메뉴 건너뛰기




Volumn 2, Issue 61, 2009, Pages

Rac1 is a critical mediator of endothelium-derived neurotrophic activity

Author keywords

[No Author keywords available]

Indexed keywords

ARTEMIN; BRCA1 ASSOCIATED RING DOMAIN PROTEIN 1; CHROMOSOME PROTEIN; COLLAGEN; CYCLINE; DNA TOPOISOMERASE (ATP HYDROLYSING); FIBRONECTIN; GELATINASE A; GLYCOPROTEIN; HEAT SHOCK PROTEIN; HEPARIN; HISTONE H1; HYDROGEN PEROXIDE; KINESIN; LIPID PEROXIDE; MOLECULAR MOTOR; NEUROTROPHIC FACTOR; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PROFILIN; PROTEIN; PROTEIN ECT2; PROTEIN FOS; PROTEIN MYB; PROTEOHEPARAN SULFATE; RAC1 PROTEIN; REACTIVE OXYGEN METABOLITE; TAU PROTEIN; THROMBOSPONDIN 1; TUBULIN; UNCLASSIFIED DRUG; UNINDEXED DRUG; ARTN PROTEIN, MOUSE; LIPOCORTIN 5; NERVE GROWTH FACTOR; NERVE PROTEIN; NEUROPEPTIDE; RAC PROTEIN; RAC1 PROTEIN, MOUSE;

EID: 66149111387     PISSN: 19450877     EISSN: 19379145     Source Type: Journal    
DOI: 10.1126/scisignal.2000162     Document Type: Article
Times cited : (28)

References (56)
  • 2
    • 29244463365 scopus 로고    scopus 로고
    • Astrocyte-endothelial interactions at the blood-brain barrier
    • N. J. Abbott, L. Ronnback, E. Hansson, Astrocyte-endothelial interactions at the blood-brain barrier. Nat. Rev. Neurosci. 7, 41-53 (2006).
    • (2006) Nat. Rev. Neurosci. , vol.7 , pp. 41-53
    • Abbott, N.J.1    Ronnback, L.2    Hansson, E.3
  • 3
    • 20344373695 scopus 로고    scopus 로고
    • Multiple roles for MMPs and TIMPs in cerebral ischemia
    • L. A. Cunningham, M. Wetzel, G. A. Rosenberg, Multiple roles for MMPs and TIMPs in cerebral ischemia. Glia 50, 329-339 (2005).
    • (2005) Glia , vol.50 , pp. 329-339
    • Cunningham, L.A.1    Wetzel, M.2    Rosenberg, G.A.3
  • 4
    • 0141456653 scopus 로고    scopus 로고
    • Rac regulates cardiovascular superoxide through diverse molecular interactions: More than a binary GTP switch
    • D. Gregg, F. M. Rauscher, P. J. Goldschmidt-Clermont, Rac regulates cardiovascular superoxide through diverse molecular interactions: More than a binary GTP switch. Am. J. Physiol. Cell Physiol. 285, C723-C734 (2003).
    • (2003) Am. J. Physiol. Cell Physiol. , vol.285
    • Gregg, D.1    Rauscher, F.M.2    Goldschmidt-Clermont, P.J.3
  • 5
    • 33644866797 scopus 로고    scopus 로고
    • Role of small GTPases in endothelial cytoskeletal dynamics and the shear stress response
    • E. Tzima, Role of small GTPases in endothelial cytoskeletal dynamics and the shear stress response. Circ. Res. 98, 176-185 (2006).
    • (2006) Circ. Res. , vol.98 , pp. 176-185
    • Tzima, E.1
  • 6
    • 0037069690 scopus 로고    scopus 로고
    • Rho GTPases in cell biology
    • S. Etienne-Manneville, A. Hall, Rho GTPases in cell biology. Nature 420, 629-635 (2002).
