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Volumn 279, Issue 17, 2012, Pages 3240-3250

Advanced glycation end-products induce calpain-mediated degradation of ezrin

Author keywords

advanced glycation end products; diabetes; ezrin

Indexed keywords

ADVANCED GLYCATION END PRODUCT; BOVINE SERUM ALBUMIN; CALCIUM ION; CALPAIN; CALPASTATIN; CHELATING AGENT; EZRIN; GLUCOSE; MOESIN; RADIXIN; RECOMBINANT PROTEIN;

EID: 84865255494     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2012.08710.x     Document Type: Article
Times cited : (14)

References (61)
  • 2
    • 34548506357 scopus 로고    scopus 로고
    • Below the radar: Advanced glycation end products that detour 'around the side'
    • Forbes JM, Soldatos G, &, Thomas MC, (2005) Below the radar: advanced glycation end products that detour 'around the side'. Clin Biochem Rev 26, 123-134.
    • (2005) Clin Biochem Rev , vol.26 , pp. 123-134
    • Forbes, J.M.1    Soldatos, G.2    Thomas, M.C.3
  • 3
    • 61849159854 scopus 로고    scopus 로고
    • A perspective on the Maillard reaction and the analysis of protein glycation by mass spectrometry: Probing the pathogenesis of chronic disease
    • Zhang Q, Ames JM, Smith RD, Baynes JW, &, Metz TO, (2009) A perspective on the Maillard reaction and the analysis of protein glycation by mass spectrometry: probing the pathogenesis of chronic disease. J Proteome Res 8, 754-769.
    • (2009) J Proteome Res , vol.8 , pp. 754-769
    • Zhang, Q.1    Ames, J.M.2    Smith, R.D.3    Baynes, J.W.4    Metz, T.O.5
  • 5
    • 42049118293 scopus 로고    scopus 로고
    • The role of advanced glycation end products in progression and complications of diabetes
    • Goh S, &, Cooper ME, (2008) The role of advanced glycation end products in progression and complications of diabetes. J Clin Endocrinol Metab 93, 1143-1152.
    • (2008) J Clin Endocrinol Metab , vol.93 , pp. 1143-1152
    • Goh, S.1    Cooper, M.E.2
  • 6
    • 33947671901 scopus 로고    scopus 로고
    • Advanced glycation endproducts: What is their relevance to diabetic complications?
    • Ahmed N, &, Thornalley PJ, (2007) Advanced glycation endproducts: what is their relevance to diabetic complications? Diabetes Obes Metab 9, 233-245.
    • (2007) Diabetes Obes Metab , vol.9 , pp. 233-245
    • Ahmed, N.1    Thornalley, P.J.2
  • 7
    • 0037477342 scopus 로고    scopus 로고
    • The amino terminal domains of ERM proteins bind advanced glycation endproducts: An interaction that may play a role in the development of diabetic complications
    • McRobert EA, Gallicchio M, Jerums G, Cooper ME, &, Bach LA, (2003) The amino terminal domains of ERM proteins bind advanced glycation endproducts: an interaction that may play a role in the development of diabetic complications. J Biol Chem 278, 25783-25789.
    • (2003) J Biol Chem , vol.278 , pp. 25783-25789
    • McRobert, E.A.1    Gallicchio, M.2    Jerums, G.3    Cooper, M.E.4    Bach, L.A.5
  • 8
    • 65149104670 scopus 로고    scopus 로고
    • Merlin and the ERM proteins - Regulators of receptor distribution and signalling at the cell cortex
    • McClatchey AI, &, Fehon RG, (2009) Merlin and the ERM proteins-regulators of receptor distribution and signalling at the cell cortex. Trends Cell Biol 19, 198-206.
    • (2009) Trends Cell Biol , vol.19 , pp. 198-206
    • McClatchey, A.I.1    Fehon, R.G.2
  • 9
    • 39049085828 scopus 로고    scopus 로고
    • Ezrin/radixin/moesin: Versatile controllers of signaling molecules and of the cortical cytoskeleton
    • Niggli V, &, Rossy J, (2008) Ezrin/radixin/moesin: versatile controllers of signaling molecules and of the cortical cytoskeleton. Int J Biochem Cell Biol 40, 344-349.
