메뉴 건너뛰기




Volumn 5, Issue 7, 2006, Pages 1300-1313

Proteomic analysis of ischemia-reperfusion injury upon human liver transplantation reveals the protective role of IQGAP1

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; IQ MOTIF CONTAINING GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN 1; PHOSPHOPROTEIN; PROTEIN CDC42; RAC1 PROTEIN;

EID: 33746275653     PISSN: 15359476     EISSN: None     Source Type: Journal    
DOI: 10.1074/mcp.M500393-MCP200     Document Type: Article
Times cited : (32)

References (46)
  • 1
    • 24044467417 scopus 로고    scopus 로고
    • Update on post-liver transplantation infections, malignancies, and surgical complications
    • Washington, K. (2005) Update on post-liver transplantation infections, malignancies, and surgical complications. Adv. Anat. Pathol. 12, 221-226
    • (2005) Adv. Anat. Pathol. , vol.12 , pp. 221-226
    • Washington, K.1
  • 2
    • 0142186208 scopus 로고    scopus 로고
    • Intrahepatic cholestasis after liver transplantation
    • Ben-Ari, Z., Pappo, O., and Mor, E. (2003) Intrahepatic cholestasis after liver transplantation. Liver Transplant. 9, 1005-1018
    • (2003) Liver Transplant. , vol.9 , pp. 1005-1018
    • Ben-Ari, Z.1    Pappo, O.2    Mor, E.3
  • 3
    • 0025514092 scopus 로고
    • Characteristics of biliary lipid metabolism after liver transplantation
    • Ericzon, B. G., Eusufzai, S., Kubota, K., Einarsson, K., and Angelin, B. (1990) Characteristics of biliary lipid metabolism after liver transplantation. Hepatology 12, 1222-1228
    • (1990) Hepatology , vol.12 , pp. 1222-1228
    • Ericzon, B.G.1    Eusufzai, S.2    Kubota, K.3    Einarsson, K.4    Angelin, B.5
  • 4
    • 0032899635 scopus 로고    scopus 로고
    • Reorganization of cholangiocyte, membrane domains represents an early event in rat liver ischemia
    • Doctor, R. B., Dahl, R. H., Salter, K. D., and Fitz, J. G. (1999) Reorganization of cholangiocyte, membrane domains represents an early event in rat liver ischemia. Hepatology 29, 1364-1374
    • (1999) Hepatology , vol.29 , pp. 1364-1374
    • Doctor, R.B.1    Dahl, R.H.2    Salter, K.D.3    Fitz, J.G.4
  • 6
    • 0000752197 scopus 로고
    • Junctional complexes in various epithelia
    • Farquhar, M. G., and Palade, G. E. (1963) Junctional complexes in various epithelia. J. Cell Biol. 17, 375-412
    • (1963) J. Cell Biol. , vol.17 , pp. 375-412
    • Farquhar, M.G.1    Palade, G.E.2
  • 7
    • 0025986006 scopus 로고
    • Regional orientation of actin filaments in the pericanalicular cytoplasm of rat hepatocytes
    • Ishii, M., Washioka, H., Tonosaki, A., and Toyota, T. (1991) Regional orientation of actin filaments in the pericanalicular cytoplasm of rat hepatocytes. Gastroenterology 101, 1663-1672
    • (1991) Gastroenterology , vol.101 , pp. 1663-1672
    • Ishii, M.1    Washioka, H.2    Tonosaki, A.3    Toyota, T.4
  • 8
    • 0023427610 scopus 로고
    • Effects of cytochalasin and phalloidin on actin
    • Cooper, J. A. (1987) Effects of cytochalasin and phalloidin on actin. J. Cell Biol. 105, 1473-1478
    • (1987) J. Cell Biol. , vol.105 , pp. 1473-1478
    • Cooper, J.A.1
  • 9
    • 0025720142 scopus 로고
