메뉴 건너뛰기




Volumn 75, Issue 5, 2014, Pages 644-658

Cytosolic phospholipase A2 protein as a novel therapeutic target for spinal cord injury

Author keywords

[No Author keywords available]

Indexed keywords

ARACHIDONIC ACID; ARACHIDONYL TRIFLUOROMETHYL KETONE; CALCIMYCIN; CERAMIDE 1 PHOSPHATE; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHOLIPASE A2; 1,3 BUTADIENE DERIVATIVE; 1,4 DIAMINO 1,4 BIS(2 AMINOPHENYLTHIO) 2,3 DICYANOBUTADIENE; ENZYME INHIBITOR; NITRILE; PHOSPHOLIPASE A2 GROUP IV;

EID: 84902277551     PISSN: 03645134     EISSN: 15318249     Source Type: Journal    
DOI: 10.1002/ana.24134     Document Type: Article
Times cited : (72)

References (59)
  • 1
    • 84874447289 scopus 로고    scopus 로고
    • Spinal cord injury facts and figures at a glance
    • Spinal cord injury facts and figures at a glance. J Spinal Cord Med 2012; 35: 480-481.
    • (2012) J Spinal Cord Med , vol.35 , pp. 480-481
  • 3
    • 0027475987 scopus 로고
    • Secondary injury mechanisms in acute spinal cord injury
    • Young W,. Secondary injury mechanisms in acute spinal cord injury. J Emerg Med 1993; 11 (suppl 1): 13-22.
    • (1993) J Emerg Med , vol.11 , Issue.SUPPL. 1 , pp. 13-22
    • Young, W.1
  • 4
    • 0022921520 scopus 로고
    • Role of lipid peroxidation in post-traumatic spinal cord degeneration: A review
    • Hall ED, Braughler JM,. Role of lipid peroxidation in post-traumatic spinal cord degeneration: a review. Cent Nerv Syst Trauma 1986; 3: 281-294.
    • (1986) Cent Nerv Syst Trauma , vol.3 , pp. 281-294
    • Hall, E.D.1    Braughler, J.M.2
  • 5
    • 3042816808 scopus 로고    scopus 로고
    • The role of excitotoxicity in secondary mechanisms of spinal cord injury: A review with an emphasis on the implications for white matter degeneration
    • Park E, Velumian AA, Fehlings MG,. The role of excitotoxicity in secondary mechanisms of spinal cord injury: a review with an emphasis on the implications for white matter degeneration. J Neurotrauma 2004; 21: 754-774.
    • (2004) J Neurotrauma , vol.21 , pp. 754-774
    • Park, E.1    Velumian, A.A.2    Fehlings, M.G.3
  • 6
    • 0034655408 scopus 로고    scopus 로고
    • Cytochrome c release and caspase activation in traumatic axonal injury
    • Buki A, Okonkwo DO, Wang KK, Povlishock JT,. Cytochrome c release and caspase activation in traumatic axonal injury. J Neurosci 2000; 20: 2825-2834.
    • (2000) J Neurosci , vol.20 , pp. 2825-2834
    • Buki, A.1    Okonkwo, D.O.2    Wang, K.K.3    Povlishock, J.T.4
  • 7
    • 79952445447 scopus 로고    scopus 로고
    • Inhibition of cPLA2 activation by Ginkgo biloba extract protects spinal cord neurons from glutamate excitotoxicity and oxidative stress-induced cell death
    • Zhao Z, Liu N, Huang J, et al. Inhibition of cPLA2 activation by Ginkgo biloba extract protects spinal cord neurons from glutamate excitotoxicity and oxidative stress-induced cell death. J Neurochem 2011; 116: 1057-1065.
    • (2011) J Neurochem , vol.116 , pp. 1057-1065
    • Zhao, Z.1    Liu, N.2    Huang, J.3
  • 8
    • 77955086151 scopus 로고    scopus 로고
    • Phospholipase A2 and its molecular mechanism after spinal cord injury
    • Liu NK, Xu XM,. Phospholipase A2 and its molecular mechanism after spinal cord injury. Mol Neurobiol 2010; 41: 197-205.
