메뉴 건너뛰기




Volumn 580, Issue 9, 2006, Pages 2233-2237

Reversible inhibition of caspase-3 activity by iron(III). Potential role in physiological control of apoptosis

Author keywords

Caspase 3; Desferoxamine; Iron; Protein disulfide isomerase

Indexed keywords

CASPASE 3; CASPASE 3 INHIBITOR; DEFEROXAMINE; FERRIC ION; PROTEIN DISULFIDE ISOMERASE;

EID: 33645976203     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2006.03.031     Document Type: Article
Times cited : (16)

References (37)
  • 1
    • 0029670265 scopus 로고    scopus 로고
    • ICE/CED3-like proteases as therapeutic targets for the control of inappropriate apoptosis
    • Nicholson D. ICE/CED3-like proteases as therapeutic targets for the control of inappropriate apoptosis. Nat. Biotechnol. 14 (1996) 297-301
    • (1996) Nat. Biotechnol. , vol.14 , pp. 297-301
    • Nicholson, D.1
  • 2
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: enemies within
    • Thornberry N.A., and Lazebnik Y. Caspases: enemies within. Science 281 (1998) 1312-1316
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 3
    • 2642689658 scopus 로고    scopus 로고
    • Proteases to die for
    • Cryns V., and Yuan J. Proteases to die for. Genes Dev. 12 (1998) 1551-1570
    • (1998) Genes Dev. , vol.12 , pp. 1551-1570
    • Cryns, V.1    Yuan, J.2
  • 6
    • 0028102478 scopus 로고
    • Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE
    • Lazebnik Y.A., Kaufmann S.H., Desnoyers S., Poirier G.G., and Earnshaw W.C. Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE. Nature 371 (1994) 346-347
    • (1994) Nature , vol.371 , pp. 346-347
    • Lazebnik, Y.A.1    Kaufmann, S.H.2    Desnoyers, S.3    Poirier, G.G.4    Earnshaw, W.C.5
  • 8
    • 10544220838 scopus 로고    scopus 로고
    • Heteronuclear ribonucleoproteins C1 and C2, components of the spliceosome, are specific targets of interleukin 1beta-converting enzyme-like proteases in apoptosis
    • Waterhouse N., Kumar S., Song Q., Strike P., Sparrow L., Dreyfuss G., Alnemri E.S., Litwack G., Lavin M., and Watters D. Heteronuclear ribonucleoproteins C1 and C2, components of the spliceosome, are specific targets of interleukin 1beta-converting enzyme-like proteases in apoptosis. JBC 271 (1996) 29335-29341
    • (1996) JBC , vol.271 , pp. 29335-29341
    • Waterhouse, N.1    Kumar, S.2    Song, Q.3    Strike, P.4    Sparrow, L.5    Dreyfuss, G.6    Alnemri, E.S.7    Litwack, G.8    Lavin, M.9    Watters, D.10
  • 10
    • 0030462563 scopus 로고    scopus 로고
    • Specific cleavage of the retinoblastoma protein by an ICE-like protease in apoptosis
    • Janicke R.U., Walker P.A., Lin X.Y., and Porter A.G. Specific cleavage of the retinoblastoma protein by an ICE-like protease in apoptosis. EMBO J. 15 (1996) 6969-6978
    • (1996) EMBO J. , vol.15 , pp. 6969-6978
    • Janicke, R.U.1    Walker, P.A.2    Lin, X.Y.3    Porter, A.G.4
  • 12
    • 0031576527 scopus 로고    scopus 로고
    • Nitric oxide reversibly inhibits seven members of the caspase family via S-nitrosylation
    • Li J., Billiar T.R., Talanian R.V., and Kim Y.M. Nitric oxide reversibly inhibits seven members of the caspase family via S-nitrosylation. BBRC 240 (1997) 419-424
    • (1997) BBRC , vol.240 , pp. 419-424
    • Li, J.1    Billiar, T.R.2    Talanian, R.V.3    Kim, Y.M.4
  • 13
    • 0030662226 scopus 로고    scopus 로고
    • Nitric oxide inhibits apoptosis by preventing increases in caspase-3-like activity via two distinct mechanisms
    • Kim Y.M., Talanian R.V., and Billiar T.R. Nitric oxide inhibits apoptosis by preventing increases in caspase-3-like activity via two distinct mechanisms. JBC 272 (1997) 31138-31148
    • (1997) JBC , vol.272 , pp. 31138-31148
    • Kim, Y.M.1    Talanian, R.V.2    Billiar, T.R.3
  • 14
    • 0035816440 scopus 로고    scopus 로고
    • Caspases are reversibly inactivated by hydrogen peroxide
    • Borutaite V., and Brown G.C. Caspases are reversibly inactivated by hydrogen peroxide. FEBS Lett. 500 (2001) 114-118