    • Motility of bile canaliculi in the living animal: Implications for bile flow
    • Watanabe, N., Tsukada, N., Smith, C. R., and Phillips, M. J. (1991) Motility of bile canaliculi in the living animal: implications for bile flow. J. Cell Biol. 113, 1069-1080
    • (1991) J. Cell Biol. , vol.113 , pp. 1069-1080
    • Watanabe, N.1    Tsukada, N.2    Smith, C.R.3    Phillips, M.J.4
  • 10
    • 0032209808 scopus 로고    scopus 로고
    • Microstructural changes of bile canaliculi in canine liver: The effect of cold ischemia-reperfusion in orthotopic liver transplantation
    • Yasui, H., Yoshimura, N., Kobayashi, Y., Ochiai, S., Matsuda, T., Takamatsu, T., and Oka, T. (1998) Microstructural changes of bile canaliculi in canine liver: the effect of cold ischemia-reperfusion in orthotopic liver transplantation. Transplant Proc. 30, 3754-3757
    • (1998) Transplant Proc. , vol.30 , pp. 3754-3757
    • Yasui, H.1    Yoshimura, N.2    Kobayashi, Y.3    Ochiai, S.4    Matsuda, T.5    Takamatsu, T.6    Oka, T.7
  • 11
    • 0034897983 scopus 로고    scopus 로고
    • Effect of ischemia-reperfusion on bile canalicular F-actin microfilaments in hepatocytes of human liver allograft: Image analysis by confocal laser scanning microscopy
    • Benkoel, L., Dodero, F., Hardwigsen, J., Campan, P., Botta-Fridlund, D., Lombardo, D., Le Treut, Y. P., and Chamlian, A. (2001) Effect of ischemia-reperfusion on bile canalicular F-actin microfilaments in hepatocytes of human liver allograft: image analysis by confocal laser scanning microscopy. Dig. Dis. Sci. 46, 1663-1667
    • (2001) Dig. Dis. Sci. , vol.46 , pp. 1663-1667
    • Benkoel, L.1    Dodero, F.2    Hardwigsen, J.3    Campan, P.4    Botta-Fridlund, D.5    Lombardo, D.6    Le Treut, Y.P.7    Chamlian, A.8
  • 12
    • 0033055564 scopus 로고    scopus 로고
    • Detergent-insoluble glycosphingolipid/cholesterolrich membrane domains, lipid rafts and caveolae (review)
    • Hooper, N. M. (1999) Detergent-insoluble glycosphingolipid/ cholesterolrich membrane domains, lipid rafts and caveolae (review). Mol. Membr. Biol. 16, 145-156
    • (1999) Mol. Membr. Biol. , vol.16 , pp. 145-156
    • Hooper, N.M.1
  • 13
    • 23944437417 scopus 로고    scopus 로고
    • Distinct endoplasmic reticulum stress responses are triggered during human liver transplantation
    • Emadali, A., Nguyen, D. T., Rochon, C., Tzimas, G. N., Metrakos, P. P., and Chevet, E. (2005) Distinct endoplasmic reticulum stress responses are triggered during human liver transplantation. J. Pathol. 207, 111-118
    • (2005) J. Pathol. , vol.207 , pp. 111-118
    • Emadali, A.1    Nguyen, D.T.2    Rochon, C.3    Tzimas, G.N.4    Metrakos, P.P.5    Chevet, E.6
  • 15
    • 2442723696 scopus 로고    scopus 로고
    • Identification and characterization of an intracellular protein complex that binds fibroblast growth factor-2 in bovine brain
    • Chevet, E., Lemaitre, G., Cailleret, K., Dahan, S., Bergeron, J. J., and Katinka, M. D. (1999) Identification and characterization of an intracellular protein complex that binds fibroblast growth factor-2 in bovine brain. Biochem. J. 341, 713-723
    • (1999) Biochem. J. , vol.341 , pp. 713-723