    • (2010) Mol Neurobiol , vol.41 , pp. 197-205
    • Liu, N.K.1    Xu, X.M.2
  • 9
    • 70450220984 scopus 로고    scopus 로고
    • Differential expression of sPLA2 following spinal cord injury and a functional role for sPLA2-IIA in mediating oligodendrocyte death
    • Titsworth WL, Cheng X, Ke Y, et al. Differential expression of sPLA2 following spinal cord injury and a functional role for sPLA2-IIA in mediating oligodendrocyte death. Glia 2009; 57: 1521-1537.
    • (2009) Glia , vol.57 , pp. 1521-1537
    • Titsworth, W.L.1    Cheng, X.2    Ke, Y.3
  • 10
    • 0033791814 scopus 로고    scopus 로고
    • Membrane breakdown in acute and chronic neurodegeneration: Focus on choline-containing phospholipids
    • Klein J,. Membrane breakdown in acute and chronic neurodegeneration: focus on choline-containing phospholipids. J Neural Transm 2000; 107: 1027-1063.
    • (2000) J Neural Transm , vol.107 , pp. 1027-1063
    • Klein, J.1
  • 11
    • 2942696319 scopus 로고    scopus 로고
    • Activation of cytosolic phospholipase A2 in Her14 fibroblasts by hydrogen peroxide: A p42/44(MAPK)-dependent and phosphorylation-independent mechanism
    • van Rossum GS, Drummen GP, Verkleij AJ, et al. Activation of cytosolic phospholipase A2 in Her14 fibroblasts by hydrogen peroxide: a p42/44(MAPK)-dependent and phosphorylation-independent mechanism. Biochim Biophys Acta 2004; 1636: 183-195.
    • (2004) Biochim Biophys Acta , vol.1636 , pp. 183-195
    • Van Rossum, G.S.1    Drummen, G.P.2    Verkleij, A.J.3
  • 12
    • 48249106275 scopus 로고    scopus 로고
    • Role of secretory phospholipase a(2) in CNS inflammation: Implications in traumatic spinal cord injury
    • Titsworth WL, Liu NK, Xu XM,. Role of secretory phospholipase a(2) in CNS inflammation: implications in traumatic spinal cord injury. CNS Neurol Disord Drug Targets 2008; 7: 254-269.
    • (2008) CNS Neurol Disord Drug Targets , vol.7 , pp. 254-269
    • Titsworth, W.L.1    Liu, N.K.2    Xu, X.M.3
  • 14
    • 0030222498 scopus 로고    scopus 로고
    • Roles of phospholipases A2 in brain cell and tissue injury associated with ischemia and excitotoxicity
    • Bonventre JV,. Roles of phospholipases A2 in brain cell and tissue injury associated with ischemia and excitotoxicity. J Lipid Mediat Cell Signal 1996; 14: 15-23.
    • (1996) J Lipid Mediat Cell Signal , vol.14 , pp. 15-23
    • Bonventre, J.V.1
  • 15
    • 33645786025 scopus 로고    scopus 로고
    • A novel role of phospholipase A2 in mediating spinal cord secondary injury
    • Liu NK, Zhang YP, Titsworth WL, et al. A novel role of phospholipase A2 in mediating spinal cord secondary injury. Ann Neurol 2006; 59: 606-619.
    • (2006) Ann Neurol , vol.59 , pp. 606-619
    • Liu, N.K.1    Zhang, Y.P.2    Titsworth, W.L.3
  • 16
    • 34948894950 scopus 로고    scopus 로고
    • Annexin A1 reduces inflammatory reaction and tissue damage through inhibition of phospholipase A2 activation in adult rats following spinal cord injury
    • Liu NK, Zhang YP, Han S, et al. Annexin A1 reduces inflammatory reaction and tissue damage through inhibition of phospholipase A2 activation in adult rats following spinal cord injury. J Neuropathol Exp Neurol 2007; 66: 932-943.
    • (2007) J Neuropathol Exp Neurol , vol.66 , pp. 932-943
    • Liu, N.K.1    Zhang, Y.P.2    Han, S.3
  • 18
    • 82655171632 scopus 로고    scopus 로고
    • Phospholipase A2 superfamily members play divergent roles after spinal cord injury
    • Lopez-Vales R, Ghasemlou N, Redensek A, et al. Phospholipase A2 superfamily members play divergent roles after spinal cord injury. FASEB J 2011; 25: 4240-4252.
