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Volumn 78, Issue 1, 2009, Pages 33-39

Calpain-1 induces apoptosis in pulmonary microvascular endothelial cells under septic conditions

Author keywords

Apoptosis; Calpain; Calpastatin; Endothelial cells; NADPH oxidase; Sepsis

Indexed keywords

CALPAIN 1; CALPAIN 2; CALPASTATIN; CASPASE 3; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; SMALL INTERFERING RNA;

EID: 67349170024     PISSN: 00262862     EISSN: 10959319     Source Type: Journal    
DOI: 10.1016/j.mvr.2009.04.005     Document Type: Article
Times cited : (41)

References (38)
  • 1
    • 0033567878 scopus 로고    scopus 로고
    • Association of calpain (Ca(2+)-dependent thiol protease) with its endogenous inhibitor calpastatin in myoblasts
    • Barnoy S., Zipser Y., Glaser T., Grimberg Y., and Kosower N.S. Association of calpain (Ca(2+)-dependent thiol protease) with its endogenous inhibitor calpastatin in myoblasts. J. Cell. Biochem. 74 (1999) 522-531
    • (1999) J. Cell. Biochem. , vol.74 , pp. 522-531
    • Barnoy, S.1    Zipser, Y.2    Glaser, T.3    Grimberg, Y.4    Kosower, N.S.5
  • 2
    • 51449107134 scopus 로고    scopus 로고
    • Lipopolysaccharide plus hypoxia and reoxygenation synergistically reduce electrical coupling between microvascular endothelial cells by dephosphorylating connexin40
    • Bolon M.L., Peng T., Kidder G.M., and Tyml K. Lipopolysaccharide plus hypoxia and reoxygenation synergistically reduce electrical coupling between microvascular endothelial cells by dephosphorylating connexin40. J. Cell. Physiol. 217 (2008) 350-359
    • (2008) J. Cell. Physiol. , vol.217 , pp. 350-359
    • Bolon, M.L.1    Peng, T.2    Kidder, G.M.3    Tyml, K.4
  • 3
    • 1542541983 scopus 로고    scopus 로고
    • Modulation of endotoxin-induced endothelial function by calcium/calmodulin-dependent protein kinase
    • Cuschieri J., Gourlay D., Garcia I., Jelacic S., and Maier R.V. Modulation of endotoxin-induced endothelial function by calcium/calmodulin-dependent protein kinase. Shock 20 (2003) 176-182
    • (2003) Shock , vol.20 , pp. 176-182
    • Cuschieri, J.1    Gourlay, D.2    Garcia, I.3    Jelacic, S.4    Maier, R.V.5
  • 5
    • 53649092912 scopus 로고    scopus 로고
    • Alveolar macrophage inducible nitric oxide synthase-dependent pulmonary microvascular endothelial cell septic barrier dysfunction
    • Farley K.S., Wang L.F., Law C., and Mehta S. Alveolar macrophage inducible nitric oxide synthase-dependent pulmonary microvascular endothelial cell septic barrier dysfunction. Microvasc. Res. 76 (2008) 208-216
    • (2008) Microvasc. Res. , vol.76 , pp. 208-216
    • Farley, K.S.1    Wang, L.F.2    Law, C.3    Mehta, S.4
  • 6
    • 0037072469 scopus 로고    scopus 로고
    • Development of heart failure and congenital septal defects in mice lacking endothelial nitric oxide synthase
    • Feng Q., Song W., Lu X., Hamilton J.A., Lei M., Peng T., and Yee S.P. Development of heart failure and congenital septal defects in mice lacking endothelial nitric oxide synthase. Circulation 106 (2002) 873-879
    • (2002) Circulation , vol.106 , pp. 873-879
    • Feng, Q.1    Song, W.2    Lu, X.3    Hamilton, J.A.4    Lei, M.5    Peng, T.6    Yee, S.P.7
  • 7
    • 33947158300 scopus 로고    scopus 로고
    • Septic plasma-induced oxidative stress in endothelial cells: a sensitive bioassay predicting outcome in septic shock?