    • Chevet, E.1    Lemaitre, G.2    Cailleret, K.3    Dahan, S.4    Bergeron, J.J.5    Katinka, M.D.6
  • 16
    • 29544444603 scopus 로고    scopus 로고
    • Efficient enrichment of intact phosphorylated proteins by modified immobilized metal-affinity chromatography
    • Dubrovska, A., and Souchelnytskyi, S. (2005) Efficient enrichment of intact phosphorylated proteins by modified immobilized metal-affinity chromatography. Proteomics 5, 4678-4683
    • (2005) Proteomics , vol.5 , pp. 4678-4683
    • Dubrovska, A.1    Souchelnytskyi, S.2
  • 19
    • 0041663987 scopus 로고    scopus 로고
    • Quantitative analysis of protein phosphorylation status and protein kinase activity on microarrays using a novel fluorescent phosphorylation sensor dye
    • Martin, K., Steinberg, T. H., Cooley, L. A., Gee, K. R., Beechem, J. M., and Patton, W. F. (2003) Quantitative analysis of protein phosphorylation status and protein kinase activity on microarrays using a novel fluorescent phosphorylation sensor dye. Proteomics 3, 1244-1255
    • (2003) Proteomics , vol.3 , pp. 1244-1255
    • Martin, K.1    Steinberg, T.H.2    Cooley, L.A.3    Gee, K.R.4    Beechem, J.M.5    Patton, W.F.6
  • 22
    • 0035067251 scopus 로고    scopus 로고
    • Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome
    • Oda, Y., Nagasu, T., and Chait, B. T. (2001) Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome. Nat. Biotechnol. 19, 379-382
    • (2001) Nat. Biotechnol. , vol.19 , pp. 379-382
    • Oda, Y.1    Nagasu, T.2    Chait, B.T.3
  • 24
    • 0037305895 scopus 로고    scopus 로고
    • Tackling the phosphoproteome: Tools and strategies
    • Kalume, D. E., Molina, H., and Pandey, A. (2003) Tackling the phosphoproteome: tools and strategies. Curr. Opin. Chem. Biol. 7, 64-69
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 64-69
    • Kalume, D.E.1    Molina, H.2    Pandey, A.3
  • 29
    • 0043093686 scopus 로고    scopus 로고
    • IQGAP proteins are integral components of cytoskeletal regulation
    • Briggs, M. W., and Sacks, D. B. (2003) IQGAP proteins are integral components of cytoskeletal regulation. EMBO Rep. 4, 571-574
    • (2003) EMBO Rep. , vol.4 , pp. 571-574
    • Briggs, M.W.1    Sacks, D.B.2
  • 30
    • 0036163555 scopus 로고    scopus 로고
    • Ischemia-reperfusion injury of the liver with special reference to calcium-dependent mechanisms
    • Sakon, M., Ariyoshi, H., Umeshita, K., and Monden, M. (2002) Ischemia-reperfusion injury of the liver with special reference to calcium-dependent mechanisms. Surg. Today 32, 1-12
    • (2002) Surg. Today , vol.32 , pp. 1-12
    • Sakon, M.1    Ariyoshi, H.2    Umeshita, K.3    Monden, M.4
  • 31
    • 0033454637 scopus 로고    scopus 로고
    • Pathophysiology and functional significance of apical membrane disruption during ischemia
    • Ashworth, S. L., and Molitoris, B. A. (1999) Pathophysiology and functional significance of apical membrane disruption during ischemia. Curr. Opin. Nephrol. Hypertens. 8, 449-458
    • (1999) Curr. Opin. Nephrol. Hypertens. , vol.8 , pp. 449-458
    • Ashworth, S.L.1    Molitoris, B.A.2
  • 32
    • 0031893838 scopus 로고    scopus 로고
    • Molecular structure and assembly of the tight junction