    • (2011) FASEB J , vol.25 , pp. 4240-4252
    • Lopez-Vales, R.1    Ghasemlou, N.2    Redensek, A.3
  • 19
    • 0034739477 scopus 로고    scopus 로고
    • Specific physiological roles of cytosolic phospholipase A(2) as defined by gene knockouts
    • Sapirstein A, Bonventre JV,. Specific physiological roles of cytosolic phospholipase A(2) as defined by gene knockouts. Biochim Biophys Acta 2000; 1488: 139-148.
    • (2000) Biochim Biophys Acta , vol.1488 , pp. 139-148
    • Sapirstein, A.1    Bonventre, J.V.2
  • 20
    • 0031471709 scopus 로고    scopus 로고
    • Reduced fertility and postischaemic brain injury in mice deficient in cytosolic phospholipase A2
    • Bonventre JV, Huang Z, Taheri MR, et al. Reduced fertility and postischaemic brain injury in mice deficient in cytosolic phospholipase A2. Nature 1997; 390: 622-625.
    • (1997) Nature , vol.390 , pp. 622-625
    • Bonventre, J.V.1    Huang, Z.2    Taheri, M.R.3
  • 21
    • 0032891034 scopus 로고    scopus 로고
    • Animal models of spinal cord contusion injuries
    • Khan T, Havey RM, Sayers ST, et al. Animal models of spinal cord contusion injuries. Lab Anim Sci 1999; 49: 161-172.
    • (1999) Lab Anim Sci , vol.49 , pp. 161-172
    • Khan, T.1    Havey, R.M.2    Sayers, S.T.3
  • 22
    • 0035873540 scopus 로고    scopus 로고
    • Neurotrophic factors and receptors in the immature and adult spinal cord after mechanical injury or kainic acid
    • Widenfalk J, Lundstromer K, Jubran M, et al. Neurotrophic factors and receptors in the immature and adult spinal cord after mechanical injury or kainic acid. J Neurosci 2001; 21: 3457-3475.
    • (2001) J Neurosci , vol.21 , pp. 3457-3475
    • Widenfalk, J.1    Lundstromer, K.2    Jubran, M.3
  • 23
    • 43049168863 scopus 로고    scopus 로고
    • No evidence for chronic demyelination in spared axons after spinal cord injury in a mouse
    • Lasiene J, Shupe L, Perlmutter S, Horner P,. No evidence for chronic demyelination in spared axons after spinal cord injury in a mouse. J Neurosci 2008; 28: 3887-3896.
    • (2008) J Neurosci , vol.28 , pp. 3887-3896
    • Lasiene, J.1    Shupe, L.2    Perlmutter, S.3    Horner, P.4
  • 24
    • 17844400031 scopus 로고    scopus 로고
    • An adult rat spinal cord contusion model of sensory axon degeneration: The estrus cycle or a preconditioning lesion do not affect outcome
    • Baker KA, Hagg T,. An adult rat spinal cord contusion model of sensory axon degeneration: the estrus cycle or a preconditioning lesion do not affect outcome. J Neurotrauma 2005; 22: 415-428.
    • (2005) J Neurotrauma , vol.22 , pp. 415-428
    • Baker, K.A.1    Hagg, T.2
  • 25
    • 0030157694 scopus 로고    scopus 로고
    • Graded histological and locomotor outcomes after spinal cord contusion using the NYU weight-drop device versus transection
    • Basso DM, Beattie MS, Bresnahan JC,. Graded histological and locomotor outcomes after spinal cord contusion using the NYU weight-drop device versus transection. Exp Neurol 1996; 139: 244-256.
    • (1996) Exp Neurol , vol.139 , pp. 244-256
    • Basso, D.M.1    Beattie, M.S.2    Bresnahan, J.C.3
  • 26
    • 77649160197 scopus 로고    scopus 로고
    • Comparison of immunopathology and locomotor recovery in C57BL/6, BUB/BnJ, and NOD-SCID mice after contusion spinal cord injury
    • Luchetti S, Beck KD, Galvan MD, et al. Comparison of immunopathology and locomotor recovery in C57BL/6, BUB/BnJ, and NOD-SCID mice after contusion spinal cord injury. J Neurotrauma 2010; 27: 411-421.
