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Volumn 227, Issue 1-2, 2006, Pages 21-35

Calmodulin mediates sulfur mustard toxicity in human keratinocytes

Author keywords

Apoptosis; Calcineurin; CaM; Caspase 3; SM

Indexed keywords

1 [N,O BIS(5 ISOQUINOLINESULFONYL) N METHYLTYROSYL] 4 PHENYLPIPERAZINE; CALCINEURIN; CALCINEURIN INHIBITOR; CALMODULIN; CALMODULIN INHIBITOR; CASPASE 3; CASPASE 6; CASPASE 7; CASPASE 9; CYCLOSPORIN A; FAS ANTIGEN; MUSTARD GAS; N (4 AMINOBUTYL) 2 NAPSYLAMIDE; N (4 AMINOBUTYL) 5 CHLORO 2 NAPSYLAMIDE; N [2 [[N [3 (4 CHLOROPHENYL) 2 PROPENYL] N METHYLAMINO]METHYL]PHENYL] N (2 HYDROXYETHYL) 4 METHOXYBENZENESULFONAMIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PROTEIN BAD; RETROVIRUS VECTOR; RNA;

EID: 33748749702     PISSN: 0300483X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tox.2006.06.019     Document Type: Article
Times cited : (40)

References (92)
  • 1
    • 0026085940 scopus 로고
    • Effect of the calmodulin antagonist CGS 9343B on skin burns
    • Beitner R., Chen-Zion M., and Bassukevitz Y. Effect of the calmodulin antagonist CGS 9343B on skin burns. Gen. Pharmacol. 22 (1991) 67-72
    • (1991) Gen. Pharmacol. , vol.22 , pp. 67-72
    • Beitner, R.1    Chen-Zion, M.2    Bassukevitz, Y.3
  • 3
    • 0032472329 scopus 로고    scopus 로고
    • Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochondrial transmembrane depolarisation
    • Bossy-Wetzel E., Newmeyer D.D., and Green D.R. Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochondrial transmembrane depolarisation. EMBO J. 17 (1998) 37-49
    • (1998) EMBO J. , vol.17 , pp. 37-49
    • Bossy-Wetzel, E.1    Newmeyer, D.D.2    Green, D.R.3
  • 4
    • 0029890823 scopus 로고    scopus 로고
    • Apopain/CPP32 cleaves proteins that are essential for cellular repair: a fundamental principle of apoptotic death
    • Casciola-Rosen L., Nicholson D., Chong T., Rowan K., Thornberry N., Miller D., and Rosen A. Apopain/CPP32 cleaves proteins that are essential for cellular repair: a fundamental principle of apoptotic death. J. Exp. Med. 183 (1996) 1957-1964
    • (1996) J. Exp. Med. , vol.183 , pp. 1957-1964
    • Casciola-Rosen, L.1    Nicholson, D.2    Chong, T.3    Rowan, K.4    Thornberry, N.5    Miller, D.6    Rosen, A.7
  • 5
    • 0031056002 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent, cytoskeletal-associated protein kinase, with cell death-inducing functions that depend on its catalytic activity
    • 2+/calmodulin-dependent, cytoskeletal-associated protein kinase, with cell death-inducing functions that depend on its catalytic activity. EMBO J. 16 (1997) 998-1008
    • (1997) EMBO J. , vol.16 , pp. 998-1008
    • Cohen, O.1    Feinstein, E.2    Kimchi, A.3
  • 7
    • 0030702123 scopus 로고    scopus 로고
    • Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
    • Datta S.R., Dudek H., Tao X., Masters S., Fu H., Gotoh Y., and Greenberg M.E. Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery. Cell 91 (1997) 231-241
    • (1997) Cell , vol.91 , pp. 231-241
    • Datta, S.R.1    Dudek, H.2    Tao, X.3    Masters, S.4    Fu, H.5    Gotoh, Y.6    Greenberg, M.E.7
  • 8
    • 0030298093 scopus 로고    scopus 로고
    • Reduced level of calmodulin in PC12 cells induced by stable expression of calmodulin antisense RNA inhibits cell proliferation and induces neurite outgrowth
    • Davidkova G., Zhang S.P., Nichols R.A., and Weiss B. Reduced level of calmodulin in PC12 cells induced by stable expression of calmodulin antisense RNA inhibits cell proliferation and induces neurite outgrowth. Neuroscience 75 (1996) 1003-1019
    • (1996) Neuroscience , vol.75 , pp. 1003-1019
    • Davidkova, G.1    Zhang, S.P.2    Nichols, R.A.3    Weiss, B.4
  • 9
    • 0023006881 scopus 로고
    • Isolation of the yeast calmodulin gene: calmodulin is an essential protein
    • Davis T.N., Urdea M.S., Masiarz F.R., and Thorner J. Isolation of the yeast calmodulin gene: calmodulin is an essential protein. Cell 47 (1986) 423-431
    • (1986) Cell , vol.47 , pp. 423-431
    • Davis, T.N.1    Urdea, M.S.2    Masiarz, F.R.3    Thorner, J.4
  • 10
    • 1842333237 scopus 로고    scopus 로고
    • Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt
    • del Peso L., Gonzalez-Garcia M., Page C., Herrera R., and Nunez G. Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt. Science 278 (1997) 687-689
    • (1997) Science , vol.278 , pp. 687-689
    • del Peso, L.1    Gonzalez-Garcia, M.2    Page, C.3    Herrera, R.4    Nunez, G.5
  • 12
    • 33748753702 scopus 로고    scopus 로고
    • Fischer, R., Koller, M., Flura, M., Mathews, S., Strehler-Page, M.A., Krebs, J., Penniston, J.T., Carafoli, E., Strehler, E.E., Shindo, Y., Witt, E., Han, D., Epstein, W., Packer, L., 1988. Multiple divergent mRNAs code for a single human calmodulin.