    • Filep J.G. Septic plasma-induced oxidative stress in endothelial cells: a sensitive bioassay predicting outcome in septic shock?. Crit. Care Med. 35 (2007) 967-968
    • (2007) Crit. Care Med. , vol.35 , pp. 967-968
    • Filep, J.G.1
  • 8
    • 0037090069 scopus 로고    scopus 로고
    • Role of NADPH oxidase in the mechanism of lung neutrophil sequestration and microvessel injury induced by Gram-negative sepsis: studies in p47phox-/- and gp91phox-/- mice
    • Gao X.P., Standiford T.J., Rahman A., Newstead M., Holland S.M., Dinauer M.C., Liu Q.H., and Malik A.B. Role of NADPH oxidase in the mechanism of lung neutrophil sequestration and microvessel injury induced by Gram-negative sepsis: studies in p47phox-/- and gp91phox-/- mice. J. Immunol. 168 (2002) 3974-3982
    • (2002) J. Immunol. , vol.168 , pp. 3974-3982
    • Gao, X.P.1    Standiford, T.J.2    Rahman, A.3    Newstead, M.4    Holland, S.M.5    Dinauer, M.C.6    Liu, Q.H.7    Malik, A.B.8
  • 11
    • 34547190160 scopus 로고    scopus 로고
    • Cytokine profile of human septic shock serum inducing cardiomyocyte contractile dysfunction
    • Joulin O., Petillot P., Labalette M., Lancel S., and Neviere R. Cytokine profile of human septic shock serum inducing cardiomyocyte contractile dysfunction. Physiol. Res. 56 (2007) 291-297
    • (2007) Physiol. Res. , vol.56 , pp. 291-297
    • Joulin, O.1    Petillot, P.2    Labalette, M.3    Lancel, S.4    Neviere, R.5
  • 12
    • 0033873787 scopus 로고    scopus 로고
    • Protection from lethal apoptosis in lipopolysaccharide-induced acute lung injury in mice by a caspase inhibitor
    • Kawasaki M., Kuwano K., Hagimoto N., Matsuba T., Kunitake R., Tanaka T., Maeyama T., and Hara N. Protection from lethal apoptosis in lipopolysaccharide-induced acute lung injury in mice by a caspase inhibitor. Am. J. Pathol. 157 (2000) 597-603
    • (2000) Am. J. Pathol. , vol.157 , pp. 597-603
    • Kawasaki, M.1    Kuwano, K.2    Hagimoto, N.3    Matsuba, T.4    Kunitake, R.5    Tanaka, T.6    Maeyama, T.7    Hara, N.8
  • 13
    • 0942265562 scopus 로고    scopus 로고
    • Requirement of protein kinase C micro activation and calpain-mediated proteolysis for arachidonic acid-stimulated adhesion of MDA-MB-435 human mammary carcinoma cells to collagen type IV
    • Kennett S.B., Roberts J.D., and Olden K. Requirement of protein kinase C micro activation and calpain-mediated proteolysis for arachidonic acid-stimulated adhesion of MDA-MB-435 human mammary carcinoma cells to collagen type IV. J. Biol. Chem. 279 (2004) 3300-3307
    • (2004) J. Biol. Chem. , vol.279 , pp. 3300-3307
    • Kennett, S.B.1    Roberts, J.D.2    Olden, K.3
  • 14
    • 33751060765 scopus 로고    scopus 로고
    • Involvement of nitric oxide synthase and ROS-mediated activation of L-type voltage-gated Ca2+ channels in NMDA-induced DPYSL3 degradation
    • Kowara R., Moraleja K.L., and Chakravarthy B. Involvement of nitric oxide synthase and ROS-mediated activation of L-type voltage-gated Ca2+ channels in NMDA-induced DPYSL3 degradation. Brain Res. 1119 (2006) 40-49
    • (2006) Brain Res. , vol.1119 , pp. 40-49
    • Kowara, R.1    Moraleja, K.L.2    Chakravarthy, B.3
  • 15
    • 20444388435 scopus 로고    scopus 로고