    • (2010) J Neurotrauma , vol.27 , pp. 411-421
    • Luchetti, S.1    Beck, K.D.2    Galvan, M.D.3
  • 27
    • 12544251257 scopus 로고    scopus 로고
    • Voluntary wheel running improves recovery from a moderate spinal cord injury
    • Engesser-Cesar C, Anderson AJ, Basso DM, et al. Voluntary wheel running improves recovery from a moderate spinal cord injury. J Neurotrauma 2005; 22: 157-171.
    • (2005) J Neurotrauma , vol.22 , pp. 157-171
    • Engesser-Cesar, C.1    Anderson, A.J.2    Basso, D.M.3
  • 28
    • 3242742080 scopus 로고    scopus 로고
    • Upregulation of annexins I, II, and v after traumatic spinal cord injury in adult rats
    • Liu N, Han S, Lu PH, Xu XM,. Upregulation of annexins I, II, and V after traumatic spinal cord injury in adult rats. J Neurosci Res 2004; 77: 391-401.
    • (2004) J Neurosci Res , vol.77 , pp. 391-401
    • Liu, N.1    Han, S.2    Lu, P.H.3    Xu, X.M.4
  • 29
    • 1242293632 scopus 로고    scopus 로고
    • Cytosolic phospholipase A2 plays a key role in the pathogenesis of multiple sclerosis-like disease
    • Kalyvas A, David S,. Cytosolic phospholipase A2 plays a key role in the pathogenesis of multiple sclerosis-like disease. Neuron 2004; 41: 323-335.
    • (2004) Neuron , vol.41 , pp. 323-335
    • Kalyvas, A.1    David, S.2
  • 30
    • 33645983692 scopus 로고    scopus 로고
    • Basso Mouse Scale for locomotion detects differences in recovery after spinal cord injury in five common mouse strains
    • Basso DM, Fisher LC, Anderson AJ, et al. Basso Mouse Scale for locomotion detects differences in recovery after spinal cord injury in five common mouse strains. J Neurotrauma 2006; 23: 635-659.
    • (2006) J Neurotrauma , vol.23 , pp. 635-659
    • Basso, D.M.1    Fisher, L.C.2    Anderson, A.J.3
  • 31
    • 59849088007 scopus 로고    scopus 로고
    • Anatomical and functional outcomes following a precise, graded, dorsal laceration spinal cord injury in C57BL/6 mice
    • Hill RL, Zhang YP, Burke DA, et al. Anatomical and functional outcomes following a precise, graded, dorsal laceration spinal cord injury in C57BL/6 mice. J Neurotrauma 2009; 26: 1-15.
    • (2009) J Neurotrauma , vol.26 , pp. 1-15
    • Hill, R.L.1    Zhang, Y.P.2    Burke, D.A.3
  • 33
    • 0017843399 scopus 로고
    • Purification from brain of an intrinsic membrane protein fraction enriched in (Na+ + K+)-ATPase
    • Sweadner KJ,. Purification from brain of an intrinsic membrane protein fraction enriched in (Na+ + K+)-ATPase. Biochim Biophys Acta 1978; 508: 486-499.
    • (1978) Biochim Biophys Acta , vol.508 , pp. 486-499
    • Sweadner, K.J.1
  • 34
    • 0023802003 scopus 로고
    • ATPase and phosphatase activity of Na+,K+-ATPase: Molar and specific activity, protein determination
    • Esmann M,. ATPase and phosphatase activity of Na+,K+-ATPase: molar and specific activity, protein determination. Methods Enzymol 1988; 156: 105-115.
    • (1988) Methods Enzymol , vol.156 , pp. 105-115
    • Esmann, M.1
  • 35
    • 0037561933 scopus 로고    scopus 로고
    • Ca2+-independent phospholipase A2 is a novel determinant of store-operated Ca2+ entry
    • Smani T, Zakharov SI, Leno E, et al. Ca2+-independent phospholipase A2 is a novel determinant of store-operated Ca2+ entry. J Biol Chem 2003; 278: 11909-11915.
    • (2003) J Biol Chem , vol.278 , pp. 11909-11915
    • Smani, T.1    Zakharov, S.I.2    Leno, E.3
  • 36
    • 0029152947 scopus 로고
    • A natural disruption of the secretory group II phospholipase A2 gene in inbred mouse strains
    • Kennedy BP, Payette P, Mudgett J, et al. A natural disruption of the secretory group II phospholipase A2 gene in inbred mouse strains. J Biol Chem 1995; 270: 22378-22385.
