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Volumn 86, Issue 1-2, 1997, Pages 77-85

Proteolysis of ankyrin and Na+/K+-ATPase in postmortem rat brain: Is calpain involved?

Author keywords

Ankyrin; Calpain; Cytoskeleton; Na+ K+ ATPase; Postmortem

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); ANKYRIN; ANTIBODY; CALCIUM; CALPAIN; MEMBRANE PROTEIN;

EID: 0030941585     PISSN: 03790738     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0379-0738(97)02120-8     Document Type: Article
Times cited : (8)

References (20)
  • 1
    • 0025730273 scopus 로고
    • The spectrin skeleton: From red cells to brain
    • V. Bennett and S. Lambert, The spectrin skeleton: from red cells to brain. J. Clin. Invest., 87 (1991) 1483-1489.
    • (1991) J. Clin. Invest. , vol.87 , pp. 1483-1489
    • Bennett, V.1    Lambert, S.2
  • 2
    • 0026806912 scopus 로고
    • Ankyrins. Adaptors between diverse plasma membrane proteins and the cytoplasm
    • V. Bennett, Ankyrins. Adaptors between diverse plasma membrane proteins and the cytoplasm. J. Biol. Chem., 267 (1992) 8703-8706.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8703-8706
    • Bennett, V.1
  • 4
    • 0001848892 scopus 로고
    • Calpain substrate specificity
    • In R. Mellegren and T. Murachi (eds.), CRC Press, Inc., Boca Raton, FL
    • K. Takahashi, Calpain substrate specificity. In R. Mellegren and T. Murachi (eds.), Intracellular Calcium-Dependent Proteolysis, CRC Press, Inc., Boca Raton, FL, 1990, pp. 55-74.
    • (1990) Intracellular Calcium-Dependent Proteolysis , pp. 55-74
    • Takahashi, K.1
  • 5
    • 0025831476 scopus 로고
    • Calcium-activated neutral protease (Calpain) system: Structure, function and regulation
    • D.E. Croall and G.N. Demartino, Calcium-activated neutral protease (Calpain) system: structure, function and regulation. Physiol. Rev., 71 (1991) 813-847.
    • (1991) Physiol. Rev. , vol.71 , pp. 813-847
    • Croall, D.E.1    Demartino, G.N.2
  • 6
    • 0027535150 scopus 로고
    • Degradation of spectrin and ankyrin in the ischemic rat kidney
    • R.B. Doctor, V. Bennett 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, R.B.1    Bennett, V.2    Mandel, L.J.3
  • 7
    • 0024347477 scopus 로고
    • Ischemia triggers NMDA receptor-linked cytoskeletal proteolysis in hippocampus
    • P. Seubert, K. Lee and G. Lynch, Ischemia triggers NMDA receptor-linked cytoskeletal proteolysis in hippocampus. Brain Res., 492 (1989) 366-370.
    • (1989) Brain Res. , vol.492 , pp. 366-370
    • Seubert, P.1    Lee, K.2    Lynch, G.3
  • 8
    • 0029113594 scopus 로고
    • Kawashima and K. Sobue, Reperfusion of rat heart after brief ischemia induces calspectin (fodrin) proteolysis by calpain
    • K. Yoshida, M. Inui, K. Harada, T. Saido, Y. Sorimachi, T. Ishihara, S. Kawashima and K. Sobue, Reperfusion of rat heart after brief ischemia induces calspectin (fodrin) proteolysis by calpain. Circ. Res., 77 (1995) 603-610.
    • (1995) Circ. Res. , vol.77 , pp. 603-610
    • Yoshida, K.1    Inui, M.2    Harada, K.3    Saido, T.4    Sorimachi, Y.5    Ishihara, T.6
  • 9
    • 0030586896 scopus 로고    scopus 로고
    • Involvement of calpain in postmortem proteolysis in the rat brain
    • Y. Sorimachi, K. Harada and K. Yoshida, Involvement of calpain in postmortem proteolysis in the rat brain. Forensic Sci. Int., 81 (1996) 165-174.
    • (1996) Forensic Sci. Int. , vol.81 , pp. 165-174
    • Sorimachi, Y.1    Harada, K.2    Yoshida, K.3
  • 10
    • 0024418455 scopus 로고
    • 2+ release in smooth muscle: Physiological role of inositol 1,4,5-triphosphate in pharmacomechanical coupling
