메뉴 건너뛰기




Volumn 276, Issue 4 45-4, 1999, Pages

Ischemia activates actin depolymerizing factor: Role in proximal tubule microvillar actin alterations

Author keywords

Actin cytoskeleton; Acute renal failure; ATP depletion; Cofilin; LIM kinase; Renal proximal tubule cell

Indexed keywords

ACTIN;

EID: 0032941377     PISSN: 1931857X     EISSN: 15221466     Source Type: Journal    
DOI: 10.1152/ajprenal.1999.276.4.f544     Document Type: Article
Times cited : (85)

References (45)
  • 1
    • 0029149885 scopus 로고
    • Reactivation of phosphorylated actin depolymerizing factor and identification of the regulatory site
    • Agnew, B. J., L. S. Minamide, and J. R. Bamburg. Reactivation of phosphorylated actin depolymerizing factor and identification of the regulatory site. J. Biol. Chem. 270: 17582-17587, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17582-17587
    • Agnew, B.J.1    Minamide, L.S.2    Bamburg, J.R.3
  • 3
    • 0028609124 scopus 로고
    • ATP depletion: A novel method to study junctional properties in epithelial tissues. I. Rearrangement of the actin cytoskeleton
    • Bacallao, R., A. Garfinkel, S. Monke, G. Zampighi, and L. J. Mandel. ATP depletion: a novel method to study junctional properties in epithelial tissues. I. Rearrangement of the actin cytoskeleton. J. Cell Sci. 107: 3301-3313, 1994.
    • (1994) J. Cell Sci. , vol.107 , pp. 3301-3313
    • Bacallao, R.1    Garfinkel, A.2    Monke, S.3    Zampighi, G.4    Mandel, L.J.5
  • 4
    • 0023571668 scopus 로고
    • Distribution and cellular localization of actin depolymerizing factor
    • Bamburg, J. R., and D. Bray. Distribution and cellular localization of actin depolymerizing factor. J. Cell Biol. 105: 2817-2825, 1987.
    • (1987) J. Cell Biol. , vol.105 , pp. 2817-2825
    • Bamburg, J.R.1    Bray, D.2
  • 5
    • 0022098747 scopus 로고
    • Effects of metabolic acidosis on viability of cells exposed to anoxia
    • Cell Physiol. 18
    • Bonventre, J. V., and J. Y. Cheung. Effects of metabolic acidosis on viability of cells exposed to anoxia. Am. J. Physiol. 249 (Cell Physiol. 18): C149-C159, 1985.
    • (1985) Am. J. Physiol. , vol.249
    • Bonventre, J.V.1    Cheung, J.Y.2
  • 6
    • 0026346859 scopus 로고
    • Effect of reversible ATP depletion on tight junction integrity
    • Renal Fluid Electrolyte Physiol. 30
    • Canfield, P. E., A. E. Geerdes, and B. A. Molitoris. Effect of reversible ATP depletion on tight junction integrity. Am. J. Physiol. 261 (Renal Fluid Electrolyte Physiol. 30): F1038-F1045, 1991.
    • (1991) Am. J. Physiol. , vol.261
    • Canfield, P.E.1    Geerdes, A.E.2    Molitoris, B.A.3
  • 7
    • 0030843484 scopus 로고    scopus 로고
    • Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: Implication in actin-based motility
    • Carlier, M. F., V. Laurent, J. Santolini, R. Melki, D. Dominique, X. Xia, Y. Hong, N. H. Chua, and D. Pantaloni. Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: implication in actin-based motility. J. Cell Biol. 136: 1307-1323, 1997.
    • (1997) J. Cell Biol. , vol.136 , pp. 1307-1323
    • Carlier, M.F.1    Laurent, V.2    Santolini, J.3    Melki, R.4    Dominique, D.5    Xia, X.6    Hong, Y.7    Chua, N.H.8    Pantaloni, D.9
  • 9
    • 0030783005 scopus 로고    scopus 로고
    • Unopposed phosphatase action initiates ezrin dysfunction: A potential mechanism for anoxic injury
    • Cell Physiol. 42
    • Chen, J., and L. J. Mandel. Unopposed phosphatase action initiates ezrin dysfunction: a potential mechanism for anoxic injury. Am. J. Physiol. 273 (Cell Physiol. 42): C710-C716, 1997.