    • (2001) FEBS Lett. , vol.500 , pp. 114-118
    • Borutaite, V.1    Brown, G.C.2
  • 16
    • 0034533678 scopus 로고    scopus 로고
    • Visualization of labile zinc and its role in apoptosis of primary airway epithelial cells and cell lines
    • Troung-Tran A.Q., Ruffin R.E., and Zalewski P.D. Visualization of labile zinc and its role in apoptosis of primary airway epithelial cells and cell lines. Am. J. Physiol. 279 (2000) L1172-L1183
    • (2000) Am. J. Physiol. , vol.279
    • Troung-Tran, A.Q.1    Ruffin, R.E.2    Zalewski, P.D.3
  • 17
    • 0026472376 scopus 로고
    • Iron metabolism - new perspectives in view
    • Crichton R.R., and Ward R.J. Iron metabolism - new perspectives in view. Biochemistry 31 (1992) 11255-11264
    • (1992) Biochemistry , vol.31 , pp. 11255-11264
    • Crichton, R.R.1    Ward, R.J.2
  • 18
    • 0020579762 scopus 로고
    • Binding of apotransferrin to K562 cells: explanation of the transferrin cycle
    • Klausner R.D., Ashwell G., Van Renswoude J., Harford J.B., and Bridges K.R. Binding of apotransferrin to K562 cells: explanation of the transferrin cycle. PNAS USA 80 (1983) 2263-2266
    • (1983) PNAS USA , vol.80 , pp. 2263-2266
    • Klausner, R.D.1    Ashwell, G.2    Van Renswoude, J.3    Harford, J.B.4    Bridges, K.R.5
  • 20
    • 0027290910 scopus 로고
    • Differences in transferrin response and numbers of transferrin receptors in rat and human mammary carcinoma lines of different metastatic potentials
    • Inoue T., Cavanaugh P.G., Steck P.A., Brunner N., and Nicolson G.L. Differences in transferrin response and numbers of transferrin receptors in rat and human mammary carcinoma lines of different metastatic potentials. J. Cell. Physiol. 156 (1993) 212-217
    • (1993) J. Cell. Physiol. , vol.156 , pp. 212-217
    • Inoue, T.1    Cavanaugh, P.G.2    Steck, P.A.3    Brunner, N.4    Nicolson, G.L.5
  • 21
    • 0029932034 scopus 로고    scopus 로고
    • Iron-induced carcinogenesis: the role of redox regulation
    • Toyokuni S. Iron-induced carcinogenesis: the role of redox regulation. FRBM 20 (1996) 553-566
    • (1996) FRBM , vol.20 , pp. 553-566
    • Toyokuni, S.1
  • 22
    • 2442761708 scopus 로고    scopus 로고
    • The protein disulphide-isomerase family: unravelling a string of folds
    • Ferrari D.M., and Soling H.D. The protein disulphide-isomerase family: unravelling a string of folds. Biochem. J. 339 (1999) 1-10
    • (1999) Biochem. J. , vol.339 , pp. 1-10
    • Ferrari, D.M.1    Soling, H.D.2
  • 23
    • 0026740150 scopus 로고
    • Mechanisms involved in degradation of human insulin by cytosolic fractions of human, monkey, and rat liver
    • Wroblewski V.J., Masnyk M., Khambatta S.S., and Becker G.W. Mechanisms involved in degradation of human insulin by cytosolic fractions of human, monkey, and rat liver. Diabetes 41 (1992) 539-547
    • (1992) Diabetes , vol.41 , pp. 539-547
    • Wroblewski, V.J.1    Masnyk, M.2    Khambatta, S.S.3    Becker, G.W.4
  • 24
    • 0028225291 scopus 로고
    • Dissecting the mechanism of protein disulfide isomerase: catalysis of disulfide bond formation in a model peptide
    • Darby N.J., Freedman R.B., and Creighton T.E. Dissecting the mechanism of protein disulfide isomerase: catalysis of disulfide bond formation in a model peptide. Biochemistry 33 (1994) 7937-7947
    • (1994) Biochemistry , vol.33 , pp. 7937-7947
    • Darby, N.J.1    Freedman, R.B.2    Creighton, T.E.3
  • 25
    • 0030724094 scopus 로고    scopus 로고
    • Protein disulfide isomerase and assisted protein folding
    • Gilbert H.F. Protein disulfide isomerase and assisted protein folding. JBC 272 (1997) 29399-29402
    • (1997) JBC , vol.272 , pp. 29399-29402
    • Gilbert, H.F.1
  • 26
    • 3042572562 scopus 로고    scopus 로고
    • Zinc-dependent dimerization of the folding catalyst, protein disulfide isomerase