    • Denker, B. M., and Nigam, S. K. (1998) Molecular structure and assembly of the tight junction. Am. J. Physiol. 274, F1-F9
    • (1998) Am. J. Physiol. , vol.274
    • Denker, B.M.1    Nigam, S.K.2
  • 33
    • 0030683567 scopus 로고    scopus 로고
    • Role of the actin cytoskeleton in ischemia-induced cell injury and repair
    • Molitoris, B. A., Leiser, J., and Wagner, M. C. (1997) Role of the actin cytoskeleton in ischemia-induced cell injury and repair. Pediatr. Nephrol. 11, 761-767
    • (1997) Pediatr. Nephrol. , vol.11 , pp. 761-767
    • Molitoris, B.A.1    Leiser, J.2    Wagner, M.C.3
  • 34
    • 0029784514 scopus 로고    scopus 로고
    • The Ras GTPase-activating-protein-related human protein IQGAP2 harbors a potential actin binding domain and interacts with calmodulin and Rho family GTPases
    • Brill, S., Li, S., Lyman, C. W., Church, D. M., Wasmuth, J. J., Weissbach, L., Bernards, A., and Snijders, A. J. (1996) The Ras GTPase-activating-protein-related human protein IQGAP2 harbors a potential actin binding domain and interacts with calmodulin and Rho family GTPases. Mol. Cell. Biol. 16, 4869-4878
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4869-4878
    • Brill, S.1    Li, S.2    Lyman, C.W.3    Church, D.M.4    Wasmuth, J.J.5    Weissbach, L.6    Bernards, A.7    Snijders, A.J.8
  • 35
    • 0025335904 scopus 로고
    • The formation of bile canaliculi in human hepatoma cell lines
    • Chiu, J. H., Hu, C. P., Lui, W. Y., Lo, S. C., and Chang, C. M. (1990) The formation of bile canaliculi in human hepatoma cell lines. Hepatology 11, 834-842
    • (1990) Hepatology , vol.11 , pp. 834-842
    • Chiu, J.H.1    Hu, C.P.2    Lui, W.Y.3    Lo, S.C.4    Chang, C.M.5
  • 36
    • 0037011151 scopus 로고    scopus 로고
    • Oncostatin M regulates membrane traffic and stimulates bile canalicular membrane biogenesis in HepG2 cells
    • van der Wouden, J. M., van IJzendoom, S. C., and Hoekstra, D. (2002) Oncostatin M regulates membrane traffic and stimulates bile canalicular membrane biogenesis in HepG2 cells. EMBO J. 21, 6409-6418
    • (2002) EMBO J. , vol.21 , pp. 6409-6418
    • van der Wouden, J.M.1    van IJzendoom, S.C.2    Hoekstra, D.3
  • 37
    • 4544269197 scopus 로고    scopus 로고
    • Protein, amino acids and the control of food intake
    • Tome, D. (2004) Protein, amino acids and the control of food intake. Br. J. Nutr. 92, Suppl. 1, S27-S30
    • (2004) Br. J. Nutr. , vol.92 , Issue.SUPPL. 1
    • Tome, D.1
  • 38
    • 0028132284 scopus 로고
    • Calcium-activated proteolysis in rat neocortex induced by transient focal ischemia
    • Hong, S. C., Lanzino, G., Goto, Y., Kang, S. K., Schottler, F., Kassell, N. F., and Lee, K. S. (1994) Calcium-activated proteolysis in rat neocortex induced by transient focal ischemia. Brain Res. 661, 43-50
    • (1994) Brain Res. , vol.661 , pp. 43-50
    • Hong, S.C.1    Lanzino, G.2    Goto, Y.3    Kang, S.K.4    Schottler, F.5    Kassell, N.F.6    Lee, K.S.7
  • 39
    • 0035110722 scopus 로고    scopus 로고
    • Prednisolone suppresses ischemia-reperfusion injury of the rat liver by reducing cytokine production and calpain μ activation
