메뉴 건너뛰기




Volumn 5, Issue 12, 1998, Pages 1028-1033

Cleavage of the calpain inhibitor, calpastatin, during apoptosis

Author keywords

Apoptosis calpastatin; Calpain; Caspase

Indexed keywords

CALPAIN; CALPASTATIN; CASPASE 3; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; STAUROSPORINE; TUMOR NECROSIS FACTOR;

EID: 0041018181     PISSN: 13509047     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.cdd.4400424     Document Type: Article
Times cited : (189)

References (19)
  • 2
    • 0030931876 scopus 로고    scopus 로고
    • Caspases: The executioners of apoptosis
    • Cohen GM (1997) Caspases: the executioners of apoptosis. Biochem. J. 326: 1-16
    • (1997) Biochem. J. , vol.326 , pp. 1-16
    • Cohen, G.M.1
  • 3
    • 0022617676 scopus 로고
    • Calcium-dependent affinity purification of transglutaminase from rat liver cytosol
    • Croall DE and DeMartino GN (1986) Calcium-dependent affinity purification of transglutaminase from rat liver cytosol. Cell Calcium 7: 29-39
    • (1986) Cell Calcium , vol.7 , pp. 29-39
    • Croall, D.E.1    DeMartino, G.N.2
  • 4
    • 0027940509 scopus 로고
    • Domain structure of calpain: Mapping the binding site for calpastatin
    • Croall DE and McGrody KS (1994) Domain structure of calpain: mapping the binding site for calpastatin. Biochemistry 33: 13223-13230
    • (1994) Biochemistry , vol.33 , pp. 13223-13230
    • Croall, D.E.1    McGrody, K.S.2
  • 5
    • 0029959632 scopus 로고    scopus 로고
    • Specificcleavage of alpha-fodrin during Fas- And tumor necrosis factor-induced apoptosis is mediated by an interleukin -1β-converting enzyme/Ced-3 protease distinct from the poly(ADP-ribose) polymerase protease
    • Cryns VL, Bergeron L, Zhu H, Li H and Yuan J (1996) Specificcleavage of alpha-fodrin during Fas- and tumor necrosis factor-induced apoptosis is mediated by an interleukin -1β-converting enzyme/Ced-3 protease distinct from the poly(ADP-ribose) polymerase protease. J. Biol. Chem. 271: 31277-31282
    • (1996) J. Biol. Chem. , vol.271 , pp. 31277-31282
    • Cryns, V.L.1    Bergeron, L.2    Zhu, H.3    Li, H.4    Yuan, J.5
  • 6
    • 0029782494 scopus 로고    scopus 로고
    • Cathepsin D protease mediates programmed cell death induced by interferon-gamma, Fas/APO-1 and TNF-alpha
    • Deiss LP, Galinka H, Berissi H, Cohen O and Kimchi A (1996) Cathepsin D protease mediates programmed cell death induced by interferon-gamma, Fas/APO-1 and TNF-alpha. EMBOJ. 15: 3861-3870
    • (1996) EMBOJ. , vol.15 , pp. 3861-3870
    • Deiss, L.P.1    Galinka, H.2    Berissi, H.3    Cohen, O.4    Kimchi, A.5
  • 7
    • 0021257138 scopus 로고
    • Purification and characterization of a protein inhibitor of calcium-dependent protease from rat liver
    • DeMartino GN and Croall DE (1984) Purification and characterization of a protein inhibitor of calcium-dependent protease from rat liver. Arch. Biochem. Biophys. 232: 713-720
    • (1984) Arch. Biochem. Biophys. , vol.232 , pp. 713-720
    • DeMartino, G.N.1    Croall, D.E.2
  • 8
    • 0023835174 scopus 로고
    • All four repeating domains of the endogenous inhibitor for calcium-dependent protease independently retain inhibitory activity. Expression of the cDNA fragments in Escherichia coli
    • Emori Y, Kawasaki H, Imajoh S, Minami Y and Suzuki K (1988) All four repeating domains of the endogenous inhibitor for calcium-dependent protease independently retain inhibitory activity. Expression of the cDNA fragments in Escherichia coli. J. Biol. Chem. 263: 2364-2370