  • 13
    • 0018867301 scopus 로고
    • The genetic toxicology of nitrogen and sulphur mustard
    • Fox M., and Scott D. The genetic toxicology of nitrogen and sulphur mustard. Mutat. Res. 75 (1980) 131-168
    • (1980) Mutat. Res. , vol.75 , pp. 131-168
    • Fox, M.1    Scott, D.2
  • 14
    • 0347625386 scopus 로고    scopus 로고
    • Platelet calmodulin levels in adolescent idiopathic scoliosis. Do the levels correlate with curve progression and severity?
    • Geoffrey Burwell R., and Dangerfield P.H. Platelet calmodulin levels in adolescent idiopathic scoliosis. Do the levels correlate with curve progression and severity?. Spine 28 (2003) 2036-2037
    • (2003) Spine , vol.28 , pp. 2036-2037
    • Geoffrey Burwell, R.1    Dangerfield, P.H.2
  • 17
    • 0018865014 scopus 로고
    • Calcium regulation of growth and differentiation of mouse epidermal cells in culture
    • Hennings H., Michael D., Cheng C., Steinert P., Holbrook K., and Yuspa S.H. Calcium regulation of growth and differentiation of mouse epidermal cells in culture. Cell 19 (1980) 245-254
    • (1980) Cell , vol.19 , pp. 245-254
    • Hennings, H.1    Michael, D.2    Cheng, C.3    Steinert, P.4    Holbrook, K.5    Yuspa, S.H.6
  • 18
    • 0020643734 scopus 로고
    • Naphthalenesulfonamides as calmodulin antagonists
    • Hidaka H., and Tanaka T. Naphthalenesulfonamides as calmodulin antagonists. Meth. Enzymol. 102 (1983) 185-194
    • (1983) Meth. Enzymol. , vol.102 , pp. 185-194
    • Hidaka, H.1    Tanaka, T.2
  • 19
    • 2142721829 scopus 로고    scopus 로고
    • Interference of BAD (Bcl-xL/Bcl-2-associated death promoter)-induced apoptosis in mammalian cells by 14-3-3 isoforms and P11
    • Hsu S.Y., Kaipia A., Zhu L., and Hsueh A.J. Interference of BAD (Bcl-xL/Bcl-2-associated death promoter)-induced apoptosis in mammalian cells by 14-3-3 isoforms and P11. Mol. Endocrinol. 11 (1997) 1858-1867
    • (1997) Mol. Endocrinol. , vol.11 , pp. 1858-1867
    • Hsu, S.Y.1    Kaipia, A.2    Zhu, L.3    Hsueh, A.J.4
  • 21
    • 0018600206 scopus 로고
    • Treatment of psoriasis vulgaris with external sulfur mustard gas with particular reference to its potential carcinogenic risk. III. Clinical and experimental studies on the extent of percutaneous and inhalational uptake of sulfur mustard gas
    • Illig L., Paul E., Eyer P., Weger N., and Born W. Treatment of psoriasis vulgaris with external sulfur mustard gas with particular reference to its potential carcinogenic risk. III. Clinical and experimental studies on the extent of percutaneous and inhalational uptake of sulfur mustard gas. Z. Hautkr. 54 (1979) 941-951
    • (1979) Z. Hautkr. , vol.54 , pp. 941-951
    • Illig, L.1    Paul, E.2    Eyer, P.3    Weger, N.4    Born, W.5
  • 22
  • 23
    • 0034570328 scopus 로고    scopus 로고
    • Treatment of skin injuries induced by sulfur mustard with calmodulin antagonists, using the pig model
    • Kadar T., Fishbeine E., Meshulam Y., Sahar R., Chapman S., Liani H., Barness I., and Amir A. Treatment of skin injuries induced by sulfur mustard with calmodulin antagonists, using the pig model. J. Appl. Toxicol. 20 Suppl 1 (2000) S133-S136
    • (2000) J. Appl. Toxicol. , vol.20 , Issue.SUPPL. 1
    • Kadar, T.1    Fishbeine, E.2    Meshulam, Y.3    Sahar, R.4    Chapman, S.5    Liani, H.6    Barness, I.7    Amir, A.8
  • 25
    • 0030579099 scopus 로고    scopus 로고
    • Effects of calmodulin antagonists and anesthetics on the skin lesions induced by 2-chloroethylethyl sulfide
    • Kim Y.B., Hur G.H., Choi D.S., Shin S., Han B., Lee Y., and Sok D. Effects of calmodulin antagonists and anesthetics on the skin lesions induced by 2-chloroethylethyl sulfide. Eur. J. Pharmacol. 313 (1996) 107-114
    • (1996) Eur. J. Pharmacol. , vol.313 , pp. 107-114