    • Tezosentan-induced attenuation of lung injury in endotoxemic sheep is associated with reduced activation of protein kinase C
    • Kuklin V., Kirov M., Sovershaev M., Andreasen T., Ingebretsen O.C., Ytrehus K., and Bjertnaes L. Tezosentan-induced attenuation of lung injury in endotoxemic sheep is associated with reduced activation of protein kinase C. Crit. Care 9 (2005) R211-R217
    • (2005) Crit. Care , vol.9
    • Kuklin, V.1    Kirov, M.2    Sovershaev, M.3    Andreasen, T.4    Ingebretsen, O.C.5    Ytrehus, K.6    Bjertnaes, L.7
  • 16
    • 41449084770 scopus 로고    scopus 로고
    • Targeting the calpain/calpastatin system as a new strategy to prevent cardiovascular remodeling in angiotensin II-induced hypertension
    • Letavernier E., Perez J., Bellocq A., Mesnard L., de Castro Keller A., Haymann J.P., and Baud L. Targeting the calpain/calpastatin system as a new strategy to prevent cardiovascular remodeling in angiotensin II-induced hypertension. Circ. Res. 102 (2008) 720-728
    • (2008) Circ. Res. , vol.102 , pp. 720-728
    • Letavernier, E.1    Perez, J.2    Bellocq, A.3    Mesnard, L.4    de Castro Keller, A.5    Haymann, J.P.6    Baud, L.7
  • 17
    • 34547813240 scopus 로고    scopus 로고
    • Nox2 regulates endothelial cell cycle arrest and apoptosis via p21cip1 and p53
    • Li J.M., Fan L.M., George V.T., and Brooks G. Nox2 regulates endothelial cell cycle arrest and apoptosis via p21cip1 and p53. Free Radic. Biol. Med. 43 (2007) 976-986
    • (2007) Free Radic. Biol. Med. , vol.43 , pp. 976-986
    • Li, J.M.1    Fan, L.M.2    George, V.T.3    Brooks, G.4
  • 19
    • 57449119867 scopus 로고    scopus 로고
    • Taurine prevents cardiomyocyte death by inhibiting NADPH oxidase-mediated calpain activation
    • Li Y., Arnold J.M.O., Pampillo M., Babwah A.V., and Peng T. Taurine prevents cardiomyocyte death by inhibiting NADPH oxidase-mediated calpain activation. Free Radic. Biol. Med. 46 (2009) 51-61
    • (2009) Free Radic. Biol. Med. , vol.46 , pp. 51-61
    • Li, Y.1    Arnold, J.M.O.2    Pampillo, M.3    Babwah, A.V.4    Peng, T.5
  • 20
    • 1842863228 scopus 로고    scopus 로고
    • Cardiac myocytes activated by septic plasma promote neutrophil transendothelial migration: role of platelet-activating factor and the chemokines LIX and KC
    • Madorin W.S., Rui T., Sugimoto N., Handa O., Cepinskas G., and Kvietys P.R. Cardiac myocytes activated by septic plasma promote neutrophil transendothelial migration: role of platelet-activating factor and the chemokines LIX and KC. Circ. Res. 94 (2004) 944-951
    • (2004) Circ. Res. , vol.94 , pp. 944-951
    • Madorin, W.S.1    Rui, T.2    Sugimoto, N.3    Handa, O.4    Cepinskas, G.5    Kvietys, P.R.6
  • 21
    • 34548432210 scopus 로고    scopus 로고
    • Silencing of caspase-8 and caspase-3 by RNA interference prevents vascular endothelial cell injury in mice with endotoxic shock
    • Matsuda N., Takano Y., Kageyama S., Hatakeyama N., Shakunaga K., Kitajima I., Yamazaki M., and Hattori Y. Silencing of caspase-8 and caspase-3 by RNA interference prevents vascular endothelial cell injury in mice with endotoxic shock. Cardiovasc. Res. 76 (2007) 132-140
    • (2007) Cardiovasc. Res. , vol.76 , pp. 132-140