    • Solovyov A., and Gilbert H.F. Zinc-dependent dimerization of the folding catalyst, protein disulfide isomerase. Protein Sci. 13 (2004) 1902-1907
    • (2004) Protein Sci. , vol.13 , pp. 1902-1907
    • Solovyov, A.1    Gilbert, H.F.2
  • 27
    • 0242331275 scopus 로고    scopus 로고
    • Protein disulfide isomerase, a multifunctional protein chaperone, shows copper-binding activity
    • Narindrasorasak S., Yao P., and Sarkar B. Protein disulfide isomerase, a multifunctional protein chaperone, shows copper-binding activity. BBRC 33 (2003) 405-414
    • (2003) BBRC , vol.33 , pp. 405-414
    • Narindrasorasak, S.1    Yao, P.2    Sarkar, B.3
  • 28
    • 0034647447 scopus 로고    scopus 로고
    • Structure of a thioredoxin-like [2Fe-2S] ferredoxin from Aquifex aeolicus
    • Yeh A.P., Chatelet C., Soltis S.M., Kuhn P., Meyer J., and Rees D.C. Structure of a thioredoxin-like [2Fe-2S] ferredoxin from Aquifex aeolicus. J. Mol. Biol. 300 (2000) 587-595
    • (2000) J. Mol. Biol. , vol.300 , pp. 587-595
    • Yeh, A.P.1    Chatelet, C.2    Soltis, S.M.3    Kuhn, P.4    Meyer, J.5    Rees, D.C.6
  • 29
    • 15744403464 scopus 로고    scopus 로고
    • Characterization of the S-denitrosation activity of protein disulfide isomerase
    • Sliskovic I., Raturi A., and Mutus B. Characterization of the S-denitrosation activity of protein disulfide isomerase. JBC 280 (2005) 8733-8741
    • (2005) JBC , vol.280 , pp. 8733-8741
    • Sliskovic, I.1    Raturi, A.2    Mutus, B.3
  • 30
    • 0030881603 scopus 로고    scopus 로고
    • Biochemical characteristics of caspases-3, -6, -7, and -8
    • Stennicke H.R., and Salvesen G.S. Biochemical characteristics of caspases-3, -6, -7, and -8. JBC 272 (1997) 25719-25723
    • (1997) JBC , vol.272 , pp. 25719-25723
    • Stennicke, H.R.1    Salvesen, G.S.2
  • 31
    • 0023899855 scopus 로고
    • Rapid colorimetric micromethod for the quantitation of complexed iron in biological samples
    • Fish W.W. Rapid colorimetric micromethod for the quantitation of complexed iron in biological samples. Methods Enzymol. 54 (1988) 357-364
    • (1988) Methods Enzymol. , vol.54 , pp. 357-364
    • Fish, W.W.1
  • 33
    • 20444411531 scopus 로고    scopus 로고
    • Characterization of human glutaredoxin 2 as iron-sulfur protein: a possible role as redox sensor
    • Lillig C.H., Berndt C., Vergnolle O., Lonn M.E., Hudemann C., Bill E., and Holmgren A. Characterization of human glutaredoxin 2 as iron-sulfur protein: a possible role as redox sensor. PNAS 120 (2005) 8168-8173
    • (2005) PNAS , vol.120 , pp. 8168-8173
    • Lillig, C.H.1    Berndt, C.2    Vergnolle, O.3    Lonn, M.E.4    Hudemann, C.5    Bill, E.6    Holmgren, A.7
  • 34
    • 0034615941 scopus 로고    scopus 로고
    • Up-regulation of protein-disulfide isomerase in response to hypoxia/brain ischemia and its protective effect against apoptotic cell death
    • Tanaka S., Uehara T., and Nomura Y. Up-regulation of protein-disulfide isomerase in response to hypoxia/brain ischemia and its protective effect against apoptotic cell death. JBC 275 (2000) 10388-10393
    • (2000) JBC , vol.275 , pp. 10388-10393
    • Tanaka, S.1    Uehara, T.2    Nomura, Y.3
  • 35
    • 0027889386 scopus 로고
    • Protein disulfide-isomerase: role in biosynthesis of secretory proteins
    • Bulleid N. Protein disulfide-isomerase: role in biosynthesis of secretory proteins. Adv. Protein Chem. 44 (1993) 125-150
    • (1993) Adv. Protein Chem. , vol.44 , pp. 125-150
    • Bulleid, N.1
  • 36
    • 0036836665 scopus 로고    scopus 로고
    • Proteins of the PDI family: unpredicted non-ER locations and functions
    • Turano C., Coppari S., Altieri F., and Ferraro A. Proteins of the PDI family: unpredicted non-ER locations and functions. J. Cell. Physiol. 193 (2002) 154-163
    • (2002) J. Cell. Physiol. , vol.193 , pp. 154-163
    • Turano, C.1    Coppari, S.2    Altieri, F.3    Ferraro, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.