    • Kim, Y.B.1    Hur, G.H.2    Choi, D.S.3    Shin, S.4    Han, B.5    Lee, Y.6    Sok, D.7
  • 26
    • 0025973144 scopus 로고
    • Calmodulin levels in oestrogen receptor positive and negative human breast tumours
    • Krishnaraju K., Murugesan K., Vij U., Kapur B.M., and Farooq A. Calmodulin levels in oestrogen receptor positive and negative human breast tumours. Br. J. Cancer 63 (1991) 346-347
    • (1991) Br. J. Cancer , vol.63 , pp. 346-347
    • Krishnaraju, K.1    Murugesan, K.2    Vij, U.3    Kapur, B.M.4    Farooq, A.5
  • 28
    • 0028985962 scopus 로고
    • Chelation of intracellular calcium inhibits murine keratinocyte differentiation in vitro
    • Li L., Tucker R.W., Hennings H., and Yuspa S. Chelation of intracellular calcium inhibits murine keratinocyte differentiation in vitro. J. Cell. Physiol. 163 (1995) 105-114
    • (1995) J. Cell. Physiol. , vol.163 , pp. 105-114
    • Li, L.1    Tucker, R.W.2    Hennings, H.3    Yuspa, S.4
  • 29
    • 0033806417 scopus 로고    scopus 로고
    • Effect of zinc on cellular levels of calmodulin and cyclic adenosine monophosphate in the adipocyte
    • Lin P.Y., Lin W.H., Tsou C.T., Song Y.M., and Chen M.D. Effect of zinc on cellular levels of calmodulin and cyclic adenosine monophosphate in the adipocyte. Biol. Trace Elem. Res. 76 (2000) 229-234
    • (2000) Biol. Trace Elem. Res. , vol.76 , pp. 229-234
    • Lin, P.Y.1    Lin, W.H.2    Tsou, C.T.3    Song, Y.M.4    Chen, M.D.5
  • 30
    • 0036534025 scopus 로고    scopus 로고
    • Platelet calmodulin levels in adolescent idiopathic scoliosis: do the levels correlate with curve progression and severity?
    • Lowe T., Lawellin D., Smith D., Price C., Haher T., Merola A., and O'Brien M. Platelet calmodulin levels in adolescent idiopathic scoliosis: do the levels correlate with curve progression and severity?. Spine 27 (2002) 768-775
    • (2002) Spine , vol.27 , pp. 768-775
    • Lowe, T.1    Lawellin, D.2    Smith, D.3    Price, C.4    Haher, T.5    Merola, A.6    O'Brien, M.7
  • 31
    • 0030005659 scopus 로고    scopus 로고
    • Thapsigargin, a weak skin tumor promoter, alters the growth and differentiation of mouse keratinocytes in culture
    • Lowry D.T., Li L., and Hennings H. Thapsigargin, a weak skin tumor promoter, alters the growth and differentiation of mouse keratinocytes in culture. Carcinogenesis 17 (1996) 699-706
    • (1996) Carcinogenesis , vol.17 , pp. 699-706
    • Lowry, D.T.1    Li, L.2    Hennings, H.3
  • 32
    • 0027289307 scopus 로고
    • Essential roles for calcium and calmodulin in G2/M progression in Aspergillus nidulans
    • Lu K.P., Osmani S.A., Osmani A.H., and Means A.R. Essential roles for calcium and calmodulin in G2/M progression in Aspergillus nidulans. J. Cell Biol. 121 (1993) 621-630
    • (1993) J. Cell Biol. , vol.121 , pp. 621-630
    • Lu, K.P.1    Osmani, S.A.2    Osmani, A.H.3    Means, A.R.4
  • 35
    • 0032493743 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent protein kinase IV is cleaved by caspase-3 and calpain in SH-SY5Y human neuroblastoma cells undergoing apoptosis
    • McGinnis K.M., Whitton M.M., Gnegy M.E., and Wang K.K. Calcium/calmodulin-dependent protein kinase IV is cleaved by caspase-3 and calpain in SH-SY5Y human neuroblastoma cells undergoing apoptosis. J. Biol. Chem. 273 (1998) 19993-20000
    • (1998) J. Biol. Chem. , vol.273 , pp. 19993-20000
    • McGinnis, K.M.1    Whitton, M.M.2    Gnegy, M.E.3    Wang, K.K.4
  • 37
    • 0032537948 scopus 로고    scopus 로고
    • Alterations in human lymphocyte DNA caused by sulfur mustard can be mitigated by selective inhibitors of poly(ADP-ribose) polymerase
    • Meier H.L., and Millard C.B. Alterations in human lymphocyte DNA caused by sulfur mustard can be mitigated by selective inhibitors of poly(ADP-ribose) polymerase. Biochim. Biophys. Acta 1404 (1998) 367-376