    • Matsuda, N.1    Takano, Y.2    Kageyama, S.3    Hatakeyama, N.4    Shakunaga, K.5    Kitajima, I.6    Yamazaki, M.7    Hattori, Y.8
  • 22
    • 0037648485 scopus 로고    scopus 로고
    • Cross-talk between calpain and caspase proteolytic systems during neuronal apoptosis
    • Neumar R.W., Xu Y.A., Gada H., Guttmann R.P., and Siman R. Cross-talk between calpain and caspase proteolytic systems during neuronal apoptosis. J. Biol. Chem. 278 (2003) 14162-14167
    • (2003) J. Biol. Chem. , vol.278 , pp. 14162-14167
    • Neumar, R.W.1    Xu, Y.A.2    Gada, H.3    Guttmann, R.P.4    Siman, R.5
  • 25
    • 4544326749 scopus 로고    scopus 로고
    • Oxidative stress-induced apoptosis in retinal photoreceptor cells is mediated by calpains and caspases and blocked by the oxygen radical scavenger CR-6
    • Sanvicens N., Go'mez-Vicente V., Masip I., Messeguer A., and Cotter T.G. Oxidative stress-induced apoptosis in retinal photoreceptor cells is mediated by calpains and caspases and blocked by the oxygen radical scavenger CR-6. J. Biol. Chem. 279 (2004) 39268-39278
    • (2004) J. Biol. Chem. , vol.279 , pp. 39268-39278
    • Sanvicens, N.1    Go'mez-Vicente, V.2    Masip, I.3    Messeguer, A.4    Cotter, T.G.5
  • 26
    • 34548133145 scopus 로고    scopus 로고
    • Phospholipase Cgamma1 signalling regulates lipopolysaccharide-induced cyclooxygenase-2 expression in cardiomyocytes
    • Shen E., Fan J., Chen R., Yee S.P., and Peng T. Phospholipase Cgamma1 signalling regulates lipopolysaccharide-induced cyclooxygenase-2 expression in cardiomyocytes. J. Mol. Cell. Cardiol. 43 (2007) 308-318
    • (2007) J. Mol. Cell. Cardiol. , vol.43 , pp. 308-318
    • Shen, E.1    Fan, J.2    Chen, R.3    Yee, S.P.4    Peng, T.5
  • 27
    • 1442335807 scopus 로고    scopus 로고
    • Remnant lipoprotein particles induce apoptosis in endothelial cells by NAD(P)H oxidase-mediated production of superoxide and cytokines via lectin-like oxidized low-density lipoprotein receptor-1 activation: prevention by cilostazol
    • Shin H.K., Kim Y.K., Kim K.Y., Lee J.H., and Hong K.W. Remnant lipoprotein particles induce apoptosis in endothelial cells by NAD(P)H oxidase-mediated production of superoxide and cytokines via lectin-like oxidized low-density lipoprotein receptor-1 activation: prevention by cilostazol. Circulation 109 (2004) 1022-1028
    • (2004) Circulation , vol.109 , pp. 1022-1028
    • Shin, H.K.1    Kim, Y.K.2    Kim, K.Y.3    Lee, J.H.4    Hong, K.W.5
  • 28
    • 0036207773 scopus 로고    scopus 로고
    • Activation of m-calpain (calpain II) by epidermal growth factor is limited by protein kinase A phosphorylation of m-calpain
    • Shiraha H., Glading A., Chou J., Jia Z., and Wells A. Activation of m-calpain (calpain II) by epidermal growth factor is limited by protein kinase A phosphorylation of m-calpain. Mol. Cell. Biol. 22 (2002) 2716-2727
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 2716-2727
    • Shiraha, H.1    Glading, A.2    Chou, J.3    Jia, Z.4    Wells, A.5
  • 29
    • 0030183965 scopus 로고    scopus 로고
    • Acute lung injury in endotoxemic rats is associated with sustained circulating IL-6 levels and intrapulmonary CINC activity and neutrophil recruitment-role of circulating TNF-alpha and IL-beta?
