinase inhibitor establishes a predominant role for protein kinase D as a cardiac class IIa histone deacetylase kinase
    • Monovich L, Vega RB, Meredith E, et al. A novel kinase inhibitor establishes a predominant role for protein kinase D as a cardiac class IIa histone deacetylase kinase. FEBS Lett. 2010;584(3):631-637.
    • (2010) FEBS Lett , vol.584 , Issue.3 , pp. 631-637
    • Monovich, L.1    Vega, R.B.2    Meredith, E.3
  • 28
    • 0035830496 scopus 로고    scopus 로고
    • Protein Kinase D regulates the fission of cell surface destined transport carriers from the trans-Golgi network
    • DOI 10.1016/S0092-8674(01)00228-8
    • Liljedahl M, Maeda Y, Colanzi A,Ayala I, Van Lint J, Malhotra V. Protein kinase D regulates the fission of cell surface destined transport carriers from the trans-Golgi network. Cell. 2001;104(3):409-420. (Pubitemid 32206461)
    • (2001) Cell , vol.104 , Issue.3 , pp. 409-420
    • Liljedahl, M.1    Maeda, Y.2    Colanzi, A.3    Ayala, I.4    Van Lint, J.5    Malhotra, V.6
  • 29
    • 58249087541 scopus 로고    scopus 로고
    • Regulation of PKD by the MAPK p38delta in insulin secretion and glucose homeostasis
    • Sumara G, Formentini I, Collins S, et al. Regulation of PKD by the MAPK p38delta in insulin secretion and glucose homeostasis. Cell. 2009;136(2):235-248.
    • (2009) Cell , vol.136 , Issue.2 , pp. 235-248
    • Sumara, G.1    Formentini, I.2    Collins, S.3
  • 30
    • 3342906957 scopus 로고    scopus 로고
    • PKD1/PKCmu promotes alphavbeta3 integrin recycling and delivery to nascent focal adhesions
    • DOI 10.1038/sj.emboj.7600267
    • Woods AJ, White DP, Caswell PT, Norman JCPKD1/PKCmu promotes alphavbeta3 integrin recycling and delivery to nascent focal adhesions. EMBO J. 2004;23(13):2531-2543. (Pubitemid 38988225)
    • (2004) EMBO Journal , vol.23 , Issue.13 , pp. 2531-2543
    • Woods, A.J.1    White, D.P.2    Caswell, P.T.3    Norman, J.C.4
  • 31
    • 34248226275 scopus 로고    scopus 로고
    • Alphavbeta3 and alpha5beta1 integrin recycling pathways dictate downstream Rho kinase signaling to regulate persistent cell migration
    • DOI 10.1083/jcb.200609004
    • White DP, Caswell PT, Norman JC. Alphavbeta3 and alpha5beta1 integrin recycling pathways dictate downstream Rho kinase signaling to regulate persistent cell migration. J Cell Biol. 2007;177(3):515-525. (Pubitemid 46718279)
    • (2007) Journal of Cell Biology , vol.177 , Issue.3 , pp. 515-525
    • White, D.P.1    Caswell, P.T.2    Norman, J.C.3
  • 32
    • 23844509495 scopus 로고    scopus 로고
    • Protein kinase D1 and the beta1 integrin cytoplasmic domain control beta1 integrin function via regulation of Rap1 activation
    • DOI 10.1016/j.immuni.2005.07.006, PII S1074761305002384
    • Medeiros RB, Dickey DM, Chung H, et al. Protein kinase D1 and the beta 1 integrin cytoplasmic domain control beta 1 integrin function via regulation of Rap1 activation. Immunity. 2005;23(2):213-226. (Pubitemid 41169290)
    • (2005) Immunity , vol.23 , Issue.2 , pp. 213-226
    • Medeiros, R.B.1    Dickey, D.M.2    Chung, H.3    Quale, A.C.4    Nagarajan, L.R.5    Billadeau, D.D.6    Shimizu, Y.7
  • 33
    • 77952054098 scopus 로고    scopus 로고
    • CalDAG-GEFI and platelet activation
    • Stefanini L, Bergmeier W. CalDAG-GEFI and platelet activation. Platelets. 2010;21(4):239-243.