    • (1998) Biochim. Biophys. Acta , vol.1404 , pp. 367-376
    • Meier, H.L.1    Millard, C.B.2
  • 38
    • 0021796108 scopus 로고
    • Ionic calcium reservoirs in mammalian epidermis: ultrastructural localization by ion-capture cytochemistry
    • Menon G.K., Grayson S., and Elias P.M. Ionic calcium reservoirs in mammalian epidermis: ultrastructural localization by ion-capture cytochemistry. J. Invest. Dermatol. 84 (1985) 508-512
    • (1985) J. Invest. Dermatol. , vol.84 , pp. 508-512
    • Menon, G.K.1    Grayson, S.2    Elias, P.M.3
  • 39
    • 0034036846 scopus 로고    scopus 로고
    • Differential regulation of calmodulin content and calmodulin messenger RNA levels by acute and repeated, intermittent amphetamine in dopaminergic terminal and midbrain areas
    • Michelhaugh S.K., and Gnegy M.E. Differential regulation of calmodulin content and calmodulin messenger RNA levels by acute and repeated, intermittent amphetamine in dopaminergic terminal and midbrain areas. Neuroscience 98 (2000) 275-285
    • (2000) Neuroscience , vol.98 , pp. 275-285
    • Michelhaugh, S.K.1    Gnegy, M.E.2
  • 40
    • 0024524043 scopus 로고
    • NAD+ levels and glucose uptake of cultured human epidermal cells exposed to sulfur mustard
    • Mol M.A., van de Ruit A.M., and Kluivers A.W. NAD+ levels and glucose uptake of cultured human epidermal cells exposed to sulfur mustard. Toxicol. Appl. Pharmacol. 98 (1989) 159-165
    • (1989) Toxicol. Appl. Pharmacol. , vol.98 , pp. 159-165
    • Mol, M.A.1    van de Ruit, A.M.2    Kluivers, A.W.3
  • 41
    • 0029670560 scopus 로고    scopus 로고
    • Calcium homeostasis and calcium signalling in sulphur mustard-exposed normal human epidermal keratinocytes
    • Elsevier pp. 85-93
    • Mol M.A.E., and Smith W. Calcium homeostasis and calcium signalling in sulphur mustard-exposed normal human epidermal keratinocytes. Chemico-Biological Interactions (1996), Elsevier pp. 85-93
    • (1996) Chemico-Biological Interactions
    • Mol, M.A.E.1    Smith, W.2
  • 46
    • 0025121034 scopus 로고
    • Effects of alkylating antineoplastics alone or in combination with 3-aminobenzamide on genotoxicity, antitumor activity, and NAD levels in human lymphocytes in vitro and on Ehrlich ascites tumor cells in vivo
    • Petrou C., Mourelatos D., Mioglou E., Dozi-Vassiliades J., and Catsoulacos P. Effects of alkylating antineoplastics alone or in combination with 3-aminobenzamide on genotoxicity, antitumor activity, and NAD levels in human lymphocytes in vitro and on Ehrlich ascites tumor cells in vivo. Teratog. Carcinog. Mutagen 10 (1990) 321-331
    • (1990) Teratog. Carcinog. Mutagen , vol.10 , pp. 321-331
    • Petrou, C.1    Mourelatos, D.2    Mioglou, E.3    Dozi-Vassiliades, J.4    Catsoulacos, P.5
  • 47
    • 0030623745 scopus 로고    scopus 로고
    • The effects of altered cellular calmodulin expression on the growth and viability of C6 glioblastoma cells
    • Prostko C.R., Zhang C., and Hait W.N. The effects of altered cellular calmodulin expression on the growth and viability of C6 glioblastoma cells. Oncol. Res. 9 (1997) 13-17
    • (1997) Oncol. Res. , vol.9 , pp. 13-17
    • Prostko, C.R.1    Zhang, C.2    Hait, W.N.3
  • 48
    • 0027380585 scopus 로고
    • Keratinocyte differentiation is associated with changes in the expression and regulation of phospholipase C isoenzymes
    • Punnonen K., Denning M., Lee E., Li L., Rhee S.G., and Yuspa S.H. Keratinocyte differentiation is associated with changes in the expression and regulation of phospholipase C isoenzymes. J. Invest. Dermatol. 101 (1993) 719-726
    • (1993) J. Invest. Dermatol. , vol.101 , pp. 719-726
    • Punnonen, K.1    Denning, M.2    Lee, E.3    Li, L.4    Rhee, S.G.5    Yuspa, S.H.6
  • 49
    • 0024989788 scopus 로고