    • (2002) Nature , vol.420 , pp. 629-635
    • Etienne-Manneville, S.1    Hall, A.2
  • 7
    • 0037079071 scopus 로고    scopus 로고
    • Drug and gene delivery to the brain: The vascular route
    • W. M. Pardridge, Drug and gene delivery to the brain: The vascular route. Neuron 36, 555-558 (2002).
    • (2002) Neuron , vol.36 , pp. 555-558
    • Pardridge, W.M.1
  • 8
    • 33846501598 scopus 로고    scopus 로고
    • GDNF family receptor complexes are emerging drug targets
    • M. M. Bespalov, M. Saarma, GDNF family receptor complexes are emerging drug targets. Trends Pharmacol. Sci. 28, 68-74 (2007).
    • (2007) Trends Pharmacol. Sci. , vol.28 , pp. 68-74
    • Bespalov, M.M.1    Saarma, M.2
  • 9
    • 12344336804 scopus 로고    scopus 로고
    • Neuroprotection in experimental stroke with targeted neurotrophins
    • D. Wu, Neuroprotection in experimental stroke with targeted neurotrophins. NeuroRx 2, 120-128 (2005).
    • (2005) NeuroRx , vol.2 , pp. 120-128
    • Wu, D.1
  • 10
    • 38149090292 scopus 로고    scopus 로고
    • The blood-brain barrier in health and chronic neurodegenerative disorders
    • B. V. Zlokovic, The blood-brain barrier in health and chronic neurodegenerative disorders. Neuron 57, 178-201 (2008).
    • (2008) Neuron , vol.57 , pp. 178-201
    • Zlokovic, B.V.1
  • 11
    • 84984763363 scopus 로고    scopus 로고
    • Mechanisms, challenges and opportunities in stroke
    • E. H. Lo, T. Dalkara, M. A. Moskowitz, Mechanisms, challenges and opportunities in stroke. Nat. Rev. Neurosci. 4, 399-415 (2003).
    • (2003) Nat. Rev. Neurosci. , vol.4 , pp. 399-415
    • Lo, E.H.1    Dalkara, T.2    Moskowitz, M.A.3
  • 12
    • 0032796824 scopus 로고    scopus 로고
    • Endothelial trophic support of neuronal production and recruitment from the adult mammalian subependyma
    • C. Leventhal, S. Rafii, D. Rafii, A. Shahar, S. A. Goldman, Endothelial trophic support of neuronal production and recruitment from the adult mammalian subependyma. Mol. Cell. Neurosci. 13, 450-464 (1999).
    • (1999) Mol. Cell. Neurosci. , vol.13 , pp. 450-464
    • Leventhal, C.1    Rafii, S.2    Rafii, D.3    Shahar, A.4    Goldman, S.A.5
  • 14
    • 50949086778 scopus 로고    scopus 로고
    • Regulation of endothelial nitric oxide synthase and postnatal angiogenesis by Rac1
    • N. Sawada, S. Salomone, H. H. Kim, D. J. Kwiatkowski, J. K. Liao, Regulation of endothelial nitric oxide synthase and postnatal angiogenesis by Rac1. Circ. Res. 103, 360-368 (2008).
    • (2008) Circ. Res. , vol.103 , pp. 360-368
    • Sawada, N.1    Salomone, S.2    Kim, H.H.3    Kwiatkowski, D.J.4    Liao, J.K.5
  • 15
    • 0035911253 scopus 로고    scopus 로고
    • Conditional vascular cell adhesion molecule 1 deletion in mice: Impaired lymphocyte migration to bone marrow
    • P. A. Koni, S. K. Joshi, U. A. Temann, D. Olson, L. Burkly, R. A. Flavell, Conditional vascular cell adhesion molecule 1 deletion in mice: Impaired lymphocyte migration to bone marrow. J. Exp. Med. 193, 741-754 (2001).
