메뉴 건너뛰기




Volumn 1740, Issue 3, 2005, Pages 332-339

Effect of acetaminophen on the membrane anchoring of Na+, K +ATPase of rat renal cortical cells

Author keywords

Acetaminophen; Calpain; K+ATPase; Na+; Renal cell suspension; Triton X 100 extractability

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); CALPAIN; CHLOROACETIC ACID N' (6,7 DICHLORO 4 PHENYL 3 OXO 3,4 DIHYDROQUINOXALIN 2 YL)HYDRAZIDE; HYDRAZIDE DERIVATIVE; LACTATE DEHYDROGENASE; PARACETAMOL; SJA 7029; TRITON X 100; UNCLASSIFIED DRUG;

EID: 20444417080     PISSN: 09254439     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbadis.2004.09.011     Document Type: Article
Times cited : (14)

References (49)
  • 2
    • 0022589770 scopus 로고
    • Structure, function and regulation of Na, K ATPase in the kidney
    • P.L. Jørgensen Structure, function and regulation of Na, K ATPase in the kidney Kidney Int. 29 1986 10 20
    • (1986) Kidney Int. , vol.29 , pp. 10-20
    • Jørgensen, P.L.1
  • 3
    • 0002798339 scopus 로고
    • The potential role of ischemia in renal disease progression
    • B.A. Molitoris The potential role of ischemia in renal disease progression Kidney Int. 41 1992 S21 S25
    • (1992) Kidney Int. , vol.41
    • Molitoris, B.A.1
  • 4
    • 0015221649 scopus 로고
    • Plasma paracetamol half-life and hepatic necrosis in patients with paracetamol overdosage
    • L.F. Prescott, N. Wright, P. Roscoe, and S.S. Brown Plasma paracetamol half-life and hepatic necrosis in patients with paracetamol overdosage Lancet i 1971 519 522
    • (1971) Lancet , vol.1 , pp. 519-522
    • Prescott, L.F.1    Wright, N.2    Roscoe, P.3    Brown, S.S.4
  • 5
    • 0015231479 scopus 로고
    • Acetaminophen-induced hepatic necrosis and renal failure
    • T.D. Boyer, and S.L. Rouff Acetaminophen-induced hepatic necrosis and renal failure JAMA 218 1971 440 441
    • (1971) JAMA , vol.218 , pp. 440-441
    • Boyer, T.D.1    Rouff, S.L.2
  • 6
    • 0020034744 scopus 로고
    • Paracetamol induced acute renal failure in the absence of fulminant liver damage
    • I. Cobden, C.O. Record, M.K. Ward, and D.N.S. Kerr Paracetamol induced acute renal failure in the absence of fulminant liver damage Br. Med. J. 284 1982 21 22
    • (1982) Br. Med. J. , vol.284 , pp. 21-22
    • Cobden, I.1    Record, C.O.2    Ward, M.K.3    Kerr, D.N.S.4
  • 8
    • 0018081508 scopus 로고
    • Renal necrosis, glutathione depletion and covalent binding after acetaminophen
    • R. McMurtry, W.R. Snodgrass, and J.R. Mitchell Renal necrosis, glutathione depletion and covalent binding after acetaminophen Toxicol. Appl. Pharmacol. 46 1978 87 100
    • (1978) Toxicol. Appl. Pharmacol. , vol.46 , pp. 87-100
    • McMurtry, R.1    Snodgrass, W.R.2    Mitchell, J.R.3
  • 9
    • 0024404067 scopus 로고
    • Strain differences in acetaminophen nephrotoxicity in rats: Role of pharmacokinetics
    • J.B. Tarloff, R.S. Goldstein, and J.R. Hook Strain differences in acetaminophen nephrotoxicity in rats: Role of pharmacokinetics Toxicology 56 1989 167 177
    • (1989) Toxicology , vol.56 , pp. 167-177
    • Tarloff, J.B.1    Goldstein, R.S.2    Hook, J.R.3
  • 11
    • 0020622896 scopus 로고
    • Acetaminophen nephrotoxicity in the rat. I. Strain differences in nephrotoxicity and metabolism