    • Simons R.K., Junger W.G., Loomis W.H., and Hoyt D.B. Acute lung injury in endotoxemic rats is associated with sustained circulating IL-6 levels and intrapulmonary CINC activity and neutrophil recruitment-role of circulating TNF-alpha and IL-beta?. Shock 6 (1996) 39-45
    • (1996) Shock , vol.6 , pp. 39-45
    • Simons, R.K.1    Junger, W.G.2    Loomis, W.H.3    Hoyt, D.B.4
  • 30
    • 0034102920 scopus 로고    scopus 로고
    • Endothelial apoptosis: could it have a role in the pathogenesis and treatment of disease?
    • Stefanec T. Endothelial apoptosis: could it have a role in the pathogenesis and treatment of disease?. Chest 117 (2000) 841-854
    • (2000) Chest , vol.117 , pp. 841-854
    • Stefanec, T.1
  • 31
    • 33745826605 scopus 로고    scopus 로고
    • Ubiquitous calpains promote both apoptosis and survival signals in response to different cell death stimuli
    • Tan Y., Wu C., De Veyra T., and Greer P.A. Ubiquitous calpains promote both apoptosis and survival signals in response to different cell death stimuli. J. Biol. Chem. 281 (2006) 17689-17698
    • (2006) J. Biol. Chem. , vol.281 , pp. 17689-17698
    • Tan, Y.1    Wu, C.2    De Veyra, T.3    Greer, P.A.4
  • 32
    • 0033569660 scopus 로고    scopus 로고
    • Changes in intracellular localization of calpastatin during calpain activation
    • Tullio R.D., Passalacqua M., Averna M., Salamino F., Melloni E., and Pontremoli S. Changes in intracellular localization of calpastatin during calpain activation. Biochem. J. 343 Pt 2 (1999) 467-472
    • (1999) Biochem. J. , vol.343 , Issue.PART 2 , pp. 467-472
    • Tullio, R.D.1    Passalacqua, M.2    Averna, M.3    Salamino, F.4    Melloni, E.5    Pontremoli, S.6
  • 33
    • 0029043888 scopus 로고
    • A novel assay for apoptosis. Flow cytometric detection of phosphatidylserine expression on early apoptotic cells using fluorescein labelled Annexin V.
    • Vermes I., Haanen C., Steffens-Nakken H., and Reutelingsperger C. A novel assay for apoptosis. Flow cytometric detection of phosphatidylserine expression on early apoptotic cells using fluorescein labelled Annexin V. J. Immunol. Methods 184 (1995) 39-51
    • (1995) J. Immunol. Methods , vol.184 , pp. 39-51
    • Vermes, I.1    Haanen, C.2    Steffens-Nakken, H.3    Reutelingsperger, C.4
  • 35
  • 37
    • 34247588117 scopus 로고    scopus 로고
    • Acute lung injury and the acute respiratory distress syndrome: a clinical review
    • Wheeler A.P., and Bernard G.R. Acute lung injury and the acute respiratory distress syndrome: a clinical review. Lancet 369 (2007) 1553-1564
    • (2007) Lancet , vol.369 , pp. 1553-1564
    • Wheeler, A.P.1    Bernard, G.R.2
  • 38
    • 4143071247 scopus 로고    scopus 로고
    • Effect of phosphatidylinositol and inside-out erythrocyte vesicles on autolysis of mu- and m-calpain from bovine skeletal muscle
    • Zalewska T., Thompson V.F., and Goll D.E. Effect of phosphatidylinositol and inside-out erythrocyte vesicles on autolysis of mu- and m-calpain from bovine skeletal muscle. Biochim. Biophys. Acta 1693 (2004) 125-133
    • (2004) Biochim. Biophys. Acta , vol.1693 , pp. 125-133
    • Zalewska, T.1    Thompson, V.F.2    Goll, D.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.