    • (2001) J. Exp. Med. , vol.193 , pp. 741-754
    • Koni, P.A.1    Joshi, S.K.2    Temann, U.A.3    Olson, D.4    Burkly, L.5    Flavell, R.A.6
  • 20
    • 0029101360 scopus 로고
    • An essential role for Rho, Rac, and Cdc42 GTPases in cell cycle progression through G1
    • M. F. Olson, A. Ashworth, A. Hall, An essential role for Rho, Rac, and Cdc42 GTPases in cell cycle progression through G1. Science 269, 1270-1272 (1995).
    • (1995) Science , vol.269 , pp. 1270-1272
    • Olson, M.F.1    Ashworth, A.2    Hall, A.3
  • 21
    • 3042621447 scopus 로고    scopus 로고
    • Determinants of human plasma glutathione peroxidase (GPx-3) expression
    • C. Bierl, B. Voetsch, R. C. Jin, D. E. Handy, J. Loscalzo, Determinants of human plasma glutathione peroxidase (GPx-3) expression. J. Biol. Chem. 279, 26839-26845 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 26839-26845
    • Bierl, C.1    Voetsch, B.2    Jin, R.C.3    Handy, D.E.4    Loscalzo, J.5
  • 23
    • 0036090023 scopus 로고    scopus 로고
    • Invited review: Interplay between molecular chaperones and signaling pathways in survival of heat shock
    • V. L. Gabai, M. Y. Sherman, Invited review: Interplay between molecular chaperones and signaling pathways in survival of heat shock. J. Appl. Physiol. 92, 1743-1748 (2002).
    • (2002) J. Appl. Physiol. , vol.92 , pp. 1743-1748
    • Gabai, V.L.1    Sherman, M.Y.2
  • 24
    • 0037064065 scopus 로고    scopus 로고
    • The small heat shock protein αB-crystallin negatively regulates apoptosis during myogenic differentiation by inhibiting caspase-3 activation
    • M. C. Kamradt, F. Chen, S. Sam, V. L. Cryns, The small heat shock protein αB-crystallin negatively regulates apoptosis during myogenic differentiation by inhibiting caspase-3 activation. J. Biol. Chem. 277, 38731-38736 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 38731-38736
    • Kamradt, M.C.1    Chen, F.2    Sam, S.3    Cryns, V.L.4
  • 25
    • 0141805544 scopus 로고    scopus 로고
    • Stressed to death: Regulation of apoptotic signaling pathways by the heat shock proteins
    • RE1
    • H. M. Beere, Stressed to death: Regulation of apoptotic signaling pathways by the heat shock proteins. Sci. STKE 2001, RE1 (2001).
    • (2001) Sci. STKE , vol.2001
    • Beere, H.M.1
  • 26
    • 11844298904 scopus 로고    scopus 로고
    • The role of thrombospondins 1 and 2 in the regulation of cell-matrix interactions, collagen fibril formation, and the response to injury
    • P. Bornstein, A. Agah, T. R. Kyriakides, The role of thrombospondins 1 and 2 in the regulation of cell-matrix interactions, collagen fibril formation, and the response to injury. Int. J. Biochem. Cell Biol. 36, 1115-1125 (2004).
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 1115-1125
    • Bornstein, P.1    Agah, A.2    Kyriakides, T.R.3
  • 27
    • 0035049231 scopus 로고    scopus 로고
    • Thrombospondins as matricellular modulators of cell function
    • P. Bornstein, Thrombospondins as matricellular modulators of cell function. J. Clin. Invest. 107, 929-934 (2001).
    • (2001) J. Clin. Invest. , vol.107 , pp. 929-934
    • Bornstein, P.1
  • 28
    • 0034109215 scopus 로고    scopus 로고
    • Activation of latent TGF-beta by thrombospondin-1: Mechanisms and physiology
    • J. E. Murphy-Ullrich, M. Poczatek, Activation of latent TGF-beta by thrombospondin-1: Mechanisms and physiology. Cytokine Growth Factor Rev. 11, 59-69 (2000).