    • J.F. Newton, M. Yoshimoto, J. Bernstein, G.F. Rush, and J.B. Hook Acetaminophen nephrotoxicity in the rat. I. Strain differences in nephrotoxicity and metabolism Toxicol. Appl. Pharmacol. 69 1983 291 306
    • (1983) Toxicol. Appl. Pharmacol. , vol.69 , pp. 291-306
    • Newton, J.F.1    Yoshimoto, M.2    Bernstein, J.3    Rush, G.F.4    Hook, J.B.5
  • 13
    • 0026571135 scopus 로고
    • Acetaminophen nephrotoxicity in male Wistar rats
    • L. Trumper, G. Girardi, and M.M. Elías Acetaminophen nephrotoxicity in male Wistar rats Arch. Toxicol. 66 1992 107 111
    • (1992) Arch. Toxicol. , vol.66 , pp. 107-111
    • Trumper, L.1    Girardi, G.2    Elías, M.M.3
  • 14
    • 0028931796 scopus 로고
    • Tubular effects of acetaminophen in the isolated perfused rat kidney
    • L. Trumper, L.A. Monasterolo, E. Ochoa, and M.M. Elías Tubular effects of acetaminophen in the isolated perfused rat kidney Arch. Toxicol. 69 1995 248 252
    • (1995) Arch. Toxicol. , vol.69 , pp. 248-252
    • Trumper, L.1    Monasterolo, L.A.2    Ochoa, E.3    Elías, M.M.4
  • 15
    • 0025305262 scopus 로고
    • The sodium pump needs its β subunit
    • A.A. McDonough, K. Geering, and R.A. Farley The sodium pump needs its β subunit FASEB J. 4 1990 1598 1605
    • (1990) FASEB J. , vol.4 , pp. 1598-1605
    • McDonough, A.A.1    Geering, K.2    Farley, R.A.3
  • 16
    • 0035133295 scopus 로고    scopus 로고
    • Sodium-potassium-adenosine triphosphatase-dependent sodium transport in the kidney: Hormonal control
    • E. Féraile, and A. Doucet Sodium-potassium-adenosine triphosphatase-dependent sodium transport in the kidney: hormonal control Physiol. Rev. 81 2001 345 418
    • (2001) Physiol. Rev. , vol.81 , pp. 345-418
    • Féraile, E.1    Doucet, A.2
  • 17
    • 0026446341 scopus 로고
    • Regulation of cell surface polarity from bacteria to mammals
    • W.J. Nelson Regulation of cell surface polarity from bacteria to mammals Science 258 1992 948 955
    • (1992) Science , vol.258 , pp. 948-955
    • Nelson, W.J.1
  • 18
    • 0024439472 scopus 로고
    • Ischemia-induced loss of epithelial polarity
    • B.A. Molitoris, S.A. Falk, and R.H. Dahl Ischemia-induced loss of epithelial polarity J. Clin. Invest. 84 1989 1334 1339
    • (1989) J. Clin. Invest. , vol.84 , pp. 1334-1339
    • Molitoris, B.A.1    Falk, S.A.2    Dahl, R.H.3
  • 20
    • 0027137547 scopus 로고
    • +-ATPase that redistributes to apical membrane during ATP depletion remains functional
    • +-ATPase that redistributes to apical membrane during ATP depletion remains functional Am. J. Physiol. 265 1993 F693 F697
    • (1993) Am. J. Physiol. , vol.265
    • Molitoris, B.A.1
  • 24
    • 0031443677 scopus 로고    scopus 로고
    • Calpains mediate calcium and chloride influx during the late phase of cell injury
    • S.L. Waters, S.S. Sarang, K.K.W. Wang, and R.G. Schnellmann Calpains mediate calcium and chloride influx during the late phase of cell injury J. Pharmacol. Exp. Ther. 283 1997 1177 1184
    • (1997) J. Pharmacol. Exp. Ther. , vol.283 , pp. 1177-1184
    • Waters, S.L.1    Sarang, S.S.2    Wang, K.K.W.3    Schnellmann, R.G.4
  • 25
    • 0026333353 scopus 로고
    • Mechanisms of cyclosporin a toxicity in defined cultures of renal tubule epithelia: A role of cysteine proteases
