메뉴 건너뛰기




Volumn 122, Issue 2, 1997, Pages 279-285

Proteolysis of erythrocyte-type and brain-type ankyrins in rat heart after postischemic reperfusion

Author keywords

Ankyrin isoform; Calpain; Ischemia reperfusion; Membrane skeleton

Indexed keywords

ANKYRIN; CALPAIN; ISOPROTEIN; MEMBRANE PROTEIN; PROTEINASE;

EID: 0030870372     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021750     Document Type: Article
Times cited : (22)

References (37)
  • 1
    • 0025730273 scopus 로고
    • The spectrin skeleton: From red cells to brain
    • Bennett, V. and Lambert, S. (1991) The spectrin skeleton: From red cells to brain. J. Clin. Invest. 87, 1483-1489
    • (1991) J. Clin. Invest. , vol.87 , pp. 1483-1489
    • Bennett, V.1    Lambert, S.2
  • 2
    • 0026806912 scopus 로고
    • Ankyrins. Adapters between diverse plasma membrane proteins and the cytoplasm
    • Bennett, V. (1992) Ankyrins. Adapters between diverse plasma membrane proteins and the cytoplasm. J. Biol. Chem. 267, 8703-8706
    • (1992) J. Biol. Chem. , vol.267 , pp. 8703-8706
    • Bennett, V.1
  • 3
    • 0025314265 scopus 로고
    • Mapping the binding site of human erythrocyte ankyrin for the anion exchanger and spectrin
    • Davis, L.H. and Bennett, V. (1990) Mapping the binding site of human erythrocyte ankyrin for the anion exchanger and spectrin. J. Biol. Chem. 265, 10589-10596
    • (1990) J. Biol. Chem. , vol.265 , pp. 10589-10596
    • Davis, L.H.1    Bennett, V.2
  • 6
    • 0025827433 scopus 로고
    • Ischemia-induced loss of epithelial polarity: Potential role of the actin cytoskeleton
    • Molitoris, B.A. (1991) Ischemia-induced loss of epithelial polarity: potential role of the actin cytoskeleton. Am. J. Physiol. 260, F769-F777
    • (1991) Am. J. Physiol. , vol.260
    • Molitoris, B.A.1
  • 7
    • 0026713281 scopus 로고
    • Mapping the binding site on ankyrin for the voltage-dependent sodium channel from brain
    • Srinivasan, Y., Lewallen, M., and Angelides, K.J. (1992) Mapping the binding site on ankyrin for the voltage-dependent sodium channel from brain. J. Biol. Chem. 267, 7483-7489
    • (1992) J. Biol. Chem. , vol.267 , pp. 7483-7489
    • Srinivasan, Y.1    Lewallen, M.2    Angelides, K.J.3
  • 9
    • 0027469597 scopus 로고
    • Detergent solubility of the inositol trisphosphate receptor in rat brain membranes. Evidence for association of the receptor with ankyrin
    • Joseph, S.K. and Samanta, S. (1993) Detergent solubility of the inositol trisphosphate receptor in rat brain membranes. Evidence for association of the receptor with ankyrin. J. Biol. Chem. 268, 6477-6486
    • (1993) J. Biol. Chem. , vol.268 , pp. 6477-6486
    • Joseph, S.K.1    Samanta, S.2
  • 11
    • 0027999616 scopus 로고
    • Ankyrin binding activity shared by the neurofascin/L1/NrCAM family of nervous system cell adhesion molecules
    • Davis, J.Q. and Bennett, V. (1994) Ankyrin binding activity shared by the neurofascin/L1/NrCAM family of nervous system cell adhesion molecules. J. Biol. Chem. 269, 27163-27166
    • (1994) J. Biol. Chem. , vol.269 , pp. 27163-27166
    • Davis, J.Q.1    Bennett, V.2
  • 12
    • 0027535150 scopus 로고
    • Degradation of spectrin and ankyrin in the ischemic rat kidney
    • Doctor, R.B., Bennett, V., and Mandel, L.J. (1993) Degradation of spectrin and ankyrin in the ischemic rat kidney. Am. J. Physiol. 264, C1003-C1013
    • (1993) Am. J. Physiol. , vol.264