    • Effects of changes in calmodulin levels on cell proliferation
    • Rasmussen C.D., and Means A.R. Effects of changes in calmodulin levels on cell proliferation. Environ. Health Perspect. 84 (1990) 31-34
    • (1990) Environ. Health Perspect. , vol.84 , pp. 31-34
    • Rasmussen, C.D.1    Means, A.R.2
  • 50
    • 0026530459 scopus 로고
    • Increased calmodulin affects cell morphology and mRNA levels of cytoskeletal protein genes
    • Rasmussen C.D., and Means A.R. Increased calmodulin affects cell morphology and mRNA levels of cytoskeletal protein genes. Cell Motil. Cytoskel. 21 (1992) 45-57
    • (1992) Cell Motil. Cytoskel. , vol.21 , pp. 45-57
    • Rasmussen, C.D.1    Means, A.R.2
  • 51
    • 0028913992 scopus 로고
    • Sulfur mustard-induced increase in intracellular free calcium level and arachidonic acid release from cell membrane
    • Ray R., Legere R.H., Majerus B.J., and Petrali J.P. Sulfur mustard-induced increase in intracellular free calcium level and arachidonic acid release from cell membrane. Toxicol. Appl. Pharmacol. 131 (1995) 44-52
    • (1995) Toxicol. Appl. Pharmacol. , vol.131 , pp. 44-52
    • Ray, R.1    Legere, R.H.2    Majerus, B.J.3    Petrali, J.P.4
  • 52
    • 33748754664 scopus 로고    scopus 로고
    • Ray, R., Majerus, B.J., Munavalli, G.S., Petrali, J.P., 1993. Sulfur mustard-induced increase in intracellular calcium: a mechanism of mustard toxicity. U.S. Army Medical Research Bioscience Review, pp. 267-276.
  • 53
    • 33748757001 scopus 로고    scopus 로고
    • Renshaw, B., 1946. Mechanisms in Production of Cutaneous Injuries by Sulfur and Nitrogen Mustards. Summary Technical Report of Division 9. In: Chemical Warfare Agents and Related Chemical Problems, Parts III-VI, National Defense Research Committee, U.S. Office of Scientific Research and Development, Washington, DC.
  • 54
    • 0031283280 scopus 로고    scopus 로고
    • 2+/calmodulin-binding peptides block phototransduction in limulus ventral photoreceptors: evidence for direct inhibition of phospholipase C
    • 2+/calmodulin-binding peptides block phototransduction in limulus ventral photoreceptors: evidence for direct inhibition of phospholipase C. Proc. Natl. Acad. Sci. U.S.A. 94 (1997) 14095-14099
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 14095-14099
    • Richard, E.A.1    Ghosh, S.2    Lowenstein, J.M.3    Lisman, J.E.4
  • 59
    • 0026110473 scopus 로고
    • A human epidermal differentiation-specific keratin gene is regulated by calcium but not negative modulators of differentiation in transgenic mouse keratinocytes
    • Rosenthal D.S., Steinert P.M., Chung S., Huff C.A., Johnson J., Yuspa S.H., and Roop D.R. A human epidermal differentiation-specific keratin gene is regulated by calcium but not negative modulators of differentiation in transgenic mouse keratinocytes. Cell Growth Differ. 2 (1991) 107-113
    • (1991) Cell Growth Differ. , vol.2 , pp. 107-113
    • Rosenthal, D.S.1    Steinert, P.M.2    Chung, S.3    Huff, C.A.4    Johnson, J.5    Yuspa, S.H.6    Roop, D.R.7
  • 63
    • 0032560514 scopus 로고    scopus 로고
    • Dissociation of cytokine-induced phosphorylation of Bad and activation of PKB/akt: involvement of MEK upstream of Bad phosphorylation
    • Scheid M.P., and Duronio V. Dissociation of cytokine-induced phosphorylation of Bad and activation of PKB/akt: involvement of MEK upstream of Bad phosphorylation. Proc. Natl. Acad. Sci. U.S.A. 95 (1998) 7439-7444
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 7439-7444
    • Scheid, M.P.1    Duronio, V.2
  • 64
    • 0023519975 scopus 로고
    • Molecular analysis of human and rat calmodulin complementary DNA clones. Evidence for additional active genes in these species