    • (1995) J Biol Chem , vol.270 , pp. 22378-22385
    • Kennedy, B.P.1    Payette, P.2    Mudgett, J.3
  • 37
    • 12144287654 scopus 로고    scopus 로고
    • Ceramide 1-phosphate is a direct activator of cytosolic phospholipase A2
    • Pettus BJ, Bielawska A, Subramanian P, et al. Ceramide 1-phosphate is a direct activator of cytosolic phospholipase A2. J Biol Chem 2004; 279: 11320-11326.
    • (2004) J Biol Chem , vol.279 , pp. 11320-11326
    • Pettus, B.J.1    Bielawska, A.2    Subramanian, P.3
  • 38
    • 77950625075 scopus 로고    scopus 로고
    • Modulation of the activity of cytosolic phospholipase A2alpha (cPLA2alpha) by cellular sphingolipids and inhibition of cPLA2alpha by sphingomyelin
    • Nakamura H, Wakita S, Suganami A, et al. Modulation of the activity of cytosolic phospholipase A2alpha (cPLA2alpha) by cellular sphingolipids and inhibition of cPLA2alpha by sphingomyelin. J Lipid Res 2010; 51: 720-728.
    • (2010) J Lipid Res , vol.51 , pp. 720-728
    • Nakamura, H.1    Wakita, S.2    Suganami, A.3
  • 39
    • 0027314633 scopus 로고
    • Slow- and tight-binding inhibitors of the 85-kDa human phospholipase A2
    • Street IP, Lin HK, Laliberte F, et al. Slow- and tight-binding inhibitors of the 85-kDa human phospholipase A2. Biochemistry 1993; 32: 5935-5940.
    • (1993) Biochemistry , vol.32 , pp. 5935-5940
    • Street, I.P.1    Lin, H.K.2    Laliberte, F.3
  • 40
    • 0027131849 scopus 로고
    • NMR structural studies of the tight complex between a trifluoromethyl ketone inhibitor and the 85-kDa human phospholipase A2
    • Trimble LA, Street IP, Perrier H, et al. NMR structural studies of the tight complex between a trifluoromethyl ketone inhibitor and the 85-kDa human phospholipase A2. Biochemistry 1993; 32: 12560-12565.
    • (1993) Biochemistry , vol.32 , pp. 12560-12565
    • Trimble, L.A.1    Street, I.P.2    Perrier, H.3
  • 41
    • 0028272107 scopus 로고
    • Arachidonyl trifluoromethyl ketone, a potent inhibitor of 85-kDa phospholipase A2, blocks production of arachidonate and 12- hydroxyeicosatetraenoic acid by calcium ionophore-challenged platelets
    • Riendeau D, Guay J, Weech PK, et al. Arachidonyl trifluoromethyl ketone, a potent inhibitor of 85-kDa phospholipase A2, blocks production of arachidonate and 12-hydroxyeicosatetraenoic acid by calcium ionophore-challenged platelets. J Biol Chem 1994; 269: 15619-15624.
    • (1994) J Biol Chem , vol.269 , pp. 15619-15624
    • Riendeau, D.1    Guay, J.2    Weech, P.K.3
  • 42
    • 0028985263 scopus 로고
    • Inhibition of macrophage Ca(2+)-independent phospholipase A2 by bromoenol lactone and trifluoromethyl ketones
    • Ackermann EJ, Conde-Frieboes K, Dennis EA,. Inhibition of macrophage Ca(2+)-independent phospholipase A2 by bromoenol lactone and trifluoromethyl ketones. J Biol Chem 1995; 270: 445-450.
    • (1995) J Biol Chem , vol.270 , pp. 445-450
    • Ackermann, E.J.1    Conde-Frieboes, K.2    Dennis, E.A.3
  • 43
    • 0032794186 scopus 로고    scopus 로고
    • Trifluoromethyl ketones and methyl fluorophosphonates as inhibitors of group IV and VI phospholipases A(2): Structure-function studies with vesicle, micelle, and membrane assays
    • Ghomashchi F, Loo R, Balsinde J, et al. Trifluoromethyl ketones and methyl fluorophosphonates as inhibitors of group IV and VI phospholipases A(2): structure-function studies with vesicle, micelle, and membrane assays. Biochim Biophys Acta 1999; 1420: 45-56.