    • (2008) Int J Biochem Cell Biol , vol.40 , pp. 344-349
    • Niggli, V.1    Rossy, J.2
  • 10
    • 43049170065 scopus 로고    scopus 로고
    • Localization of the ezrin binding epitope for advanced glycation endproducts
    • McRobert EA, Tikoo A, Cooper ME, &, Bach LA, (2008) Localization of the ezrin binding epitope for advanced glycation endproducts. Int J Biochem Cell Biol 40, 1570-1580.
    • (2008) Int J Biochem Cell Biol , vol.40 , pp. 1570-1580
    • McRobert, E.A.1    Tikoo, A.2    Cooper, M.E.3    Bach, L.A.4
  • 11
    • 0036346708 scopus 로고    scopus 로고
    • ERM proteins and merlin: Integrators at the cell cortex
    • Bretscher A, Edwards K, &, Fehon RG, (2002) ERM proteins and merlin: integrators at the cell cortex. Nat Rev Mol Cell Biol 3, 586-599.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 586-599
    • Bretscher, A.1    Edwards, K.2    Fehon, R.G.3
  • 12
    • 33645456451 scopus 로고    scopus 로고
    • Advanced glycation end products inhibit tubulogenesis and migration of kidney epithelial cells in an ezrin-dependent manner
    • Gallicchio MA, McRobert EA, Tikoo A, Cooper ME, &, Bach LA, (2006) Advanced glycation end products inhibit tubulogenesis and migration of kidney epithelial cells in an ezrin-dependent manner. J Am Soc Nephrol 17, 414-421.
    • (2006) J Am Soc Nephrol , vol.17 , pp. 414-421
    • Gallicchio, M.A.1    McRobert, E.A.2    Tikoo, A.3    Cooper, M.E.4    Bach, L.A.5
  • 13
    • 0033542725 scopus 로고    scopus 로고
    • Identification of a 55-kDa ezrin-related protein that induces cytoskeletal changes and localizes to the nucleolus
    • Kaul SC, Kawai R, Nomura H, Mitsui Y, Reddel RR, &, Wadha R, (1999) Identification of a 55-kDa ezrin-related protein that induces cytoskeletal changes and localizes to the nucleolus. Exp Cell Res 250, 51-61.
    • (1999) Exp Cell Res , vol.250 , pp. 51-61
    • Kaul, S.C.1    Kawai, R.2    Nomura, H.3    Mitsui, Y.4    Reddel, R.R.5    Wadha, R.6
  • 14
    • 0034722326 scopus 로고    scopus 로고
    • Mutagenesis of the phosphatidyl 4,5-biphosphate (PIP2) binding site in the NH2-terminal domain of ezrin correlates with its altered cellular distribution
    • Barret C, Roy C, Montcourrier P, Mangeat P, &, Niggli V, (2000) Mutagenesis of the phosphatidyl 4,5-biphosphate (PIP2) binding site in the NH2-terminal domain of ezrin correlates with its altered cellular distribution. J Cell Biol 151, 1067-1080.
    • (2000) J Cell Biol , vol.151 , pp. 1067-1080
    • Barret, C.1    Roy, C.2    Montcourrier, P.3    Mangeat, P.4    Niggli, V.5
  • 15
    • 0027162182 scopus 로고
    • Ezrin-calpain 1 interactions in gastric parietal cells
    • Yao X, Thibodeau A, &, Forte JG, (1993) Ezrin-calpain 1 interactions in gastric parietal cells. Am J Physiol 265, C36-C46.
    • (1993) Am J Physiol , vol.265
    • Yao, X.1    Thibodeau, A.2    Forte, J.G.3
  • 17
    • 26244434596 scopus 로고    scopus 로고
    • Regulating cell migration: Calpains make the cut
    • Franco JS, &, Huttenlocher A, (2005) Regulating cell migration: calpains make the cut. J Cell Sci 118, 3829-3838.
