메뉴 건너뛰기




Volumn 6, Issue , 2015, Pages

Pannexin 1 channels regulate leukocyte emigration through the venous endothelium during acute inflammation

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CYTOKINE; ION CHANNEL; PANNEXIN 1; PROTEIN TYROSINE KINASE; PURINERGIC RECEPTOR; TAMOXIFEN; TUMOR NECROSIS FACTOR ALPHA; TUMOR NECROSIS FACTOR RECEPTOR 1; UNCLASSIFIED DRUG; GAP JUNCTION PROTEIN; NERVE PROTEIN; PANX1 PROTEIN, HUMAN; PANX1 PROTEIN, MOUSE; TUMOR NECROSIS FACTOR;

EID: 84938931625     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms8965     Document Type: Article
Times cited : (153)

References (57)
  • 1
    • 34548230927 scopus 로고    scopus 로고
    • Getting to the site of inflammation: The leukocyte adhesion cascade updated
    • Ley, K., Laudanna, C., Cybulsky, M. I. & Nourshargh, S. Getting to the site of inflammation: The leukocyte adhesion cascade updated. Nat. Rev. Immunol. 7, 678-689 (2007).
    • (2007) Nat. Rev. Immunol. , vol.7 , pp. 678-689
    • Ley, K.1    Laudanna, C.2    Cybulsky, M.I.3    Nourshargh, S.4
  • 2
    • 0031754497 scopus 로고    scopus 로고
    • Receptors for purines and pyrimidines
    • Ralevic, V. & Burnstock, G. Receptors for purines and pyrimidines. Pharmacol. Rev. 50, 413-492 (1998).
    • (1998) Pharmacol. Rev. , vol.50 , pp. 413-492
    • Ralevic, V.1    Burnstock, G.2
  • 3
    • 79958166577 scopus 로고    scopus 로고
    • Major contribution of the P2Y(1)receptor in purinergic regulation of TNFalpha-induced vascular inflammation
    • Zerr, M. et al. Major contribution of the P2Y(1)receptor in purinergic regulation of TNFalpha-induced vascular inflammation. Circulation 123, 2404-2413 (2011).
    • (2011) Circulation , vol.123 , pp. 2404-2413
    • Zerr, M.1
  • 4
    • 79952131899 scopus 로고    scopus 로고
    • Selective induction of endothelial P2Y6 nucleotide receptor promotes vascular inflammation
    • Riegel, A. K. et al. Selective induction of endothelial P2Y6 nucleotide receptor promotes vascular inflammation. Blood 117, 2548-2555 (2011).
    • (2011) Blood , vol.117 , pp. 2548-2555
    • Riegel, A.K.1
  • 5
    • 66449110381 scopus 로고    scopus 로고
    • Self-regulation of inflammatory cell trafficking in mice by the leukocyte surface apyrase CD39
    • Hyman, M. C. et al. Self-regulation of inflammatory cell trafficking in mice by the leukocyte surface apyrase CD39. J. Clin. Invest. 119, 1136-1149 (2009).
    • (2009) J. Clin. Invest. , vol.119 , pp. 1136-1149
    • Hyman, M.C.1
  • 6
    • 77957943307 scopus 로고    scopus 로고
    • Intravascular danger signals guide neutrophils to sites of sterile inflammation
    • McDonald, B. et al. Intravascular danger signals guide neutrophils to sites of sterile inflammation. Science 330, 362-366 (2010).
    • (2010) Science , vol.330 , pp. 362-366
    • McDonald, B.1
  • 7
    • 59649088866 scopus 로고    scopus 로고
    • Adenosine and inflammation: CD39 and CD73 are critical mediators in LPS-induced PMN trafficking into the lungs
    • Reutershan, J. et al. Adenosine and inflammation: CD39 and CD73 are critical mediators in LPS-induced PMN trafficking into the lungs. FASEB J. 23, 473-482 (2009).