    • (1999) Biochim Biophys Acta , vol.1420 , pp. 45-56
    • Ghomashchi, F.1    Loo, R.2    Balsinde, J.3
  • 44
    • 0032790541 scopus 로고    scopus 로고
    • Activation of the caspase-3 apoptotic cascade in traumatic spinal cord injury
    • Springer JE, Azbill RD, Knapp PE,. Activation of the caspase-3 apoptotic cascade in traumatic spinal cord injury. Nat Med 1999; 5: 943-946.
    • (1999) Nat Med , vol.5 , pp. 943-946
    • Springer, J.E.1    Azbill, R.D.2    Knapp, P.E.3
  • 45
    • 0023613493 scopus 로고
    • Early membrane lipid changes in laminectomized and traumatized cat spinal cord
    • Demediuk P, Saunders RD, Anderson DK, et al. Early membrane lipid changes in laminectomized and traumatized cat spinal cord. Neurochem Pathol 1987; 7: 79-89.
    • (1987) Neurochem Pathol , vol.7 , pp. 79-89
    • Demediuk, P.1    Saunders, R.D.2    Anderson, D.K.3
  • 46
    • 0011895769 scopus 로고
    • Membrane lipid changes in laminectomized and traumatized cat spinal cord
    • Demediuk P, Saunders RD, Anderson DK, et al. Membrane lipid changes in laminectomized and traumatized cat spinal cord. Proc Natl Acad Sci U S A 1985; 82: 7071-7075.
    • (1985) Proc Natl Acad Sci U S A , vol.82 , pp. 7071-7075
    • Demediuk, P.1    Saunders, R.D.2    Anderson, D.K.3
  • 47
    • 0035851791 scopus 로고    scopus 로고
    • Regional and temporal changes in prostaglandin E2 and thromboxane B2 concentrations after spinal cord injury
    • Resnick DK, Nguyen P, Cechvala CF,. Regional and temporal changes in prostaglandin E2 and thromboxane B2 concentrations after spinal cord injury. Spine J 2001; 1: 432-436.
    • (2001) Spine J , vol.1 , pp. 432-436
    • Resnick, D.K.1    Nguyen, P.2    Cechvala, C.F.3
  • 48
    • 0024321192 scopus 로고
    • Changes in free fatty acids, phospholipids, and cholesterol following impact injury to the rat spinal cord
    • Demediuk P, Daly MP, Faden AI,. Changes in free fatty acids, phospholipids, and cholesterol following impact injury to the rat spinal cord. J Neurosci Res 1989; 23: 95-106.
    • (1989) J Neurosci Res , vol.23 , pp. 95-106
    • Demediuk, P.1    Daly, M.P.2    Faden, A.I.3
  • 49
    • 16944363478 scopus 로고    scopus 로고
    • Neuronal and glial apoptosis after traumatic spinal cord injury
    • Liu XZ, Xu XM, Hu R, et al. Neuronal and glial apoptosis after traumatic spinal cord injury. J Neurosci 1997; 17: 5395-5406.
    • (1997) J Neurosci , vol.17 , pp. 5395-5406
    • Liu, X.Z.1    Xu, X.M.2    Hu, R.3
  • 50
    • 0031015075 scopus 로고    scopus 로고
    • Apoptosis and delayed degeneration after spinal cord injury in rats and monkeys
    • Crowe MJ, Bresnahan JC, Shuman SL, et al. Apoptosis and delayed degeneration after spinal cord injury in rats and monkeys. Nat Med 1997; 3: 73-76.
    • (1997) Nat Med , vol.3 , pp. 73-76
    • Crowe, M.J.1    Bresnahan, J.C.2    Shuman, S.L.3
  • 51
    • 19944428712 scopus 로고    scopus 로고
    • Cytosolic phospholipase A2 mediates neuronal apoptosis induced by soluble oligomers of the amyloid-beta peptide
    • Kriem B, Sponne I, Fifre A, et al. Cytosolic phospholipase A2 mediates neuronal apoptosis induced by soluble oligomers of the amyloid-beta peptide. FASEB J 2005; 19: 85-87.