    • (2005) J Cell Sci , vol.118 , pp. 3829-3838
    • Franco, J.S.1    Huttenlocher, A.2
  • 18
    • 0028898820 scopus 로고
    • Indirect association of ezrin with F-actin: Isoform specificity and calcium sensitivity
    • Shuster CB, &, Herman IM, (1995) Indirect association of ezrin with F-actin: isoform specificity and calcium sensitivity. J Cell Biol 128, 837-848.
    • (1995) J Cell Biol , vol.128 , pp. 837-848
    • Shuster, C.B.1    Herman, I.M.2
  • 20
    • 0029088469 scopus 로고
    • High glucose alters actin assembly in glomerular mesangial and epithelial cells
    • Zhou X, Hurst RD, D T, &, Whiteside C, (1995) High glucose alters actin assembly in glomerular mesangial and epithelial cells. Lab Invest 73, 372-383.
    • (1995) Lab Invest , vol.73 , pp. 372-383
    • Zhou, X.1    Hurst, R.D.2    D, T.3    Whiteside, C.4
  • 21
    • 0026640556 scopus 로고
    • Corneal endothelial cytoskeletal changes in F-actin with aging, diabetes and after cytochalasin exposure
    • Kim EK, Geroski DH, Holley GP, Urken SI, &, Edelhauser HF, (1992) Corneal endothelial cytoskeletal changes in F-actin with aging, diabetes and after cytochalasin exposure. Am J Ophthalmol 114, 329-335.
    • (1992) Am J Ophthalmol , vol.114 , pp. 329-335
    • Kim, E.K.1    Geroski, D.H.2    Holley, G.P.3    Urken, S.I.4    Edelhauser, H.F.5
  • 23
    • 0032731318 scopus 로고    scopus 로고
    • The tubulointerstitium in progressive diabetic kidney disease: More than an aftermath of glomerular injury
    • Gilbert RE, &, Cooper ME, (1999) The tubulointerstitium in progressive diabetic kidney disease: more than an aftermath of glomerular injury. Kidney Int 56, 1627-1637.
    • (1999) Kidney Int , vol.56 , pp. 1627-1637
    • Gilbert, R.E.1    Cooper, M.E.2
  • 24
    • 33748857020 scopus 로고    scopus 로고
    • Ezrin - A useful factor in the prognosis of nephrotic syndrome in children: An immunohistochemical approach
    • Ostalska-Nowicka D, Zachwieja J, Nowicki N, Kaczmarek E, Siwinska A, &, Witt M, (2006) Ezrin-a useful factor in the prognosis of nephrotic syndrome in children: an immunohistochemical approach. J Clin Pathol 59, 916-920.
    • (2006) J Clin Pathol , vol.59 , pp. 916-920
    • Ostalska-Nowicka, D.1    Zachwieja, J.2    Nowicki, N.3    Kaczmarek, E.4    Siwinska, A.5    Witt, M.6
  • 26
    • 78349264651 scopus 로고    scopus 로고
    • Glucose-induced ERM protein activation and translocation regulates insulin secretion
    • Lopez JP, Turner JR, &, Philipson LH, (2010) Glucose-induced ERM protein activation and translocation regulates insulin secretion. Am J Physiol Endocrinol Metab 299, E772-E785.
    • (2010) Am J Physiol Endocrinol Metab , vol.299
    • Lopez, J.P.1    Turner, J.R.2    Philipson, L.H.3
  • 27
    • 77957740531 scopus 로고    scopus 로고
    • Clinical impact of glycated albumin as another glycaemic control marker
    • Koga M, &, Kasayama S, (2010) Clinical impact of glycated albumin as another glycaemic control marker. Endocrine J 57, 751-762.
    • (2010) Endocrine J , vol.57 , pp. 751-762
    • Koga, M.1    Kasayama, S.2
  • 29
    • 79952446703 scopus 로고    scopus 로고
    • The glycation of albumin: Structural and functional impacts
    • Rondeau P, &, Bourdon E, (2011) The glycation of albumin: structural and functional impacts. Biochimie 93, 645-658.