    • SenGupta B., Friedberg F., and Detera-Wadleigh S.D. Molecular analysis of human and rat calmodulin complementary DNA clones. Evidence for additional active genes in these species. J. Biol. Chem. 262 (1987) 16663-16670
    • (1987) J. Biol. Chem. , vol.262 , pp. 16663-16670
    • SenGupta, B.1    Friedberg, F.2    Detera-Wadleigh, S.D.3
  • 65
    • 0024368696 scopus 로고
    • Cyclosporin A inhibits activation-induced cell death in T-cell hybidomas and thymocytes
    • Shi Y., Sahai B.M., and Green D.R. Cyclosporin A inhibits activation-induced cell death in T-cell hybidomas and thymocytes. Nature 339 (1989) 625-626
    • (1989) Nature , vol.339 , pp. 625-626
    • Shi, Y.1    Sahai, B.M.2    Green, D.R.3
  • 66
    • 0030901628 scopus 로고    scopus 로고
    • Suppression of signalling through transcription factor NF-AT by interactions between calcineurin and Bcl-2
    • Shibasaki F., Kondo E., Akagi T., and McKeon F. Suppression of signalling through transcription factor NF-AT by interactions between calcineurin and Bcl-2. Nature 386 (1997) 728-731
    • (1997) Nature , vol.386 , pp. 728-731
    • Shibasaki, F.1    Kondo, E.2    Akagi, T.3    McKeon, F.4
  • 67
    • 0037025310 scopus 로고    scopus 로고
    • HPV-16 E6/7 immortalization sensitizes human keratinocytes to ultraviolet B by altering the pathway from caspase-8 to caspase-9-dependent apoptosis
    • Simbulan-Rosenthal C.M., Velena A., Veldman T., Schlegel R., and Rosenthal D.S. HPV-16 E6/7 immortalization sensitizes human keratinocytes to ultraviolet B by altering the pathway from caspase-8 to caspase-9-dependent apoptosis. J. Biol. Chem. 277 (2002) 24709-24716
    • (2002) J. Biol. Chem. , vol.277 , pp. 24709-24716
    • Simbulan-Rosenthal, C.M.1    Velena, A.2    Veldman, T.3    Schlegel, R.4    Rosenthal, D.S.5
  • 68
    • 0035831473 scopus 로고    scopus 로고
    • Executioner caspase-3, -6, and -7 perform distinct, non-redundant roles during the demolition phase of apoptosis
    • Slee E., Adrain C., and Martin S. Executioner caspase-3, -6, and -7 perform distinct, non-redundant roles during the demolition phase of apoptosis. J. Biol. Chem. 276 (2001) 7320-7326
    • (2001) J. Biol. Chem. , vol.276 , pp. 7320-7326
    • Slee, E.1    Adrain, C.2    Martin, S.3
  • 69
    • 0025175904 scopus 로고
    • The use of human epidermal keratinocytes in culture as a model for studying the biochemical mechanisms of sulfur mustard toxicity
    • Smith W.J., Gross C.L., Chan P., and Meier H.L. The use of human epidermal keratinocytes in culture as a model for studying the biochemical mechanisms of sulfur mustard toxicity. Cell Biol. Toxicol. 6 (1990) 285-291
    • (1990) Cell Biol. Toxicol. , vol.6 , pp. 285-291
    • Smith, W.J.1    Gross, C.L.2    Chan, P.3    Meier, H.L.4
  • 70
    • 84907039834 scopus 로고
    • Flow cytometric analysis of toxicity by vesicating agents in human cells in vitro
    • Smith W.J., Sanders K.M., Gales Y.A., and Gross C.L. Flow cytometric analysis of toxicity by vesicating agents in human cells in vitro. Toxicology (1991) 10
    • (1991) Toxicology , pp. 10
    • Smith, W.J.1    Sanders, K.M.2    Gales, Y.A.3    Gross, C.L.4
  • 73
    • 0020957390 scopus 로고
    • Specific epidermal protein markers are modulated during calcium-induced terminal differentiation
    • Stanley J.R., and Yuspa S.H. Specific epidermal protein markers are modulated during calcium-induced terminal differentiation. J. Cell Biol. 96 (1983) 1809-1814
    • (1983) J. Cell Biol. , vol.96 , pp. 1809-1814
    • Stanley, J.R.1    Yuspa, S.H.2
  • 75
    • 0027081161 scopus 로고
    • Mutations in yeast calmodulin cause defects in spindle pole body functions and nuclear integrity
    • Sun G.H., Hirata A., Ohya Y., and Anraku Y. Mutations in yeast calmodulin cause defects in spindle pole body functions and nuclear integrity. J. Cell Biol. 119 (1992) 1625-1639