    • (2009) FASEB J. , vol.23 , pp. 473-482
    • Reutershan, J.1
  • 8
    • 0029968687 scopus 로고    scopus 로고
    • Adenosine inhibits cytokine release and expression of adhesion molecules by activated human endothelial cells
    • Bouma, M. G., Van Den Wildenberg, F. A. & Buurman, W. A. Adenosine inhibits cytokine release and expression of adhesion molecules by activated human endothelial cells. Am. J. Physiol. 270, C522-C529 (1996).
    • (1996) Am. J. Physiol. , vol.270 , pp. 522-529
    • Bouma, M.G.1    Van Den Wildenberg, F.A.2    Buurman, W.A.3
  • 9
    • 6344283049 scopus 로고    scopus 로고
    • Targeted disruption of cd73/ecto-5'-nucleotidase alters thromboregulation and augments vascular inflammatory response
    • Koszalka, P. et al. Targeted disruption of cd73/ecto-5'-nucleotidase alters thromboregulation and augments vascular inflammatory response. Circ. Res. 95, 814-821 (2004).
    • (2004) Circ. Res. , vol.95 , pp. 814-821
    • Koszalka, P.1
  • 10
    • 84862747859 scopus 로고    scopus 로고
    • Expression of pannexin isoforms in the systemic murine arterial network
    • Lohman, A. W. et al. Expression of pannexin isoforms in the systemic murine arterial network. J. Vasc. Res. 49, 405-416 (2012).
    • (2012) J. Vasc. Res. , vol.49 , pp. 405-416
    • Lohman, A.W.1
  • 11
    • 79960013081 scopus 로고    scopus 로고
    • Pannexin1 regulates alpha1-adrenergic receptor-mediated vasoconstriction
    • Billaud, M. et al. Pannexin1 regulates alpha1-adrenergic receptor-mediated vasoconstriction. Circ. Res. 109, 80-85 (2011).
    • (2011) Circ. Res. , vol.109 , pp. 80-85
    • Billaud, M.1
  • 12
    • 84933530564 scopus 로고    scopus 로고
    • Pannexin 1 facilitates arterial relaxation via an endothelium-derived hyperpolarization mechanism
    • Gaynullina, D., Shestopalov, V. I., Panchin, Y. & Tarasova, O. S. Pannexin 1 facilitates arterial relaxation via an endothelium-derived hyperpolarization mechanism. FEBS Lett. 589, 1164-1170 (2015).
    • (2015) FEBS Lett. , vol.589 , pp. 1164-1170
    • Gaynullina, D.1    Shestopalov, V.I.2    Panchin, Y.3    Tarasova, O.S.4
  • 14
    • 4143127920 scopus 로고    scopus 로고
    • Pannexin membrane channels are mechanosensitive conduits for ATP
    • Bao, L., Locovei, S. & Dahl, G. Pannexin membrane channels are mechanosensitive conduits for ATP. FEBS Lett. 572, 65-68 (2004).
    • (2004) FEBS Lett. , vol.572 , pp. 65-68
    • Bao, L.1    Locovei, S.2    Dahl, G.3
  • 15
    • 84869234325 scopus 로고    scopus 로고
    • S-nitrosylation inhibits pannexin 1 channel function
    • Lohman, A. W. et al. S-nitrosylation inhibits pannexin 1 channel function. J. Biol. Chem. 287, 39602-39612 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 39602-39612
    • Lohman, A.W.1
  • 16
    • 84898847537 scopus 로고    scopus 로고
    • The role of pannexin1 in the induction and resolution of inflammation
    • Adamson, S. E. & Leitinger, N. The role of pannexin1 in the induction and resolution of inflammation. FEBS Lett. 588, 1416-1422 (2014).