    • (2011) Biochimie , vol.93 , pp. 645-658
    • Rondeau, P.1    Bourdon, E.2
  • 33
    • 0037088661 scopus 로고    scopus 로고
    • Calpastatin subdomains A and C are activators of calpain
    • Tompa P, Mucsi Z, Orosz G, &, Friedrich P, (2002) Calpastatin subdomains A and C are activators of calpain. J Biol Chem 277, 9022-9026.
    • (2002) J Biol Chem , vol.277 , pp. 9022-9026
    • Tompa, P.1    Mucsi, Z.2    Orosz, G.3    Friedrich, P.4
  • 34
    • 15944428524 scopus 로고    scopus 로고
    • The calcium-dependent protease calpain causes endothelial dysfunction in type 2 diabetes
    • Stalker TJ, Gong Y, &, Scalia R, (2005) The calcium-dependent protease calpain causes endothelial dysfunction in type 2 diabetes. Diabetes 54, 1132-1140.
    • (2005) Diabetes , vol.54 , pp. 1132-1140
    • Stalker, T.J.1    Gong, Y.2    Scalia, R.3
  • 36
    • 33947661527 scopus 로고    scopus 로고
    • High glucose initiates calpain-induced necrosis before apoptosis in LLLC-PK1 cells
    • Harwood SM, Allen DA, Raftery MJ, &, Yaqoob MM, (2007) High glucose initiates calpain-induced necrosis before apoptosis in LLLC-PK1 cells. Kidney Int 71, 655-663.
    • (2007) Kidney Int , vol.71 , pp. 655-663
    • Harwood, S.M.1    Allen, D.A.2    Raftery, M.J.3    Yaqoob, M.M.4
  • 37
    • 72849111282 scopus 로고    scopus 로고
    • Activation of protease calpain by oxidized and glycated LDL increases the degradation of endothelial nitric oxide synthase
    • Dong Y, Wu Y, Wu M, Wang SC, Zhang J, Xie Z, Xu J, Song P, Wilson K, Zhao Z, et al. (2009) Activation of protease calpain by oxidized and glycated LDL increases the degradation of endothelial nitric oxide synthase. J Cell Mol Med 13, 2899-2910.
    • (2009) J Cell Mol Med , vol.13 , pp. 2899-2910
    • Dong, Y.1    Wu, Y.2    Wu, M.3    Wang, S.C.4    Zhang, J.5    Xie, Z.6    Xu, J.7    Song, P.8    Wilson, K.9    Zhao, Z.10
  • 39
    • 0030723168 scopus 로고    scopus 로고
    • Role of elevated cystolic calcium in the pathogenesis of complications in diabetes mellitus
    • Massry SG, &, Smorgorzewski M, (1997) Role of elevated cystolic calcium in the pathogenesis of complications in diabetes mellitus. Miner Electrolyte Metab 23, 253-260.
    • (1997) Miner Electrolyte Metab , vol.23 , pp. 253-260
    • Massry, S.G.1    Smorgorzewski, M.2
  • 40
    • 14844350043 scopus 로고    scopus 로고
    • Effect of methylglyoxal on intracellular calcium levels and viability in renal tubular cells
    • Jan CR, Chen CH, Wang SC, &, Kuo SY, (2005) Effect of methylglyoxal on intracellular calcium levels and viability in renal tubular cells. Cell Signal 17, 847-855.
    • (2005) Cell Signal , vol.17 , pp. 847-855
    • Jan, C.R.1    Chen, C.H.2    Wang, S.C.3    Kuo, S.Y.4
  • 41
    • 33644500455 scopus 로고    scopus 로고
    • Involvement of EP1 and EP2 receptors in the regulation of the Na, K-ATPase by prostaglandins in MDCK cells
    • Matihagela K, &, Taub M, (2006) Involvement of EP1 and EP2 receptors in the regulation of the Na, K-ATPase by prostaglandins in MDCK cells. Prostaglandins Other Lipid Mediat 79, 101-113.