    • (1992) J. Cell Biol. , vol.119 , pp. 1625-1639
    • Sun, G.H.1    Hirata, A.2    Ohya, Y.3    Anraku, Y.4
  • 76
    • 0033046402 scopus 로고    scopus 로고
    • Apoptosis and necrosis induced by sulfur mustard in Hela cells
    • Sun J., Wang Y.X., and Sun M.J. Apoptosis and necrosis induced by sulfur mustard in Hela cells. Chung Kuo Yao Li Hsueh Pao 20 (1999) 445-448
    • (1999) Chung Kuo Yao Li Hsueh Pao , vol.20 , pp. 445-448
    • Sun, J.1    Wang, Y.X.2    Sun, M.J.3
  • 77
    • 0028990125 scopus 로고
    • Yama/CPP32b, a mammalian homolog of CED-3, is a crmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase
    • Tewari M., Quan L.T., O'Rourke K., Desnoyers S., Zeng Z., Beidler D.R., Poirier G.G., Salvesen G.S., and Dixit V.M. Yama/CPP32b, a mammalian homolog of CED-3, is a crmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell 81 (1995) 801-809
    • (1995) Cell , vol.81 , pp. 801-809
    • Tewari, M.1    Quan, L.T.2    O'Rourke, K.3    Desnoyers, S.4    Zeng, Z.5    Beidler, D.R.6    Poirier, G.G.7    Salvesen, G.S.8    Dixit, V.M.9
  • 78
    • 0031805347 scopus 로고    scopus 로고
    • Characterization of the human CALM2 calmodulin gene and comparison of the transcriptional activity of CALM1, CALM2 and CALM3
    • Toutenhoofd S.L., Foletti D., Wicki R., Rhyner J.A., Garcia F., Tolon R., and Strehler E.E. Characterization of the human CALM2 calmodulin gene and comparison of the transcriptional activity of CALM1, CALM2 and CALM3. Cell Calcium 23 (1998) 323-338
    • (1998) Cell Calcium , vol.23 , pp. 323-338
    • Toutenhoofd, S.L.1    Foletti, D.2    Wicki, R.3    Rhyner, J.A.4    Garcia, F.5    Tolon, R.6    Strehler, E.E.7
  • 79
    • 0023139759 scopus 로고
    • Calmodulin levels in psoriasis and other skin disorders
    • van Erp P.E., and van de Kerkhof P.C. Calmodulin levels in psoriasis and other skin disorders. Arch. Dermatol. Res. 279 (1987) 151-153
    • (1987) Arch. Dermatol. Res. , vol.279 , pp. 151-153
    • van Erp, P.E.1    van de Kerkhof, P.C.2
  • 80
    • 0023986366 scopus 로고
    • Epidermal calmodulin levels and reference variables
    • van Erp P.E., and van de Kerkhof P.C. Epidermal calmodulin levels and reference variables. J. Invest. Dermatol. 90 (1988) 536-537
    • (1988) J. Invest. Dermatol. , vol.90 , pp. 536-537
    • van Erp, P.E.1    van de Kerkhof, P.C.2
  • 81
    • 33748749388 scopus 로고    scopus 로고
    • Dephosphorylation of pro-apoptotic protein Bad by calcineurin results in association with intracellular membranes
    • Wang H.G., Mckeon F., and Reed J.C. Dephosphorylation of pro-apoptotic protein Bad by calcineurin results in association with intracellular membranes. Program. Cell Death (1997)
    • (1997) Program. Cell Death
    • Wang, H.G.1    Mckeon, F.2    Reed, J.C.3
  • 82
    • 0029608883 scopus 로고
    • Functional elimination of calmodulin within the nucleus by targeted expression of an inhibitor peptide
    • Wang J., Campos B., Jamieson Jr. G.A., Kaetzel M.A., and Dedman J.R. Functional elimination of calmodulin within the nucleus by targeted expression of an inhibitor peptide. J. Biol. Chem. 270 (1995) 30245-30248
    • (1995) J. Biol. Chem. , vol.270 , pp. 30245-30248
    • Wang, J.1    Campos, B.2    Jamieson Jr., G.A.3    Kaetzel, M.A.4    Dedman, J.R.5
  • 83
    • 0029924463 scopus 로고    scopus 로고
    • Calcineurin A alpha (PPP3CA), calcineurin A beta (PPP3CB) and calcineurin B (PPP3R1) are located on human chromosomes 4, 10q21 → q22 and 2p16 → p15 respectively
    • Wang M.G., Yi H., Guerini D., Klee C.B., and McBride O.W. Calcineurin A alpha (PPP3CA), calcineurin A beta (PPP3CB) and calcineurin B (PPP3R1) are located on human chromosomes 4, 10q21 → q22 and 2p16 → p15 respectively. Cytogenet. Cell Genet. 72 (1996) 236-241
    • (1996) Cytogenet. Cell Genet. , vol.72 , pp. 236-241