    • (2014) FEBS Lett. , vol.588 , pp. 1416-1422
    • Adamson, S.E.1    Leitinger, N.2
  • 17
    • 33750473352 scopus 로고    scopus 로고
    • Pannexin-1 mediates large pore formation and interleukin-1beta release by the ATP-gated P2X7 receptor
    • Pelegrin, P. & Surprenant, A. Pannexin-1 mediates large pore formation and interleukin-1beta release by the ATP-gated P2X7 receptor. EMBO J. 25, 5071-5082 (2006).
    • (2006) EMBO J. , vol.25 , pp. 5071-5082
    • Pelegrin, P.1    Surprenant, A.2
  • 18
    • 67650546999 scopus 로고    scopus 로고
    • The pannexin 1 channel activates the inflammasome in neurons and astrocytes
    • Silverman, W. R. et al. The pannexin 1 channel activates the inflammasome in neurons and astrocytes. J. Biol. Chem. 284, 18143-18151 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 18143-18151
    • Silverman, W.R.1
  • 19
    • 77957942834 scopus 로고    scopus 로고
    • Pannexin 1 channels mediate 'find-me' signal release and membrane permeability during apoptosis
    • Chekeni, F. B. et al. Pannexin 1 channels mediate 'find-me' signal release and membrane permeability during apoptosis. Nature 467, 863-867 (2010).
    • (2010) Nature , vol.467 , pp. 863-867
    • Chekeni, F.B.1
  • 20
    • 78149326486 scopus 로고    scopus 로고
    • Pannexin-1 hemichannel-mediated ATP release together with P2X1 and P2X4 receptors regulate T-cell activation at the immune synapse
    • Woehrle, T. et al. Pannexin-1 hemichannel-mediated ATP release together with P2X1 and P2X4 receptors regulate T-cell activation at the immune synapse. Blood 116, 3475-3484 (2010).
    • (2010) Blood , vol.116 , pp. 3475-3484
    • Woehrle, T.1
  • 21
    • 84863393008 scopus 로고    scopus 로고
    • Activation of neuronal P2X7 receptor-pannexin-1 mediates death of enteric neurons during colitis
    • Gulbransen, B. D. et al. Activation of neuronal P2X7 receptor-pannexin-1 mediates death of enteric neurons during colitis. Nat. Med. 18, 600-604 (2012).
    • (2012) Nat. Med. , vol.18 , pp. 600-604
    • Gulbransen, B.D.1
  • 22
    • 77957101431 scopus 로고    scopus 로고
    • Extracellular ATP is a danger signal activating P2X7 receptor in lung inflammation and fibrosis
    • Riteau, N. et al. Extracellular ATP is a danger signal activating P2X7 receptor in lung inflammation and fibrosis. Am. J. Respir. Crit. Care Med. 182, 774-783 (2010).
    • (2010) Am. J. Respir. Crit. Care Med. , vol.182 , pp. 774-783
    • Riteau, N.1
  • 23
    • 84866492972 scopus 로고    scopus 로고
    • Mechanisms of ATP release and signalling in the blood vessel wall
    • Lohman, A. W., Billaud, M. & Isakson, B. E. Mechanisms of ATP release and signalling in the blood vessel wall. Cardiovasc. Res. 95, 269-280 (2012).
    • (2012) Cardiovasc. Res. , vol.95 , pp. 269-280
    • Lohman, A.W.1    Billaud, M.2    Isakson, B.E.3
  • 24
    • 84898886896 scopus 로고    scopus 로고
    • Differentiating connexin hemichannels and pannexin channels in cellular ATP release
    • Lohman, A. W. & Isakson, B. E. Differentiating connexin hemichannels and pannexin channels in cellular ATP release. FEBS Lett. 588, 1379-1388 (2014).
    • (2014) FEBS Lett. , vol.588 , pp. 1379-1388
    • Lohman, A.W.1    Isakson, B.E.2
  • 25
    • 33645002735 scopus 로고    scopus 로고
    • Life cycle of connexins in health and disease
    • Laird, D. W. Life cycle of connexins in health and disease. Biochem. J. 394, 527-543 (2006).