    • 2+ release in smooth muscle: physiological role of inositol 1,4,5-triphosphate in pharmacomechanical coupling. J. Biol. Chem., 264 (1989) 17997-18004.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17997-18004
    • Kobayashi, S.1    Kitazawa, T.2    Somlyo, A.V.3    Somlyo, A.P.4
  • 11
    • 73049155988 scopus 로고
    • The isolation of nerve endings from brain: An electron-microscopic study of cell fragments derived by homogenization and centrifugation
    • E.G. Gray and V.P. Whittaker, The isolation of nerve endings from brain: an electron-microscopic study of cell fragments derived by homogenization and centrifugation. J. Anat., 96 (1962) 79-88.
    • (1962) J. Anat. , vol.96 , pp. 79-88
    • Gray, E.G.1    Whittaker, V.P.2
  • 13
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • H. Towbin, T. Staehelin and J. Gordon, Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc. Natl. Acad. Sci. USA, 76 (1979) 4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 14
    • 0027313425 scopus 로고
    • Calpain activity alters in rat myocardial subfractions after ischemia or reperfusion
    • K. Yoshida, Y. Yamasaki and S. Kawashima, Calpain activity alters in rat myocardial subfractions after ischemia or reperfusion. Biochim. Biophys. Acta., 1182 (1993) 215-220.
    • (1993) Biochim. Biophys. Acta. , vol.1182 , pp. 215-220
    • Yoshida, K.1    Yamasaki, Y.2    Kawashima, S.3
  • 15
    • 0028804523 scopus 로고
    • Calpain is implicated in rat myocardial injury after ischemia or reperfusion
    • K. Yoshida, Y. Sorimachi, M. Fujiwara and K. Hironaka, Calpain is implicated in rat myocardial injury after ischemia or reperfusion. Jpn. Circ. J., 59 (1995) 40-48.
    • (1995) Jpn. Circ. J. , vol.59 , pp. 40-48
    • Yoshida, K.1    Sorimachi, Y.2    Fujiwara, M.3    Hironaka, K.4
  • 16
    • 0022746352 scopus 로고
    • Isolation and characterization of monoclonal antibodies against calcium-activated neutral protease with low calcium sensitivity
    • Y. Kasai, M. Inomata, M. Hayashi, K. Imahori and S. Kawashima, Isolation and characterization of monoclonal antibodies against calcium-activated neutral protease with low calcium sensitivity. J. Biochem., 100 (1986) 183-190.
    • (1986) J. Biochem. , vol.100 , pp. 183-190
    • Kasai, Y.1    Inomata, M.2    Hayashi, M.3    Imahori, K.4    Kawashima, S.5
  • 17
    • 0003768786 scopus 로고
    • Activities of proteinase inhibitors of microbial origin
    • In: A.J. Barrett (ed.), Elsevier, Amsterdam
    • H. Umezawa and T. Aoyagi, Activities of proteinase inhibitors of microbial origin. In: A.J. Barrett (ed.), Proteinases in Mammalian Cells and Tissues, Elsevier, Amsterdam, 1977, pp. 637-662.
    • (1977) Proteinases in Mammalian Cells and Tissues , pp. 637-662
    • Umezawa, H.1    Aoyagi, T.2
  • 18
    • 0028293250 scopus 로고
    • Comparison of the effect of calpain inhibitors on two extralysosomal proteinases: The multicatalytic proteinase complex and m-calpain
    • M.E. Figueiredo-Pereira, N. Banik and S. Wilk, Comparison of the effect of calpain inhibitors on two extralysosomal proteinases: the multicatalytic proteinase complex and m-calpain. J. Neurochem., 62 (1994) 1989-1994.
    • (1994) J. Neurochem. , vol.62 , pp. 1989-1994
    • Figueiredo-Pereira, M.E.1    Banik, N.2    Wilk, S.3
  • 19
    • 0026454458 scopus 로고
    • Positive regulation of μ-calpain action by polyphosphoinositides
    • T.C. Saido, M. Shibata, T. Takenawa, H. Murofushi and K. Suzuki, Positive regulation of μ-calpain action by polyphosphoinositides. J. Biol. Chem., 267 (1992) 24585-24590.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24585-24590
    • Saido, T.C.1    Shibata, M.2    Takenawa, T.3    Murofushi, H.4    Suzuki, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.