    • (2000) Cytokine Growth Factor Rev. , vol.11 , pp. 59-69
    • Murphy-Ullrich, J.E.1    Poczatek, M.2
  • 29
    • 21444434608 scopus 로고    scopus 로고
    • Fibronectin regulates latent transforming growth factor-β (TGFβ) by controlling matrix assembly of latent TGFβ-binding protein-1
    • S. L. Dallas, P. Sivakumar, C. J. Jones, Q. Chen, D. M. Peters, D. F. Mosher, M. J. Humphries, C. M. Kielty, Fibronectin regulates latent transforming growth factor-β (TGFβ) by controlling matrix assembly of latent TGFβ-binding protein-1. J. Biol. Chem. 280, 18871-18880 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 18871-18880
    • Dallas, S.L.1    Sivakumar, P.2    Jones, C.J.3    Chen, Q.4    Peters, D.M.5    Mosher, D.F.6    Humphries, M.J.7    Kielty, C.M.8
  • 30
    • 0034105456 scopus 로고    scopus 로고
    • Co-activation of TGF-ss and cytokine signaling pathways are required for neurotrophic functions
    • K. Unsicker, K. Krieglstein, Co-activation of TGF-ss and cytokine signaling pathways are required for neurotrophic functions. Cytokine Growth Factor Rev. 11, 97-102 (2000).
    • (2000) Cytokine Growth Factor Rev. , vol.11 , pp. 97-102
    • Unsicker, K.1    Krieglstein, K.2
  • 31
    • 0037079702 scopus 로고    scopus 로고
    • Increased and prolonged inflammation and angiogenesis in delayed-type hypersensitivity reactions elicited in the skin of thrombospondin-2-deficient mice
    • B. Lange-Asschenfeldt, W. Weninger, P. Velasco, T. R. Kyriakides, U. H. von Andrian, P. Bornstein, M. Detmar, Increased and prolonged inflammation and angiogenesis in delayed-type hypersensitivity reactions elicited in the skin of thrombospondin-2-deficient mice. Blood 99, 538-545 (2002).
    • (2002) Blood , vol.99 , pp. 538-545
    • Lange-Asschenfeldt, B.1    Weninger, W.2    Velasco, P.3    Kyriakides, T.R.4    Von Andrian, U.H.5    Bornstein, P.6    Detmar, M.7
  • 32
    • 0034807581 scopus 로고    scopus 로고
    • Cytoskeletal regulation of pulmonary vascular permeability
    • S. M. Dudek, J. G. Garcia, Cytoskeletal regulation of pulmonary vascular permeability. J. Appl. Physiol. 91, 1487-1500 (2001).
    • (2001) J. Appl. Physiol. , vol.91 , pp. 1487-1500
    • Dudek, S.M.1    Garcia, J.G.2
  • 33
    • 33745833345 scopus 로고    scopus 로고
    • Genetic deletion of Rac1 GTPase reveals its critical role in actin stress fiber formation and focal adhesion complex assembly
    • F. Guo, M. Debidda, L. Yang, D. A. Williams, Y. Zheng, Genetic deletion of Rac1 GTPase reveals its critical role in actin stress fiber formation and focal adhesion complex assembly. J. Biol. Chem. 281, 18652-18659 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 18652-18659
    • Guo, F.1    Debidda, M.2    Yang, L.3    Williams, D.A.4    Zheng, Y.5
  • 34
    • 33646867122 scopus 로고    scopus 로고
    • Mechanistic differences in actin bundling activity of two mammalian formins, FRL1 and mDia2
    • E. S. Harris, I. Rouiller, D. Hanein, H. N. Higgs, Mechanistic differences in actin bundling activity of two mammalian formins, FRL1 and mDia2. J. Biol. Chem. 281, 14383-14392 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 14383-14392
    • Harris, E.S.1    Rouiller, I.2    Hanein, D.3    Higgs, H.N.4
  • 36
    • 0141742631 scopus 로고    scopus 로고
    • Fibroblast growth factors and their receptors in the central nervous system
    • B. Reuss, O. von Bohlen und Halbach, Fibroblast growth factors and their receptors in the central nervous system. Cell Tissue Res. 313, 139-157 (2003).