    • P.D. Wilson, and P.A. Hartz Mechanisms of cyclosporin A toxicity in defined cultures of renal tubule epithelia: A role of cysteine proteases Cell Biol. Int. Rep. 15 1991 1243 1258
    • (1991) Cell Biol. Int. Rep. , vol.15 , pp. 1243-1258
    • Wilson, P.D.1    Hartz, P.A.2
  • 27
    • 0030593657 scopus 로고    scopus 로고
    • Autolysis of human erythrocyte calpain produces two active enzyme forms with different cell localization
    • M. Michetti, F. Salamino, I. Tedesco, M. Averna, R. Minafra, E. Melloni, and S. Pontremoli Autolysis of human erythrocyte calpain produces two active enzyme forms with different cell localization FEBS Lett. 392 1996 11 15
    • (1996) FEBS Lett. , vol.392 , pp. 11-15
    • Michetti, M.1    Salamino, F.2    Tedesco, I.3    Averna, M.4    Minafra, R.5    Melloni, E.6    Pontremoli, S.7
  • 28
    • 0031839786 scopus 로고    scopus 로고
    • A novel aspect of calpain activation
    • K. Suzuki, and H. Sorimachi A novel aspect of calpain activation FEBS Lett. 433 1998 1 4
    • (1998) FEBS Lett. , vol.433 , pp. 1-4
    • Suzuki, K.1    Sorimachi, H.2
  • 29
    • 0028088153 scopus 로고
    • Calpain: New perspectives in molecular diversity and physiological- pathological involvement
    • T.C. Saido, H. Sorimachi, and K. Suzuki Calpain: new perspectives in molecular diversity and physiological-pathological involvement FASEB J. 8 1994 814 822
    • (1994) FASEB J. , vol.8 , pp. 814-822
    • Saido, T.C.1    Sorimachi, H.2    Suzuki, K.3
  • 30
    • 0037214421 scopus 로고    scopus 로고
    • Calpains mediates progresssive plasma membrane permeability and proteolysis of cytoskeleton-associated paxillin, talin, and vinculin during renal cell death
    • X. Liu, and R.G. Schnellmann Calpains mediates progresssive plasma membrane permeability and proteolysis of cytoskeleton-associated paxillin, talin, and vinculin during renal cell death J. Pharmacol. Exp. Ther. 304 2003 63 70
    • (2003) J. Pharmacol. Exp. Ther. , vol.304 , pp. 63-70
    • Liu, X.1    Schnellmann, R.G.2
  • 31
    • 0034655757 scopus 로고    scopus 로고
    • +ATPase and alkaline phosphatase on plasma membranes of renal proximal tubules
    • +ATPase and alkaline phosphatase on plasma membranes of renal proximal tubules Toxicol. Appl. Pharmacol. 164 2000 143 148
    • (2000) Toxicol. Appl. Pharmacol. , vol.164 , pp. 143-148
    • Trumper, L.1    Coux, G.2    Elías, M.M.3
  • 32
    • 0026573743 scopus 로고
    • +-ATPase activity from intact renal proximal tubule cells
    • +-ATPase activity from intact renal proximal tubule cells J. Cell. Sci. 101 1992 343 347
    • (1992) J. Cell. Sci. , vol.101 , pp. 343-347
    • Bertorello, A.M.1
  • 34
    • 0017390556 scopus 로고
    • A rapid, sensitive and versatile assay for protein using Coomassie Brilliant Blue G-250
    • J.J. Sedmak, and S.E. Grossberg A rapid, sensitive and versatile assay for protein using Coomassie Brilliant Blue G-250 Anal. Biochem. 79 1971 544 552
    • (1971) Anal. Biochem. , vol.79 , pp. 544-552
    • Sedmak, J.J.1    Grossberg, S.E.2
  • 36
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 37
  • 38
    • 0032563192 scopus 로고    scopus 로고
    • Structure of the ankyrin-binding domain of α-Na, K ATPase
    • Z. Zhang, P. Devajaran, A.L. Dorfman, and J.S. Morrow Structure of the ankyrin-binding domain of α-Na, K ATPase J. Biol. Chem. 273 1998 18681 18684