    • (1997) Am. J. Physiol. , vol.273
    • Chen, J.1    Mandel, L.J.2
  • 10
    • 0017851122 scopus 로고
    • Tubular leakage and obstruction after renal ischemia: Structural functional correlations
    • Donohoe, J. F., M. A. Venkatachalam, D. B. Bernard, and N. G. Levinsky. Tubular leakage and obstruction after renal ischemia: structural functional correlations. Kidney Int. 13: 208-222, 1978.
    • (1978) Kidney Int. , vol.13 , pp. 208-222
    • Donohoe, J.F.1    Venkatachalam, M.A.2    Bernard, D.B.3    Levinsky, N.G.4
  • 11
    • 0028114458 scopus 로고
    • Extracellular acidosis minimizes actin cytoskeletal alterations during ATP depletion
    • Renal Fluid Electrolyte Physiol. 36
    • Fish, E. M., and B. A. Molitoris. Extracellular acidosis minimizes actin cytoskeletal alterations during ATP depletion. Am. J. Physiol. 267 (Renal Fluid Electrolyte Physiol. 36): F566-F572, 1994.
    • (1994) Am. J. Physiol. , vol.267
    • Fish, E.M.1    Molitoris, B.A.2
  • 13
    • 0017350242 scopus 로고
    • Studies on the cellular recovery from injury. II. Ultrastructural studies on the recovery of the pars convoluta of the proximal tubule of the rat kidney from temporary ischemia
    • Glaumann, B., H. Glaumann, I. K. Berezesky, and B. F. Trump. Studies on the cellular recovery from injury. II. Ultrastructural studies on the recovery of the pars convoluta of the proximal tubule of the rat kidney from temporary ischemia. Virchows Arch. 24: 1-18, 1977.
    • (1977) Virchows Arch. , vol.24 , pp. 1-18
    • Glaumann, B.1    Glaumann, H.2    Berezesky, I.K.3    Trump, B.F.4
  • 14
    • 0024504126 scopus 로고
    • Intracellular pH during "chemical hypoxia" in cultured rat hepatocytes. Protection by intracellular acidosis against the onset of cell death
    • Gores, G. J., A. L. Nieminen, B. E. Wray, B. Herman, and J. J. Lemasters. Intracellular pH during "chemical hypoxia" in cultured rat hepatocytes. Protection by intracellular acidosis against the onset of cell death. J. Clin. Invest. 83: 386-396, 1989.
    • (1989) J. Clin. Invest. , vol.83 , pp. 386-396
    • Gores, G.J.1    Nieminen, A.L.2    Wray, B.E.3    Herman, B.4    Lemasters, J.J.5
  • 15
    • 0024449827 scopus 로고
    • Membrane traffic in endocytosis: Insights from cell-free assays
    • Gruenberg, J., and K. E. Howell. Membrane traffic in endocytosis: insights from cell-free assays. Annu. Rev. Cell Biol. 5: 453-481, 1989.
    • (1989) Annu. Rev. Cell Biol. , vol.5 , pp. 453-481
    • Gruenberg, J.1    Howell, K.E.2
  • 16
    • 0027439319 scopus 로고
    • Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments
    • Hawkins, M., B. Pope, S. K. Maciver, and A. G. Weeds. Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments. Biochemistry 32: 9985-9993, 1993.
    • (1993) Biochemistry , vol.32 , pp. 9985-9993
    • Hawkins, M.1    Pope, B.2    Maciver, S.K.3    Weeds, A.G.4
  • 17
    • 0027494863 scopus 로고
    • Analysis of the interactions of actin depolymerizing factor with G- And F-actin
    • Hayden, S. M., P. S. Miller, A. Brauweiler, and J. R. Bamburg. Analysis of the interactions of actin depolymerizing factor with G- and F-actin. Biochemistry 32: 9994-10004, 1993.