    • (1988) J. Biol. Chem. , vol.263 , pp. 2364-2370
    • Emori, Y.1    Kawasaki, H.2    Imajoh, S.3    Minami, Y.4    Suzuki, K.5
  • 10
    • 0029995766 scopus 로고    scopus 로고
    • A license to kill
    • Fraser A and Evan G (1996) A license to kill. Cell 85: 781-784
    • (1996) Cell , vol.85 , pp. 781-784
    • Fraser, A.1    Evan, G.2
  • 11
    • 0017716047 scopus 로고
    • Studies on a cyclic nucleotide-independent protein kinase and its proenzyme in mammalian tissues. II. Proenzyme and its activation by calcium-dependent protease from rat brain
    • Inoue K, Kishimoto A, Takai Y and Nishizuka Y (1977) Studies on a cyclic nucleotide-independent protein kinase and its proenzyme in mammalian tissues. II. Proenzyme and its activation by calcium-dependent protease from rat brain. J. Biol. Chem. 252: 7610-7616
    • (1977) J. Biol. Chem. , vol.252 , pp. 7610-7616
    • Inoue, K.1    Kishimoto, A.2    Takai, Y.3    Nishizuka, Y.4
  • 13
    • 0026644784 scopus 로고
    • Molecular diversity in amino-terminal domains of human calpastatin by exon skipping
    • Lee WJ, Ma H, Takano E, Yang HQ, Hatanaka M and Maki M (1992) Molecular diversity in amino-terminal domains of human calpastatin by exon skipping J. Biol. Chem. 267: 8437-8442
    • (1992) J. Biol. Chem. , vol.267 , pp. 8437-8442
    • Lee, W.J.1    Ma, H.2    Takano, E.3    Yang, H.Q.4    Hatanaka, M.5    Maki, M.6
  • 14
    • 0002397847 scopus 로고
    • Structure-function relationship of calpastatins
    • Mellgren RL and Murachi T, eds. (Boca Raton: CRC Press)
    • Maki M, Hatanaka M, Takano E and Murachi T(1990) Structure-function relationship of calpastatins. In Intracellular calcium-dependent proteolysis. Mellgren RL and Murachi T, eds. (Boca Raton: CRC Press) pp. 37-54
    • (1990) Intracellular Calcium-dependent Proteolysis , pp. 37-54
    • Maki, M.1    Hatanaka, M.2    Takano, E.3    Murachi, T.4
  • 15
    • 0023659729 scopus 로고
    • All four internally repetitive domains of pig calpastatin possess inhibitory activities against calpains I and II
    • Maki M, Takano E, Mori H,Sato A, Murachi T and Hatanaka M (1987) All four internally repetitive domains of pig calpastatin possess inhibitory activities against calpains I and II. FEBS Lett. 223: 174-180
    • (1987) FEBS Lett. , vol.223 , pp. 174-180
    • Maki, M.1    Takano, E.2    Mori, H.3    Sato, A.4    Murachi, T.5    Hatanaka, M.6
  • 17
    • 0029199452 scopus 로고
    • The end of the (cell) line: Methods for the study of apoptosis in vitro
    • Schwartz LM and Osborne BA, eds. (San Diego: Academic Press)
    • McGahon AJ, Martin SJ, Bissonnette RP, Mahboubi A, Shi Y, Mogil RJ, Nishioka WK and Green DR (1995) The end of the (cell) line: Methods for the study of apoptosis in vitro. In Cell Death. Schwartz LM and Osborne BA, eds. (San Diego: Academic Press) pp. 153-185
    • (1995) Cell Death , pp. 153-185
    • McGahon, A.J.1    Martin, S.J.2    Bissonnette, R.P.3    Mahboubi, A.4    Shi, Y.5    Mogil, R.J.6    Nishioka, W.K.7    Green, D.R.8
  • 18
    • 0030726132 scopus 로고    scopus 로고
    • Specificities of cell permeant peptidyl inhibitors for the proteinase activities of mu-calpain and the 20 S proteasome
    • Mellgren RL(1997) Specificities of cell permeant peptidyl inhibitors for the proteinase activities of mu-calpain and the 20 S proteasome. J. Biol. Chem. 272: 29899-29903
    • (1997) J. Biol. Chem. , vol.272 , pp. 29899-29903
    • Mellgren, R.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.