    • Wang, M.G.1    Yi, H.2    Guerini, D.3    Klee, C.B.4    McBride, O.W.5
  • 84
    • 0021127994 scopus 로고
    • Isolation and nucleotide sequence of a cDNA encoding human calmodulin
    • Wawrzynczak E.J., and Perham R.N. Isolation and nucleotide sequence of a cDNA encoding human calmodulin. Biochem. Int. 9 (1984) 177-185
    • (1984) Biochem. Int. , vol.9 , pp. 177-185
    • Wawrzynczak, E.J.1    Perham, R.N.2
  • 86
    • 0032576996 scopus 로고    scopus 로고
    • Chemotherapeutic drug activation of the AP24 protease in apoptosis: requirement for caspase 3-like-proteases
    • Wright S.C., Schellenberger U., Wang H., Wang Y., and Kinder D.H. Chemotherapeutic drug activation of the AP24 protease in apoptosis: requirement for caspase 3-like-proteases. Biochem. Biophys. Res. Commun. 245 (1998) 797-803
    • (1998) Biochem. Biophys. Res. Commun. , vol.245 , pp. 797-803
    • Wright, S.C.1    Schellenberger, U.2    Wang, H.3    Wang, Y.4    Kinder, D.H.5
  • 87
    • 0032401880 scopus 로고    scopus 로고
    • Bcl-2-mediated resistance to apoptosis is associated with glutathione-induced inhibition of AP24 activation of nuclear DNA fragmentation
    • Wright S.C., Wang H., Wei Q.S., Kinder D.H., and Larrick J.W. Bcl-2-mediated resistance to apoptosis is associated with glutathione-induced inhibition of AP24 activation of nuclear DNA fragmentation. Cancer Res. 58 (1998) 5570-5576
    • (1998) Cancer Res. , vol.58 , pp. 5570-5576
    • Wright, S.C.1    Wang, H.2    Wei, Q.S.3    Kinder, D.H.4    Larrick, J.W.5
  • 88
    • 23844504243 scopus 로고    scopus 로고
    • Fas binding to calmodulin regulates apoptosis in osteoclasts
    • Wu X., Ahn E.Y., McKenna M.A., Yeo H., and McDonald J.M. Fas binding to calmodulin regulates apoptosis in osteoclasts. J. Biol. Chem. 280 (2005) 29964-29970
    • (2005) J. Biol. Chem. , vol.280 , pp. 29964-29970
    • Wu, X.1    Ahn, E.Y.2    McKenna, M.A.3    Yeo, H.4    McDonald, J.M.5
  • 89
    • 0028809209 scopus 로고
    • Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death
    • Yang E., Zha J., Jockel J., Boise L.H., Thompson C.B., and Korsmeyer S.J. Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death. Cell 80 (1995) 285-291
    • (1995) Cell , vol.80 , pp. 285-291
    • Yang, E.1    Zha, J.2    Jockel, J.3    Boise, L.H.4    Thompson, C.B.5    Korsmeyer, S.J.6
  • 90
    • 32844468634 scopus 로고    scopus 로고
    • Calcineurin inhibitors decrease DNA repair and apoptosis in human keratinocytes following ultraviolet B irradiation
    • Yarosh D.B., Pena A.V., Nay S.L., Canning M.T., and Brown D.A. Calcineurin inhibitors decrease DNA repair and apoptosis in human keratinocytes following ultraviolet B irradiation. J. Invest. Dermatol. 125 (2005) 1020-1025
    • (2005) J. Invest. Dermatol. , vol.125 , pp. 1020-1025
    • Yarosh, D.B.1    Pena, A.V.2    Nay, S.L.3    Canning, M.T.4    Brown, D.A.5
  • 91
    • 0030827971 scopus 로고    scopus 로고
    • BH3 domain of BAD is required for heterodimerization with BCL-XL and pro-apoptotic activity
    • Zha J., Harada H., Osipov K., Jockel J., Waksman G., and Korsmeyer S.J. BH3 domain of BAD is required for heterodimerization with BCL-XL and pro-apoptotic activity. J. Biol. Chem. 272 (1997) 24101-24104
    • (1997) J. Biol. Chem. , vol.272 , pp. 24101-24104
    • Zha, J.1    Harada, H.2    Osipov, K.3    Jockel, J.4    Waksman, G.5    Korsmeyer, S.J.6
  • 92
    • 0032128301 scopus 로고    scopus 로고
    • Inhibition of the anti-apoptotic PI(3)K/Akt/Bad pathway by stress
    • Zundel W., and Giaccia A. Inhibition of the anti-apoptotic PI(3)K/Akt/Bad pathway by stress. Genes Dev. 12 (1998) 1941-1946
    • (1998) Genes Dev. , vol.12 , pp. 1941-1946
    • Zundel, W.1    Giaccia, A.2


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