    • (2003) Cell Tissue Res. , vol.313 , pp. 139-157
    • Reuss, B.1    Von Bohlen2    Halbach, O.3
  • 37
    • 12744252899 scopus 로고    scopus 로고
    • Stroke and TGF-β proteins: Glial cell line-derived neurotrophic factor and bone morphogenetic protein
    • B. K. Harvey, B. J. Hoffer, Y. Wang, Stroke and TGF-β proteins: Glial cell line-derived neurotrophic factor and bone morphogenetic protein. Pharmacol. Ther. 105, 113-125 (2005).
    • (2005) Pharmacol. Ther. , vol.105 , pp. 113-125
    • Harvey, B.K.1    Hoffer, B.J.2    Wang, Y.3
  • 38
    • 0034353578 scopus 로고    scopus 로고
    • What role(s) for TGFα in the central nervous system?
    • M. P. Junier, What role(s) for TGFα in the central nervous system? Prog. Neurobiol. 62, 443-473 (2000).
    • (2000) Prog. Neurobiol. , vol.62 , pp. 443-473
    • Junier, M.P.1
  • 39
    • 0036275026 scopus 로고    scopus 로고
    • Protective effects of glial cell line-derived neurotrophic factor in ischemic brain injury
    • Y. Wang, C. F. Chang, M. Morales, Y. H. Chiang, J. Hoffer, Protective effects of glial cell line-derived neurotrophic factor in ischemic brain injury. Ann. N. Y. Acad. Sci. 962, 423-437 (2002).
    • (2002) Ann. N.Y. Acad. Sci. , vol.962 , pp. 423-437
    • Wang, Y.1    Chang, C.F.2    Morales, M.3    Chiang, Y.H.4    Hoffer, J.5
  • 40
  • 41
  • 44
    • 31444443338 scopus 로고    scopus 로고
    • GDNF family ligands display distinct action profiles on cultured GABAergic and serotonergic neurons of rat ventral mesencephalon
    • A. Ducray, S. H. Krebs, B. Schaller, R. W. Seiler, M. Meyer, H. R. Widmer, GDNF family ligands display distinct action profiles on cultured GABAergic and serotonergic neurons of rat ventral mesencephalon. Brain Res. 1069, 104-112 (2006).
    • (2006) Brain Res. , vol.1069 , pp. 104-112
    • Ducray, A.1    Krebs, S.H.2    Schaller, B.3    Seiler, R.W.4    Meyer, M.5    Widmer, H.R.6
  • 45
    • 0034519962 scopus 로고    scopus 로고
    • GDNF and neublastin protect against NMDA-induced excitotoxicity in hippocampal slice cultures
    • C. Bonde, B. W. Kristensen, M. Blaabjerg, T. E. Johansen, J. Zimmer, M. Meyer, GDNF and neublastin protect against NMDA-induced excitotoxicity in hippocampal slice cultures. Neuroreport 11, 4069-4073 (2000).
    • (2000) Neuroreport , vol.11 , pp. 4069-4073
    • Bonde, C.1    Kristensen, B.W.2    Blaabjerg, M.3    Johansen, T.E.4    Zimmer, J.5    Meyer, M.6
  • 47
    • 0034791087 scopus 로고    scopus 로고
    • Transforming growth factor β1 (TGF-β1) promotes endothelial cell survival during in vitro angiogenesis via an autocrine mechanism implicating TGF-α signaling
    • F. Viñals, J. Pouysségur, Transforming growth factor β1 (TGF-β1) promotes endothelial cell survival during in vitro angiogenesis via an autocrine mechanism implicating TGF-α signaling. Mol. Cell. Biol. 21, 7218-7230 (2001).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7218-7230
    • Viñals, F.1    Pouysségur, J.2
  • 48
    • 12844287442 scopus 로고    scopus 로고
    • Continuous low-level glial cell line-derived neurotrophic factor delivery using recombinant adeno-associated viral vectors provides neuroprotection and induces behavioral recovery in a primate model of Parkinson's disease
    • A. Eslamboli, B. Georgievska, R. M. Ridley, H. F. Baker, N. Muzyczka, C. Burger, R. J. Mandel, L. Annett, D. Kirik, Continuous low-level glial cell line-derived neurotrophic factor delivery using recombinant adeno-associated viral vectors provides neuroprotection and induces behavioral recovery in a primate model of Parkinson's disease. J. Neurosci. 25, 769-777 (2005).