    • (2006) Prostaglandins Other Lipid Mediat , vol.79 , pp. 101-113
    • Matihagela, K.1    Taub, M.2
  • 43
    • 22144443812 scopus 로고    scopus 로고
    • The cytoskeletal protein ezrin regulates EC proliferation and angiogenesis via TNF-α-induced transcriptional repression of cyclin A
    • Kishore R, Qin G, Luedemann C, Bord E, Hanley A, Silver M, Gavin M, Goukassain D, &, Losordo DW, (2005) The cytoskeletal protein ezrin regulates EC proliferation and angiogenesis via TNF-α-induced transcriptional repression of cyclin A. J Clin Invest 115, 1785-1796.
    • (2005) J Clin Invest , vol.115 , pp. 1785-1796
    • Kishore, R.1    Qin, G.2    Luedemann, C.3    Bord, E.4    Hanley, A.5    Silver, M.6    Gavin, M.7    Goukassain, D.8    Losordo, D.W.9
  • 45
    • 44049089012 scopus 로고    scopus 로고
    • Phosphoinositide binding to the substrate regulates susceptibility to proteolysis by calpain
    • Sprague CR, Fraley TS, Jang HS, Lal S, &, Greenwood JA, (2008) Phosphoinositide binding to the substrate regulates susceptibility to proteolysis by calpain. J Biol Chem 283, 9217-9223.
    • (2008) J Biol Chem , vol.283 , pp. 9217-9223
    • Sprague, C.R.1    Fraley, T.S.2    Jang, H.S.3    Lal, S.4    Greenwood, J.A.5
  • 46
    • 34247516852 scopus 로고    scopus 로고
    • ERM proteins in epithelial cell organization and functions
    • Fievet BT, Louvard D, &, Arpin M, (2006) ERM proteins in epithelial cell organization and functions. Biochem Biophys Acta 1773, 653-660.
    • (2006) Biochem Biophys Acta , vol.1773 , pp. 653-660
    • Fievet, B.T.1    Louvard, D.2    Arpin, M.3
  • 47
    • 38449120815 scopus 로고    scopus 로고
    • Inhibition of T cell activation by cyclic adenosine 5′- monophosphate requires lipid raft targeting of protein kinase A type 1 by the A-kinase anchoring protein ezrin
    • Ruppelt A, Mosenden R, Gronholm M, Aandahl EM, Tobin D, Carlson CR, Abrahamsen H, Herberg FW, Carpen O, &, Tasken K, (2007) Inhibition of T cell activation by cyclic adenosine 5′-monophosphate requires lipid raft targeting of protein kinase A type 1 by the A-kinase anchoring protein ezrin. J Immunol 179, 5159-5168.
    • (2007) J Immunol , vol.179 , pp. 5159-5168
    • Ruppelt, A.1    Mosenden, R.2    Gronholm, M.3    Aandahl, E.M.4    Tobin, D.5    Carlson, C.R.6    Abrahamsen, H.7    Herberg, F.W.8    Carpen, O.9    Tasken, K.10
  • 48
    • 0032783917 scopus 로고    scopus 로고
    • Regulation of F-actin binding to platelet moesin in vitro by both phosphorylation of threonine 558 and phosphatidylinositides
    • Nakamura F, Huang K, Pestonjamasp E, Luna J, &, Furthmayr H, (1999) Regulation of F-actin binding to platelet moesin in vitro by both phosphorylation of threonine 558 and phosphatidylinositides. Mol Biol Cell 10, 2669-2685.
    • (1999) Mol Biol Cell , vol.10 , pp. 2669-2685
    • Nakamura, F.1    Huang, K.2    Pestonjamasp, E.3    Luna, J.4    Furthmayr, H.5
  • 49
    • 83755171604 scopus 로고    scopus 로고
    • EphrinA1-EphA2 signal induces compaction and polarization of MDCK kidney cells by inactivating ezrin through negative regulation of RhoA
    • Wakayama Y, Miura K, &, Mochizuki N, (2011) EphrinA1-EphA2 signal induces compaction and polarization of MDCK kidney cells by inactivating ezrin through negative regulation of RhoA. J Biol Chem 268, 44243-44253.