    • (2005) FASEB J , vol.19 , pp. 85-87
    • Kriem, B.1    Sponne, I.2    Fifre, A.3
  • 52
    • 1442328269 scopus 로고    scopus 로고
    • Mice deficient in cytosolic phospholipase A2 are less susceptible to cerebral ischemia/reperfusion injury
    • Tabuchi S, Uozumi N, Ishii S, et al. Mice deficient in cytosolic phospholipase A2 are less susceptible to cerebral ischemia/reperfusion injury. Acta Neurochir Suppl 2003; 86: 169-172.
    • (2003) Acta Neurochir Suppl , vol.86 , pp. 169-172
    • Tabuchi, S.1    Uozumi, N.2    Ishii, S.3
  • 53
    • 25144519259 scopus 로고    scopus 로고
    • Cytosolic phospholipase A2 alpha-deficient mice are resistant to experimental autoimmune encephalomyelitis
    • Marusic S, Leach MW, Pelker JW, et al. Cytosolic phospholipase A2 alpha-deficient mice are resistant to experimental autoimmune encephalomyelitis. J Exp Med 2005; 202: 841-851.
    • (2005) J Exp Med , vol.202 , pp. 841-851
    • Marusic, S.1    Leach, M.W.2    Pelker, J.W.3
  • 54
    • 54949130109 scopus 로고    scopus 로고
    • Phospholipase A2 reduction ameliorates cognitive deficits in a mouse model of Alzheimer's disease
    • Sanchez-Mejia RO, Newman JW, Toh S, et al. Phospholipase A2 reduction ameliorates cognitive deficits in a mouse model of Alzheimer's disease. Nat Neurosci 2008; 11: 1311-1318.
    • (2008) Nat Neurosci , vol.11 , pp. 1311-1318
    • Sanchez-Mejia, R.O.1    Newman, J.W.2    Toh, S.3
  • 55
    • 30144445614 scopus 로고    scopus 로고
    • Comparative analysis of lesion development and intraspinal inflammation in four strains of mice following spinal contusion injury
    • Kigerl KA, McGaughy VM, Popovich PG,. Comparative analysis of lesion development and intraspinal inflammation in four strains of mice following spinal contusion injury. J Comp Neurol 2006; 494: 578-594.
    • (2006) J Comp Neurol , vol.494 , pp. 578-594
    • Kigerl, K.A.1    McGaughy, V.M.2    Popovich, P.G.3
  • 56
    • 0037163431 scopus 로고    scopus 로고
    • Genetic influences on secondary degeneration and wound healing following spinal cord injury in various strains of mice
    • Inman D, Guth L, Steward O,. Genetic influences on secondary degeneration and wound healing following spinal cord injury in various strains of mice. J Comp Neurol 2002; 451: 225-235.
    • (2002) J Comp Neurol , vol.451 , pp. 225-235
    • Inman, D.1    Guth, L.2    Steward, O.3
  • 57
    • 0035400122 scopus 로고    scopus 로고
    • Neuronal survival after CNS insult is determined by a genetically encoded autoimmune response
    • Kipnis J, Yoles E, Schori H, et al. Neuronal survival after CNS insult is determined by a genetically encoded autoimmune response. J Neurosci 2001; 21: 4564-4571.
    • (2001) J Neurosci , vol.21 , pp. 4564-4571
    • Kipnis, J.1    Yoles, E.2    Schori, H.3
  • 58
    • 0031741666 scopus 로고    scopus 로고
    • Mice deficient in group IV cytosolic phospholipase A2 are resistant to MPTP neurotoxicity
    • Klivenyi P, Beal MF, Ferrante RJ, et al. Mice deficient in group IV cytosolic phospholipase A2 are resistant to MPTP neurotoxicity. J Neurochem 1998; 71: 2634-2637.
    • (1998) J Neurochem , vol.71 , pp. 2634-2637
    • Klivenyi, P.1    Beal, M.F.2    Ferrante, R.J.3
  • 59
    • 0033623894 scopus 로고    scopus 로고
    • Phospholipases A2 in ischemic and toxic brain injury
    • Sapirstein A, Bonventre JV,. Phospholipases A2 in ischemic and toxic brain injury. Neurochem Res 2000; 25: 745-753.
    • (2000) Neurochem Res , vol.25 , pp. 745-753
    • Sapirstein, A.1    Bonventre, J.V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.