    • (1993) Biochemistry , vol.32 , pp. 9994-10004
    • Hayden, S.M.1    Miller, P.S.2    Brauweiler, A.3    Bamburg, J.R.4
  • 18
    • 0026742611 scopus 로고
    • Microfilament disruption occurs very early in ischemic proximal tubule cell injury
    • Kellerman, P. S., and R. T. Bogusky. Microfilament disruption occurs very early in ischemic proximal tubule cell injury. Kidney Int. 42: 896-902, 1992.
    • (1992) Kidney Int. , vol.42 , pp. 896-902
    • Kellerman, P.S.1    Bogusky, R.T.2
  • 19
    • 0025150033 scopus 로고
    • Role of microfilaments in the maintenance of proximal tubule structural and functional integrity
    • Renal Fluid Electrolyte Physiol. 28
    • Kellerman, P. S., R. A. F. Clark, C. A. Hoilien, S. L. Linas, and B. A. Molitoris. Role of microfilaments in the maintenance of proximal tubule structural and functional integrity. Am. J. Physiol. 259 (Renal Fluid Electrolyte Physiol. 28): F279-F285, 1990.
    • (1990) Am. J. Physiol. , vol.259
    • Kellerman, P.S.1    Clark, R.A.F.2    Hoilien, C.A.3    Linas, S.L.4    Molitoris, B.A.5
  • 20
    • 0030797467 scopus 로고    scopus 로고
    • Cofilin promotes rapid actin filament turnover in vivo
    • Lappalainen, P., and D. G. Drubin. Cofilin promotes rapid actin filament turnover in vivo. Nature 388: 78-82, 1997.
    • (1997) Nature , vol.388 , pp. 78-82
    • Lappalainen, P.1    Drubin, D.G.2
  • 22
    • 0028357931 scopus 로고
    • Actophorin preferentially binds monomeric ADP-actin over ATP-bound actin: Consequences for cell locomotion
    • Maciver, S. K., and A. Weeds. Actophorin preferentially binds monomeric ADP-actin over ATP-bound actin: consequences for cell locomotion. FEBS Lett. 347: 251-256, 1994.
    • (1994) FEBS Lett. , vol.347 , pp. 251-256
    • Maciver, S.K.1    Weeds, A.2
  • 23
    • 0030820734 scopus 로고    scopus 로고
    • Cofilin changes the twist of F-actin: Implications for actin filament dynamics and cellular function
    • McGough, A., B. Pope, W. Chiu, and A. Weeds. Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function. J. Cell Biol. 138: 771-781, 1997.
    • (1997) J. Cell Biol. , vol.138 , pp. 771-781
    • McGough, A.1    Pope, B.2    Chiu, W.3    Weeds, A.4
  • 24
    • 0031952055 scopus 로고    scopus 로고
    • Actin depolymerizing factor and cofilin phosphorylation dynamics: Response to signals that regulate neurite extension
    • Meberg, P. J., S. Ono, L. S. Minamide, M. Takahashi, and J. R. Bamburg. Actin depolymerizing factor and cofilin phosphorylation dynamics: response to signals that regulate neurite extension. Cell Motil. Cytoskeleton 39: 172-190, 1998.
    • (1998) Cell Motil. Cytoskeleton , vol.39 , pp. 172-190
    • Meberg, P.J.1    Ono, S.2    Minamide, L.S.3    Takahashi, M.4    Bamburg, J.R.5
  • 25
    • 0025827433 scopus 로고
    • Ischemia-induced loss of epithelial polarity: Potential role of the actin cytoskeleton
    • (Renal Fluid Electrolyte Physiol. 29)
    • Molitoris, B. A. Ischemia-induced loss of epithelial polarity: potential role of the actin cytoskeleton. Am. J. Physiol. 260 (Renal Fluid Electrolyte Physiol. 29): F769-F778, 1991.