    • (1998) J. Biol. Chem. , vol.273 , pp. 18681-18684
    • Zhang, Z.1    Devajaran, P.2    Dorfman, A.L.3    Morrow, J.S.4
  • 41
    • 0029859715 scopus 로고    scopus 로고
    • Cellular ATP depletion induces disruption of the spectrin cytoskeletal network
    • B.A. Molitoris, R. Dahl, and M. Hosford Cellular ATP depletion induces disruption of the spectrin cytoskeletal network Am. J. Physiol. 271 1996 F790 F798
    • (1996) Am. J. Physiol. , vol.271
    • Molitoris, B.A.1    Dahl, R.2    Hosford, M.3
  • 42
    • 0000236332 scopus 로고    scopus 로고
    • Cytoskeletal alterations as a basis of cellular injury in acute renal failure
    • W.B. Saunders W.B. Saunders Company Philadelphia
    • S.J. Atkinson, and B.A. Molitoris Cytoskeletal alterations as a basis of cellular injury in acute renal failure W.B. Saunders Acute Renal Failure: A Companion to Brenner and Rector's the Kidney 2001 W.B. Saunders Company Philadelphia 119 130
    • (2001) Acute Renal Failure: A Companion to Brenner and Rector's the Kidney , pp. 119-130
    • Atkinson, S.J.1    Molitoris, B.A.2
  • 43
    • 0030908027 scopus 로고    scopus 로고
    • Effect of glycine on prelethal and poslethal increases in calpain activity in rat renal proximal tubules
    • C.L. Edelstein, H. Ling, P.E. Gengaro, R.A. Nemenoff, B.A. Bahr, and R.W. Schrier Effect of glycine on prelethal and poslethal increases in calpain activity in rat renal proximal tubules Kidney Int. 51 1997 1341 1351
    • (1997) Kidney Int. , vol.51 , pp. 1341-1351
    • Edelstein, C.L.1    Ling, H.2    Gengaro, P.E.3    Nemenoff, R.A.4    Bahr, B.A.5    Schrier, R.W.6
  • 44
    • 0036085349 scopus 로고    scopus 로고
    • Cytoprotective properties of novel nonpeptide calpain inhibitors in renal cells
    • X. Liu, J.F. Harriman, and R.G. Schnellmann Cytoprotective properties of novel nonpeptide calpain inhibitors in renal cells J. Pharmacol. Exp. Ther. 302 2002 88 94
    • (2002) J. Pharmacol. Exp. Ther. , vol.302 , pp. 88-94
    • Liu, X.1    Harriman, J.F.2    Schnellmann, R.G.3
  • 45
    • 0031910645 scopus 로고    scopus 로고
    • Examination of the mechanisms of action of diverse cytoprotectants in renal cell death
    • S.L. Waters, and R.G. Schnellmann Examination of the mechanisms of action of diverse cytoprotectants in renal cell death Toxicol. Pathol. 26 1998 58 63
    • (1998) Toxicol. Pathol. , vol.26 , pp. 58-63
    • Waters, S.L.1    Schnellmann, R.G.2
  • 48
    • 0037302537 scopus 로고    scopus 로고
    • Dissociation of spectrin-ankyrin complex as a basis for loss of Na-K ATPase polarity after ischemia
    • R. Woroniecki, J.R. Ferdinand, J.S. Morrow, and P. Devajaran Dissociation of spectrin-ankyrin complex as a basis for loss of Na-K ATPase polarity after ischemia Am. J. Physiol. 284 2003 F358 F364
    • (2003) Am. J. Physiol. , vol.284
    • Woroniecki, R.1    Ferdinand, J.R.2    Morrow, J.S.3    Devajaran, P.4
  • 49
    • 0027535150 scopus 로고
    • Degradation of spectrin and ankyrin in the ischemic rat kidney
    • B.R. Doctor, V. Bennet, and L.J. Mandel Degradation of spectrin and ankyrin in the ischemic rat kidney Am. J. Physiol. 264 1993 C1003 C1013
    • (1993) Am. J. Physiol. , vol.264
    • Doctor, B.R.1    Bennet, V.2    Mandel, L.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.