    • (2006) Biochem. J. , vol.394 , pp. 527-543
    • Laird, D.W.1
  • 26
    • 36549084087 scopus 로고    scopus 로고
    • Pannexin 1 and pannexin 3 are glycoproteins that exhibit many distinct characteristics from the connexin family of gap junction proteins
    • Penuela, S. et al. Pannexin 1 and pannexin 3 are glycoproteins that exhibit many distinct characteristics from the connexin family of gap junction proteins. J. Cell Sci. 120, 3772-3783 (2007).
    • (2007) J. Cell Sci. , vol.120 , pp. 3772-3783
    • Penuela, S.1
  • 27
    • 84874956365 scopus 로고    scopus 로고
    • CALHM1 ion channel mediates purinergic neurotransmission of sweet, bitter and umami tastes
    • Taruno, A. et al. CALHM1 ion channel mediates purinergic neurotransmission of sweet, bitter and umami tastes. Nature 495, 223-226 (2013).
    • (2013) Nature , vol.495 , pp. 223-226
    • Taruno, A.1
  • 28
    • 84897897084 scopus 로고    scopus 로고
    • Unexpected link between an antibiotic, pannexin channels and apoptosis
    • Poon, I. K. et al. Unexpected link between an antibiotic, pannexin channels and apoptosis. Nature 507, 329-334 (2014).
    • (2014) Nature , vol.507 , pp. 329-334
    • Poon, I.K.1
  • 29
    • 49049106608 scopus 로고    scopus 로고
    • Type 1 TNF receptor forms a complex with and uses Jak2 and c-Src to selectively engage signaling pathways that regulate transcription factor activity
    • Pincheira, R., Castro, A. F., Ozes, O. N., Idumalla, P. S. & Donner, D. B. Type 1 TNF receptor forms a complex with and uses Jak2 and c-Src to selectively engage signaling pathways that regulate transcription factor activity. J. Immunol. 181, 1288-1298 (2008).
    • (2008) J. Immunol. , vol.181 , pp. 1288-1298
    • Pincheira, R.1    Castro, A.F.2    Ozes, O.N.3    Idumalla, P.S.4    Donner, D.B.5
  • 30
    • 0035862994 scopus 로고    scopus 로고
    • Genetic evidence for a role for Src family kinases in TNF family receptor signaling and cell survival
    • Xing, L. et al. Genetic evidence for a role for Src family kinases in TNF family receptor signaling and cell survival. Genes Dev. 15, 241-253 (2001).
    • (2001) Genes Dev. , vol.15 , pp. 241-253
    • Xing, L.1
  • 32
    • 84865708285 scopus 로고    scopus 로고
    • Anoxia-induced NMDA receptor activation opens pannexin channels via Src family kinases
    • Weilinger, N. L., Tang, P. L. & Thompson, R. J. Anoxia-induced NMDA receptor activation opens pannexin channels via Src family kinases. J. Neurosci. 32, 12579-12588 (2012).
    • (2012) J. Neurosci. , vol.32 , pp. 12579-12588
    • Weilinger, N.L.1    Tang, P.L.2    Thompson, R.J.3
  • 33
    • 0023649672 scopus 로고
    • Activation and suppression of pp60c-src transforming ability by mutation of its primary sites of tyrosine phosphorylation
    • Kmiecik, T. E. & Shalloway, D. Activation and suppression of pp60c-src transforming ability by mutation of its primary sites of tyrosine phosphorylation. Cell 49, 65-73 (1987).
    • (1987) Cell , vol.49 , pp. 65-73
    • Kmiecik, T.E.1    Shalloway, D.2
  • 34
    • 84923093408 scopus 로고    scopus 로고
    • A molecular signature in the pannexin1 intracellular loop confers channel activation by the alpha1 adrenoreceptor in smooth muscle cells
    • Billaud, M. et al. A molecular signature in the pannexin1 intracellular loop confers channel activation by the alpha1 adrenoreceptor in smooth muscle cells. Sci. Signal. 8, ra17 (2015).