    • (1991) Am. J. Physiol. , vol.260
    • Molitoris, B.A.1
  • 26
    • 33751318939 scopus 로고    scopus 로고
    • Putting the actin cytoskeleton into perspective: Pathophysiology of ischemic alterations
    • Renal Physiol. 41
    • Molitoris, B. A. Putting the actin cytoskeleton into perspective: pathophysiology of ischemic alterations. Am. J. Physiol. 272 (Renal Physiol. 41): F430-F433, 1997.
    • (1997) Am. J. Physiol. , vol.272
    • Molitoris, B.A.1
  • 28
    • 0024439472 scopus 로고
    • Ischemic-induced loss of epithelial polarity. Role of the tight junction
    • Molitoris, B. A., S. A. Falk, and R. H. Dahl. Ischemic-induced loss of epithelial polarity. Role of the tight junction. J. Clin. Invest. 84: 1334-1339, 1989.
    • (1989) J. Clin. Invest. , vol.84 , pp. 1334-1339
    • Molitoris, B.A.1    Falk, S.A.2    Dahl, R.H.3
  • 30
    • 0022336834 scopus 로고
    • Ischemia induces partial loss of surface membrane polarity and accumulation of putative calcium ionophores
    • Molitoris, B. A., P. D. Wilson, R. W. Schrier, and F. R. Simon. Ischemia induces partial loss of surface membrane polarity and accumulation of putative calcium ionophores. J. Clin. Invest. 76: 2097-2105, 1985.
    • (1985) J. Clin. Invest. , vol.76 , pp. 2097-2105
    • Molitoris, B.A.1    Wilson, P.D.2    Schrier, R.W.3    Simon, F.R.4
  • 31
    • 0028839660 scopus 로고
    • The ADF/cofilin proteins: Stimulus-responsive modulators of actin dynamics
    • Moon, A., and D. G. Drubin. The ADF/cofilin proteins: stimulus-responsive modulators of actin dynamics. Mol. Biol. Cell 6: 1423-1431, 1995.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1423-1431
    • Moon, A.1    Drubin, D.G.2
  • 32
    • 0027209983 scopus 로고
    • Isolation and characterization of a regulated form of actin depolymerizing factor
    • Morgan, T. E., R. O. Lockerbie, L. S. Minamide, M. D. Browning, and J. R. Bamburg. Isolation and characterization of a regulated form of actin depolymerizing factor. J. Cell Biol. 122: 623-633, 1993.
    • (1993) J. Cell Biol. , vol.122 , pp. 623-633
    • Morgan, T.E.1    Lockerbie, R.O.2    Minamide, L.S.3    Browning, M.D.4    Bamburg, J.R.5
  • 34
    • 0024359293 scopus 로고
    • Cytosolic ionized calcium and bleb formation after acute cell injury of cultured rabbit renal tubule cells
    • Phelps, P. C., M. W. Smith, and B. F. Trump. Cytosolic ionized calcium and bleb formation after acute cell injury of cultured rabbit renal tubule cells. Lab. Invest. 60: 630-642, 1989.
    • (1989) Lab. Invest. , vol.60 , pp. 630-642
    • Phelps, P.C.1    Smith, M.W.2    Trump, B.F.3
  • 35
    • 0030821155 scopus 로고    scopus 로고
    • Xenopus actin depolymerizing factor/cofilin (XAC) is responsible for the turnover of actin filaments in Listeria monocytogenes tails
    • Rosenblatt, J., B. J. Agnew, H. Abe, J. R. Bamburg, and T. J. Mitchison. Xenopus actin depolymerizing factor/cofilin (XAC) is responsible for the turnover of actin filaments in Listeria monocytogenes tails. J. Cell Biol. 136: 1323-1332, 1997.
    • (1997) J. Cell Biol. , vol.136 , pp. 1323-1332
    • Rosenblatt, J.1    Agnew, B.J.2    Abe, H.3    Bamburg, J.R.4    Mitchison, T.J.5
  • 36
    • 0029781191 scopus 로고    scopus 로고
    • Calcium dependence of integrity of the actin cytoskeleton of proximal tubule cell microvilli
    • Renal Fluid Electrolyte Physiol. 40
    • Sogabe, K., N. F. Roeser, J. A. Davis, S. Nurko, M. A. Venkatachalam, and J. M. Weinberg. Calcium dependence of integrity of the actin cytoskeleton of proximal tubule cell microvilli. Am. J. Physiol. 271 (Renal Fluid Electrolyte Physiol. 40): F292-F303, 1996.