    • Wang, M., Sakon, M., Umeshita, K., Okuyama, M., Shiozaki, K., Nagano, H., Dohno, K., Nakamori, S., and Monden, M. (2001) Prednisolone suppresses ischemia-reperfusion injury of the rat liver by reducing cytokine production and calpain μ activation. J. Hepatol, 34, 278-283
    • (2001) J. Hepatol. , vol.34 , pp. 278-283
    • Wang, M.1    Sakon, M.2    Umeshita, K.3    Okuyama, M.4    Shiozaki, K.5    Nagano, H.6    Dohno, K.7    Nakamori, S.8    Monden, M.9
  • 40
    • 4344566974 scopus 로고    scopus 로고
    • Protein kinase A dependent signalling mediates anti-apoptotic effects of the atrial natriuretic peptide in ischemic livers
    • Kulhanek-Heinze, S., Gerbes, A. L., Gerwig, T., Vollmar, A. M., and Kiemer, A. K. (2004) Protein kinase A dependent signalling mediates anti-apoptotic effects of the atrial natriuretic peptide in ischemic livers. J. Hepatol. 41, 414-420
    • (2004) J. Hepatol. , vol.41 , pp. 414-420
    • Kulhanek-Heinze, S.1    Gerbes, A.L.2    Gerwig, T.3    Vollmar, A.M.4    Kiemer, A.K.5
  • 41
    • 26844443598 scopus 로고    scopus 로고
    • Phosphorylation-dependent interactions of α-Actinin-1/IQGAP1 with the AMPA receptor subunit GluR4
    • Nuriya, M., Oh, S., and Huganir, R. L. (2005) Phosphorylation-dependent interactions of α-Actinin-1/IQGAP1 with the AMPA receptor subunit GluR4. J. Neurochem. 95, 544-552
    • (2005) J. Neurochem. , vol.95 , pp. 544-552
    • Nuriya, M.1    Oh, S.2    Huganir, R.L.3
  • 42
    • 10344260216 scopus 로고    scopus 로고
    • Phosphorylation of IQGAP1 modulates its binding to Cdc42, revealing a new type of rho-GTPase regulator
    • Grohmanova, K., Schlaepfer, D., Hess, D., Gutierrez, P., Beck, M., and Kroschewski, R. (2004) Phosphorylation of IQGAP1 modulates its binding to Cdc42, revealing a new type of rho-GTPase regulator. J. Biol. Chem. 279, 48495-48504
    • (2004) J. Biol. Chem. , vol.279 , pp. 48495-48504
    • Grohmanova, K.1    Schlaepfer, D.2    Hess, D.3    Gutierrez, P.4    Beck, M.5    Kroschewski, R.6
  • 43
    • 0027217613 scopus 로고
    • Bile canaliculus formation in cultured HEPG2 cells
    • Sormunen, R., Eskelinen, S., and Lehto, V. P. (1993) Bile canaliculus formation in cultured HEPG2 cells. Lab. Investig. 68, 652-662
    • (1993) Lab. Investig. , vol.68 , pp. 652-662
    • Sormunen, R.1    Eskelinen, S.2    Lehto, V.P.3
  • 44
    • 0033679661 scopus 로고    scopus 로고
    • Modeling ischemia in vitro: Selective depletion of adenine and guanine nucleotide pools
    • Dagher, P. C. (2000) Modeling ischemia in vitro: selective depletion of adenine and guanine nucleotide pools. Am. J. Physiol. 279, C1270-C1277
    • (2000) Am. J. Physiol. , vol.279
    • Dagher, P.C.1
  • 45
    • 3342986329 scopus 로고    scopus 로고
    • Endocytosis of E-cadherin regulated by Rac and Cdc42 small G proteins through IQGAP1 and actin filaments
    • Izumi, G., Sakisaka, T., Babe, T., Tanaka, S., Morimoto, K., and Takai, Y. (2004) Endocytosis of E-cadherin regulated by Rac and Cdc42 small G proteins through IQGAP1 and actin filaments. J. Cell Biol. 166, 237-248
    • (2004) J. Cell Biol. , vol.166 , pp. 237-248
    • Izumi, G.1    Sakisaka, T.2    Babe, T.3    Tanaka, S.4    Morimoto, K.5    Takai, Y.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.