    • (2015) Sci. Signal. , vol.8 , pp. 17
    • Billaud, M.1
  • 35
    • 34548294270 scopus 로고    scopus 로고
    • P2Y2 nucleotide receptor activation up-regulates vascular cell adhesion molecule-1 [corrected] expression and enhances lymphocyte adherence to a human submandibular gland cell line
    • Baker, O. J., Camden, J. M., Rome, D. E., Seye, C. I. & Weisman, G. A. P2Y2 nucleotide receptor activation up-regulates vascular cell adhesion molecule-1 [corrected] expression and enhances lymphocyte adherence to a human submandibular gland cell line. Mol. Immunol. 45, 65-75 (2008).
    • (2008) Mol. Immunol. , vol.45 , pp. 65-75
    • Baker, O.J.1    Camden, J.M.2    Rome, D.E.3    Seye, C.I.4    Weisman, G.A.5
  • 36
    • 55449114838 scopus 로고    scopus 로고
    • Involvement of native TRPC3 proteins in ATP-dependent expression of VCAM-1 and monocyte adherence in coronary artery endothelial cells
    • Smedlund, K. & Vazquez, G. Involvement of native TRPC3 proteins in ATP-dependent expression of VCAM-1 and monocyte adherence in coronary artery endothelial cells. Arterioscler. Thromb. Vasc. Biol. 28, 2049-2055 (2008).
    • (2008) Arterioscler. Thromb. Vasc. Biol. , vol.28 , pp. 2049-2055
    • Smedlund, K.1    Vazquez, G.2
  • 37
    • 78649861764 scopus 로고    scopus 로고
    • P2Y2 receptor regulates VCAM-1 membrane and soluble forms and eosinophil accumulation during lung inflammation
    • Vanderstocken, G. et al. P2Y2 receptor regulates VCAM-1 membrane and soluble forms and eosinophil accumulation during lung inflammation. J. Immunol. 185, 3702-3707 (2010).
    • (2010) J. Immunol. , vol.185 , pp. 3702-3707
    • Vanderstocken, G.1
  • 38
    • 84961033546 scopus 로고
    • The site of leucocyte emigration during inflammation
    • Marchesi, V. T. The site of leucocyte emigration during inflammation. Q. J. Exp. Physiol. Cogn. Med. Sci. 46, 115-118 (1961).
    • (1961) Q. J. Exp. Physiol. Cogn. Med. Sci. , vol.46 , pp. 115-118
    • Marchesi, V.T.1
  • 39
    • 0001731445 scopus 로고
    • Electron micrographic observations on the emigration of leucocytes
    • Marchesi, V. T. & Florey, H. W. Electron micrographic observations on the emigration of leucocytes. Q. J. Exp. Physiol. Cogn. Med. Sci. 45, 343-348 (1960).
    • (1960) Q. J. Exp. Physiol. Cogn. Med. Sci. , vol.45 , pp. 343-348
    • Marchesi, V.T.1    Florey, H.W.2
  • 40
    • 84859514212 scopus 로고    scopus 로고
    • Pannexin 1, an ATP release channel, is activated by caspase cleavage of its pore-associated C-terminal autoinhibitory region
    • Sandilos, J. K. et al. Pannexin 1, an ATP release channel, is activated by caspase cleavage of its pore-associated C-terminal autoinhibitory region. J. Biol. Chem. 287, 11303-11311 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 11303-11311
    • Sandilos, J.K.1
  • 41
    • 84902593565 scopus 로고    scopus 로고
    • Pannexin-1 is blocked by its C-terminus through a delocalized non-specific interaction surface
    • Dourado, M., Wong, E. & Hackos, D. H. Pannexin-1 is blocked by its C-terminus through a delocalized non-specific interaction surface. PLoS ONE 9, e99596 (2014).