    • (2011) J Biol Chem , vol.268 , pp. 44243-44253
    • Wakayama, Y.1    Miura, K.2    Mochizuki, N.3
  • 50
    • 2442513975 scopus 로고    scopus 로고
    • Nuclear ERM (ezrin, radixin, moesin) proteins: Regulation by cell density and nuclear import
    • Batchelor CL, Woodward AM, &, Crouch DH, (2004) Nuclear ERM (ezrin, radixin, moesin) proteins: regulation by cell density and nuclear import. Exp Cell Res 296, 208-222.
    • (2004) Exp Cell Res , vol.296 , pp. 208-222
    • Batchelor, C.L.1    Woodward, A.M.2    Crouch, D.H.3
  • 52
    • 79151484613 scopus 로고    scopus 로고
    • Advanced glycation end products induce moesin phosphorylation in murine brain endothelium
    • Li Q, Liu H, Du J, Chen B, Li Q, Guo X, Huang X, &, Huang Q, (2011) Advanced glycation end products induce moesin phosphorylation in murine brain endothelium. Brain Res 1373, 7-15.
    • (2011) Brain Res , vol.1373 , pp. 7-15
    • Li, Q.1    Liu, H.2    Du, J.3    Chen, B.4    Li, Q.5    Guo, X.6    Huang, X.7    Huang, Q.8
  • 53
    • 0027183643 scopus 로고
    • Ezrin is concentrated in the apical microvilli of a wide variety of epithelial cells whereas moesin is found primarily in endothelial cells
    • Berryman M, Franck Z, &, Bretscher A, (1993) Ezrin is concentrated in the apical microvilli of a wide variety of epithelial cells whereas moesin is found primarily in endothelial cells. J Cell Sci 105, 1025-1043.
    • (1993) J Cell Sci , vol.105 , pp. 1025-1043
    • Berryman, M.1    Franck, Z.2    Bretscher, A.3
  • 54
    • 36349036612 scopus 로고    scopus 로고
    • Immune synapse formation requires ZAP-70 recruitment by ezrin and CD43 removal by moesin
    • Ilani T, Khanna C, Zhou M, Veenstra TD, &, Bretscher A, (2007) Immune synapse formation requires ZAP-70 recruitment by ezrin and CD43 removal by moesin. J Cell Biol 179, 733-746.
    • (2007) J Cell Biol , vol.179 , pp. 733-746
    • Ilani, T.1    Khanna, C.2    Zhou, M.3    Veenstra, T.D.4    Bretscher, A.5
  • 57
    • 0030763919 scopus 로고    scopus 로고
    • Ezrin is an effector of HGF-mediated migration and morphogenesis in epithelial cells
    • Crepaldi T, Gautreau A, Comoglio PM, Louvard D, &, Arpin M, (1997) Ezrin is an effector of HGF-mediated migration and morphogenesis in epithelial cells. J Cell Biol 138, 423-434.
    • (1997) J Cell Biol , vol.138 , pp. 423-434
    • Crepaldi, T.1    Gautreau, A.2    Comoglio, P.M.3    Louvard, D.4    Arpin, M.5
  • 59
    • 77951215973 scopus 로고    scopus 로고
    • Local delivery of angiotensin II receptor blockers into the kidney passively attenuates inflammatory reactions during the early phases of streptozotocin-induced diabetic nephropathy through inhibition of calpain activity
    • Kamal F, Yanakieva-Georgieva N, Piao H, Morioka T, &, Oite T, (2010) Local delivery of angiotensin II receptor blockers into the kidney passively attenuates inflammatory reactions during the early phases of streptozotocin-induced diabetic nephropathy through inhibition of calpain activity. Nephron Exp Nephrol 115, e69-e79.
    • (2010) Nephron Exp Nephrol , vol.115
    • Kamal, F.1    Yanakieva-Georgieva, N.2    Piao, H.3    Morioka, T.4    Oite, T.5


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