    • (1996) Am. J. Physiol. , vol.271
    • Sogabe, K.1    Roeser, N.F.2    Davis, J.A.3    Nurko, S.4    Venkatachalam, M.A.5    Weinberg, J.M.6
  • 38
    • 0031691367 scopus 로고    scopus 로고
    • Mechanisms of cellular injury in ischemic ARF
    • Sutton, T. A., and B. A. Molitoris. Mechanisms of cellular injury in ischemic ARF. Semin. Nephrol. 18: 490-497, 1998.
    • (1998) Semin. Nephrol. , vol.18 , pp. 490-497
    • Sutton, T.A.1    Molitoris, B.A.2
  • 40
    • 0030798735 scopus 로고    scopus 로고
    • Accelerating on a treadmill: ADF/cofilin promotes rapid actin filament turnover in the dynamic cytoskeleton
    • Theriot, J. A. Accelerating on a treadmill: ADF/cofilin promotes rapid actin filament turnover in the dynamic cytoskeleton. J. Cell Biol. 136: 1165-1168, 1997.
    • (1997) J. Cell Biol. , vol.136 , pp. 1165-1168
    • Theriot, J.A.1
  • 41
    • 0018142634 scopus 로고
    • Ischemic damage and repair in the rat proximal tubule: Difference among the S1, S2 and S3 segments
    • Venkatachalam, M. A., D. B. Bernard, J. F. Donohoe, and N. G. Levinsky. Ischemic damage and repair in the rat proximal tubule: difference among the S1, S2 and S3 segments. Kidney Int. 14: 31-49, 1978.
    • (1978) Kidney Int. , vol.14 , pp. 31-49
    • Venkatachalam, M.A.1    Bernard, D.B.2    Donohoe, J.F.3    Levinsky, N.G.4
  • 42
    • 0019868584 scopus 로고
    • Mechanism of proximal tubule brush border loss and regeneration following mild renal ischemia
    • Venkatachalam, M. A., D. B. Jones, H. G. Rennke, D. Sandstrom, and Y. Patel. Mechanism of proximal tubule brush border loss and regeneration following mild renal ischemia. Lab. Invest. 45: 355-365, 1981.
    • (1981) Lab. Invest. , vol.45 , pp. 355-365
    • Venkatachalam, M.A.1    Jones, D.B.2    Rennke, H.G.3    Sandstrom, D.4    Patel, Y.5
  • 44
    • 0028854209 scopus 로고
    • Modulation by Gly, Ca, and acidosis on injury-associated unesterified fatty acid accumulation in proximal tubule cells
    • Renal Fluid Electrolyte Physiol. 37
    • Weinberg, J. M., M. A. Venkatachalam, H. Goldberg, N. F. Roeser, and J. A. Davis. Modulation by Gly, Ca, and acidosis on injury-associated unesterified fatty acid accumulation in proximal tubule cells. Am. J. Physiol. 268 (Renal Fluid Electrolyte Physiol. 37): F110-F121, 1995.
    • (1995) Am. J. Physiol. , vol.268
    • Weinberg, J.M.1    Venkatachalam, M.A.2    Goldberg, H.3    Roeser, N.F.4    Davis, J.A.5
  • 45
    • 0032565769 scopus 로고    scopus 로고
    • Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization
    • Yang, N., O. Higuchi, K. Ohashi, K. Nagata, A. Wada, K. Kangawa, E. Nishida, and K. Mizuno. Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization. Nature 393: 809-812, 1998.
    • (1998) Nature , vol.393 , pp. 809-812
    • Yang, N.1    Higuchi, O.2    Ohashi, K.3    Nagata, K.4    Wada, A.5    Kangawa, K.6    Nishida, E.7    Mizuno, K.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.