    • (2014) PLoS ONE , vol.9 , pp. e99596
    • Dourado, M.1    Wong, E.2    Hackos, D.H.3
  • 42
    • 14844349754 scopus 로고    scopus 로고
    • Acute tumor necrosis factor alpha signaling via NADPH oxidase in microvascular endothelial cells: Role of p47phox phosphorylation and binding to TRAF4
    • Li, J. M., Fan, L. M., Christie, M. R. & Shah, A. M. Acute tumor necrosis factor alpha signaling via NADPH oxidase in microvascular endothelial cells: Role of p47phox phosphorylation and binding to TRAF4. Mol. Cell Biol. 25, 2320-2330 (2005).
    • (2005) Mol. Cell Biol. , vol.25 , pp. 2320-2330
    • Li, J.M.1    Fan, L.M.2    Christie, M.R.3    Shah, A.M.4
  • 43
    • 84876005139 scopus 로고    scopus 로고
    • TNFalpha induces survival through the FLIP-L-dependent activation of the MAPK/ERK pathway
    • Marques-Fernandez, F. et al. TNFalpha induces survival through the FLIP-L-dependent activation of the MAPK/ERK pathway. Cell Death Dis. 4, e493 (2013).
    • (2013) Cell Death Dis. , vol.4 , pp. e493
    • Marques-Fernandez, F.1
  • 44
    • 60849084461 scopus 로고    scopus 로고
    • A permeant regulating its permeation pore: Inhibition of pannexin 1 channels by ATP
    • Qiu, F. & Dahl, G. A permeant regulating its permeation pore: Inhibition of pannexin 1 channels by ATP. Am. J. Physiol. Cell Physiol. 296, C250-C255 (2009).
    • (2009) Am. J. Physiol. Cell Physiol. , vol.296 , pp. 250-255
    • Qiu, F.1    Dahl, G.2
  • 45
    • 0033520310 scopus 로고    scopus 로고
    • Nitric oxide controls src kinase activity through a sulfhydryl group modification-mediated Tyr-527-independent and Tyr-416-linked mechanism
    • Akhand, A. A. et al. Nitric oxide controls src kinase activity through a sulfhydryl group modification-mediated Tyr-527-independent and Tyr-416-linked mechanism. J. Biol. Chem. 274, 25821-25826 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 25821-25826
    • Akhand, A.A.1
  • 46
    • 77950469934 scopus 로고    scopus 로고
    • S-nitrosylation at cysteine 498 of c-Src tyrosine kinase regulates nitric oxide-mediated cell invasion
    • Rahman, M. A. et al. S-nitrosylation at cysteine 498 of c-Src tyrosine kinase regulates nitric oxide-mediated cell invasion. J. Biol. Chem. 285, 3806-3814 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 3806-3814
    • Rahman, M.A.1
  • 48
    • 0025731835 scopus 로고
    • Nitric oxide: An endogenous modulator of leukocyte adhesion
    • Kubes, P., Suzuki, M. & Granger, D. N. Nitric oxide: An endogenous modulator of leukocyte adhesion. Proc. Natl Acad. Sci. USA 88, 4651-4655 (1991).
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 4651-4655
    • Kubes, P.1    Suzuki, M.2    Granger, D.N.3
  • 49
    • 0026507703 scopus 로고
    • Nitric oxide modulates microvascular permeability
    • Kubes, P. & Granger, D. N. Nitric oxide modulates microvascular permeability. Am. J. Physiol. 262, H611-H615 (1992).
    • (1992) Am. J. Physiol. , vol.262 , pp. 611-615
    • Kubes, P.1    Granger, D.N.2
  • 50
    • 0347757088 scopus 로고    scopus 로고
    • Neutrophil migration in inflammation: Nitric oxide inhibits rolling, adhesion and induces apoptosis
    • Dal Secco, D. et al. Neutrophil migration in inflammation: Nitric oxide inhibits rolling, adhesion and induces apoptosis. Nitric Oxide 9, 153-164 (2003).