    • (2010) Platelets , vol.21 , Issue.4 , pp. 239-243
    • Stefanini, L.1    Bergmeier, W.2
  • 34
    • 41149153993 scopus 로고    scopus 로고
    • Protein kinase D in the cardiovascular system: Emerging roles in health and disease
    • DOI 10.1161/CIRCRESAHA.107.168211, PII 0000301220080201000008
    • Avkiran M, Rowland AJ, Cuello F, Haworth RS. Protein kinase D in the cardiovascular system: emerging roles in health and disease. Circ Res. 2008;102(2):157-163. (Pubitemid 351651119)
    • (2008) Circulation Research , vol.102 , Issue.2 , pp. 157-163
    • Avkiran, M.1    Rowland, A.J.2    Cuello, F.3    Haworth, R.S.4
  • 35
    • 0032496417 scopus 로고    scopus 로고
    • Rapid activation of the novel serine/threonine protein kinase, protein kinase D by phorbol esters, angiotensin II and PDGF-BB in vascular smooth muscle cells
    • DOI 10.1016/S0014-5793(98)00427-X, PII S001457939800427X
    • Abedi H, Rozengurt E, Zachary I. Rapid activation of the novel serine/threonine protein kinase, protein kinase D by phorbol esters, angiotensin II and PDGF-BB in vascular smooth muscle cells. FEBS Lett. 1998;427(2):209-212. (Pubitemid 28225059)
    • (1998) FEBS Letters , vol.427 , Issue.2 , pp. 209-212
    • Abedi, H.1    Rozengurt, E.2    Zachary, I.3
  • 36
    • 33845934175 scopus 로고    scopus 로고
    • 165-induced angiogenesis through its interaction and regulation of phospholipase Cgamma phosphorylation
    • DOI 10.1074/jbc.M604853200
    • Qin L, Zeng H, Zhao DJ. Requirement of protein kinase D tyrosine phosphorylation for VEGFA165-induced angiogenesis through its interaction and regulation of phospholipase Cgamma phosphorylation. J Biol Chem. 2006;281(43):32550-32558. (Pubitemid 46036810)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.43 , pp. 32550-32558
    • Qin, L.1    Zeng, H.2    Zhao, D.3
  • 37
    • 69849111865 scopus 로고    scopus 로고
    • Lysophosphatidylcholine activates a novel PKD2-mediated signaling pathway that controls monocyte migration
    • Tan M, Hao F, Xu X, Chisolm GM, Cui MZ. Lysophosphatidylcholine activates a novel PKD2-mediated signaling pathway that controls monocyte migration. Arterioscler Thromb Vasc Biol. 2009;29(9):1376-1382.
    • (2009) Arterioscler Thromb Vasc Biol , vol.29 , Issue.9 , pp. 1376-1382
    • Tan, M.1    Hao, F.2    Xu, X.3    Chisolm, G.M.4    Cui, M.Z.5
  • 38
    • 59449092261 scopus 로고    scopus 로고
    • Identification of protein kinase D2 as a pivotal regulator of endothelial cell proliferation, migration, and angiogenesis
    • Hao Q, Wang L, Zhao ZJ, Tang H. Identification of protein kinase D2 as a pivotal regulator of endothelial cell proliferation, migration, and angiogenesis. J Biol Chem. 2009;284(2):799-806.
    • (2009) J Biol Chem , vol.284 , Issue.2 , pp. 799-806
    • Hao, Q.1    Wang, L.2    Zhao, Z.J.3    Tang, H.4
  • 39
    • 72749088774 scopus 로고    scopus 로고
    • Protein kinase Calpha: Disease regulator and therapeutic target
    • Konopatskaya O, Poole AW. Protein kinase Calpha: disease regulator and therapeutic target. Trends Pharmacol Sci. 2010;31(1):8-14.
    • (2010) Trends Pharmacol Sci , vol.31 , Issue.1 , pp. 8-14
    • Konopatskaya, O.1    Poole, A.W.2
  • 40
    • 42349108136 scopus 로고    scopus 로고
    • Protein kinase C alpha promotes angiogenic activity of human endothelial cells via induction of vascular endothelial growth factor
    • DOI 10.1093/cvr/cvm085
    • Xu H, Czerwinski P, Hortmann M, Sohn HY, Förstermann U, Li H. Protein kinase C alpha promotes angiogenic activity of human endothelial cells via induction of vascular endothelial growth factor. Cardiovasc Res. 2008;78(2):349-355. (Pubitemid 351556090)
    • (2008) Cardiovascular Research , vol.78 , Issue.2 , pp. 349-355
    • Xu, H.1    Czerwinski, P.2    Hortmann, M.3    Sohn, H.-Y.4    Forstermann, U.5    Li, H.6
  • 41
    • 33750439866 scopus 로고    scopus 로고
    • SDF-1-induced adhesion of monocytes to vascular endothelium is modulated by azelnidipine via protein kinase C inhibition
    • DOI 10.1016/j.ejphar.2006.09.028, PII S0014299906010557
    • Takahashi K, Shimokado K, Yoshida M. SDF-1-induced adhesion of monocytes to vascular endothelium is modulated by azelnidipine via protein kinase C inhibition. Eur J Pharmacol. 2006;552(1-3):162-169. (Pubitemid 44648085)
    • (2006) European Journal of Pharmacology , vol.552 , Issue.1-3 , pp. 162-169
    • Takahashi, K.1    Shimokado, K.2    Yoshida, M.3
  • 42
    • 0029671290 scopus 로고    scopus 로고
    • Protein kinase C-alpha regulates proliferation but not apoptosis in rat coronary vascular smooth muscle cells
    • Leszczynski D, Joenväärä, S., Foegh ML. Protein kinase C-alpha regulates proliferation but not apoptosis in rat coronary vascular smooth muscle cells. Life Sci. 1996;58(7):599-606.
    • (1996) Life Sci , vol.58 , Issue.7 , pp. 599-606
    • Leszczynski, D.1    Joenväärä, S.2    Foegh, M.L.3


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