    • (2005) J. Neurosci. , vol.25 , pp. 769-777
    • Eslamboli, A.1    Georgievska, B.2    Ridley, R.M.3    Baker, H.F.4    Muzyczka, N.5    Burger, C.6    Mandel, R.J.7    Annett, L.8    Kirik, D.9
  • 50
    • 0035099411 scopus 로고    scopus 로고
    • Plasma fibronectin supports neuronal survival and reduces brain injury following transient focal cerebral ischemia but is not essential for skin-wound healing and hemostasis
    • T. Sakai, K. J. Johnson, M. Murozono, K. Sakai, M. A. Magnuson, T. Wieloch, T. Cronberg, A. Isshiki, H. P. Erickson, R. Fässler, Plasma fibronectin supports neuronal survival and reduces brain injury following transient focal cerebral ischemia but is not essential for skin-wound healing and hemostasis. Nat. Med. 7, 324-330 (2001).
    • (2001) Nat. Med. , vol.7 , pp. 324-330
    • Sakai, T.1    Johnson, K.J.2    Murozono, M.3    Sakai, K.4    Magnuson, M.A.5    Wieloch, T.6    Cronberg, T.7    Isshiki, A.8    Erickson, H.P.9    Fässler, R.10
  • 51
    • 0042343822 scopus 로고    scopus 로고
    • Functions of fibroblast growth factor (FGF)-2 and FGF-5 in astroglial differentiation and blood-brain barrier permeability: Evidence from mouse mutants
    • B. Reuss, R. Dono, K. Unsicker, Functions of fibroblast growth factor (FGF)-2 and FGF-5 in astroglial differentiation and blood-brain barrier permeability: Evidence from mouse mutants. J. Neurosci. 23, 6404-6412 (2003).
    • (2003) J. Neurosci. , vol.23 , pp. 6404-6412
    • Reuss, B.1    Dono, R.2    Unsicker, K.3
  • 52
    • 0034597430 scopus 로고    scopus 로고
    • Vascular niche for adult hippocampal neurogenesis
    • T. D. Palmer, A. R. Willhoite, F. H. Gage, Vascular niche for adult hippocampal neurogenesis. J. Comp. Neurol. 425, 479-494 (2000).
    • (2000) J. Comp. Neurol. , vol.425 , pp. 479-494
    • Palmer, T.D.1    Willhoite, A.R.2    Gage, F.H.3
  • 54
    • 0038714289 scopus 로고    scopus 로고
    • Endothelial signaling during development
    • O. Cleaver, D. A. Melton, Endothelial signaling during development. Nat. Med. 9, 661-668 (2003).
    • (2003) Nat. Med. , vol.9 , pp. 661-668
    • Cleaver, O.1    Melton, D.A.2
  • 56
    • 77953672374 scopus 로고    scopus 로고
    • We thank D. J. Kwiatkowski for providing us with conditional Rac1 mice. This work was supported by grants from the NIH (HL052233, HL080187, and NS101828). N.S. was supported by the fellowships from the Uehara Memorial Foundation, the Cell Science Research Foundation, and Mochida Memorial Foundation for Medical and Pharmaceutical Research. There are no disclosures or conflicts of interest for all of the authors
    • We thank D. J. Kwiatkowski for providing us with conditional Rac1 mice. This work was supported by grants from the NIH (HL052233, HL080187, and NS101828). N.S. was supported by the fellowships from the Uehara Memorial Foundation, the Cell Science Research Foundation, and Mochida Memorial Foundation for Medical and Pharmaceutical Research. There are no disclosures or conflicts of interest for all of the authors.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.