    • (2003) Nitric Oxide , vol.9 , pp. 153-164
    • Dal Secco, D.1
  • 51
    • 0030832089 scopus 로고    scopus 로고
    • Neutrophil transmigration: Modulation by pentoxifylline and nitric oxide
    • Clark, S. C., Shenton, B. K., Dark, J. H. & Kirby, J. A. Neutrophil transmigration: Modulation by pentoxifylline and nitric oxide. Biochem. Soc. Trans. 25, 454S (1997).
    • (1997) Biochem. Soc. Trans. , vol.25 , pp. 454
    • Clark, S.C.1    Shenton, B.K.2    Dark, J.H.3    Kirby, J.A.4
  • 52
    • 0032521006 scopus 로고    scopus 로고
    • Nitric oxide modulation of neutrophil-endothelium interaction: Difference between arterial and venous coronary bypass grafts
    • Chello, M., Mastroroberto, P., Perticone, F., Celi, V. & Colonna, A. Nitric oxide modulation of neutrophil-endothelium interaction: Difference between arterial and venous coronary bypass grafts. J. Am. Coll. Cardiol. 31, 823-826 (1998).
    • (1998) J. Am. Coll. Cardiol. , vol.31 , pp. 823-826
    • Chello, M.1    Mastroroberto, P.2    Perticone, F.3    Celi, V.4    Colonna, A.5
  • 53
    • 78049418900 scopus 로고    scopus 로고
    • Purinergic control of neutrophil activation
    • Grassi, F. Purinergic control of neutrophil activation. J. Mol. Cell Biol. 2, 176-177 (2010).
    • (2010) J. Mol. Cell Biol. , vol.2 , pp. 176-177
    • Grassi, F.1
  • 54
    • 84869888736 scopus 로고    scopus 로고
    • Purinergic P2Y(2) receptors promote neutrophil infiltration and hepatocyte death in mice with acute liver injury
    • Ayata, C. K. et al. Purinergic P2Y(2) receptors promote neutrophil infiltration and hepatocyte death in mice with acute liver injury. Gastroenterology 143, 1620-1629 e1624 (2012).
    • (2012) Gastroenterology , vol.143 , pp. 1620-1629e1624
    • Ayata, C.K.1
  • 55
    • 33845708770 scopus 로고    scopus 로고
    • ATP release guides neutrophil chemotaxis via P2Y2 and A3 receptors
    • Chen, Y. et al. ATP release guides neutrophil chemotaxis via P2Y2 and A3 receptors. Science 314, 1792-1795 (2006).
    • (2006) Science , vol.314 , pp. 1792-1795
    • Chen, Y.1
  • 56
    • 84881254482 scopus 로고    scopus 로고
    • Pannexin 1 channels link chemoattractant receptor signaling to local excitation and global inhibition responses at the front and back of polarized neutrophils
    • Bao, Y., Chen, Y., Ledderose, C., Li, L. & Junger, W. G. Pannexin 1 channels link chemoattractant receptor signaling to local excitation and global inhibition responses at the front and back of polarized neutrophils. J. Biol. Chem. 288, 22650-22657 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 22650-22657
    • Bao, Y.1    Chen, Y.2    Ledderose, C.3    Li, L.4    Junger, W.G.5
  • 57
    • 33745866942 scopus 로고    scopus 로고
    • Role of platelets in hypercholesterolemia-induced leukocyte recruitment and arteriolar dysfunction
    • Stokes, K. Y., Calahan, L., Russell, J. M., Gurwara, S. & Granger, D. N. Role of platelets in hypercholesterolemia-induced leukocyte recruitment and arteriolar dysfunction. Microcirculation 13, 377-388 (2006).
    • (2006) Microcirculation , vol.13 , pp. 377-388
    • Stokes, K.Y.1    Calahan, L.2    Russell, J.M.3    Gurwara, S.4    Granger, D.N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.