    • Doctor, R.B.1    Bennett, V.2    Mandel, L.J.3
  • 16
    • 0025231649 scopus 로고
    • An isoform of ankyrin is localized at nodes of Ranvier in myelinated axons of central and peripheral nerves
    • Kordeli, E., Davis, J., Trapp, B., and Bennett, V. (1990) An isoform of ankyrin is localized at nodes of Ranvier in myelinated axons of central and peripheral nerves. J. Cell Biol. 110, 1341-1352
    • (1990) J. Cell Biol. , vol.110 , pp. 1341-1352
    • Kordeli, E.1    Davis, J.2    Trapp, B.3    Bennett, V.4
  • 17
    • 0024515166 scopus 로고
    • Diversity in membrane binding sites of ankyrins
    • Davis, J., Davis, L., and Bennett, V. (1989) Diversity in membrane binding sites of ankyrins. J. Biol. Chem. 264, 6417-6426
    • (1989) J. Biol. Chem. , vol.264 , pp. 6417-6426
    • Davis, J.1    Davis, L.2    Bennett, V.3
  • 18
    • 0029113594 scopus 로고
    • Reperfusion of rat heart after brief ischemia induces proteolysis of calspectin (nonerythroid spectrin or fodrin) by calpain
    • Yoshida, K., Inui, M., Harada, K., Saido, T.C., Sorimachi, T., Ishihara, S., Kawashima, S., and Sobue, K. (1995) Reperfusion of rat heart after brief ischemia induces proteolysis of calspectin (nonerythroid spectrin or fodrin) by calpain. Circ. Res. 77, 603-610
    • (1995) Circ. Res. , vol.77 , pp. 603-610
    • Yoshida, K.1    Inui, M.2    Harada, K.3    Saido, T.C.4    Sorimachi, T.5    Ishihara, S.6    Kawashima, S.7    Sobue, K.8
  • 19
    • 0028804523 scopus 로고
    • Calpain is implicated in rat myocardial injury after ischemia or reperfusion
    • Yoshida, K., Sorimachi, Y., Fujiwara, M., and Hironaka, K. (1995) Calpain is implicated in rat myocardial injury after ischemia or reperfusion. Jpn. Circ. J. 59, 40-48
    • (1995) Jpn. Circ. J. , vol.59 , pp. 40-48
    • Yoshida, K.1    Sorimachi, Y.2    Fujiwara, M.3    Hironaka, K.4
  • 20
    • 0025840276 scopus 로고
    • A new 440-kD isoform is the major ankyrin in neonatal rat brain
    • Kunimoto, M., Otto, E., and Bennett, V. (1991) A new 440-kD isoform is the major ankyrin in neonatal rat brain. J. Cell Biol. 115, 1319-1331
    • (1991) J. Cell Biol. , vol.115 , pp. 1319-1331
    • Kunimoto, M.1    Otto, E.2    Bennett, V.3
  • 21
    • 0027313425 scopus 로고
    • Calpain activity alters in rat myocardial subfractions after ischemia or reperfusion
    • Yoshida, K., Yamasaki, Y., and Kawashima, S. (1993) Calpain activity alters in rat myocardial subfractions after ischemia or reperfusion. Biochim. Biophys. Acta 1182, 215-220
    • (1993) Biochim. Biophys. Acta , vol.1182 , pp. 215-220
    • Yoshida, K.1    Yamasaki, Y.2    Kawashima, S.3
  • 23
    • 0030922032 scopus 로고    scopus 로고
    • Mitogen activated protein kinase (MAPK) translocates to the nucleus during ischemia and is activated during reperfusion in rat heart
    • in press
    • Mizukami, Y. and Yoshida, K. (1997) Mitogen activated protein kinase (MAPK) translocates to the nucleus during ischemia and is activated during reperfusion in rat heart. Biochem. J. in press
    • (1997) Biochem. J.
    • Mizukami, Y.1    Yoshida, K.2
  • 26
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets; procedure and some applications
    • Towbin, H., Staehelin, T., and Gordon, J. (1970) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets; procedure and some applications. Proc. Natl. Acad. Sci. USA 76, 4350-4354
    • (1970) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 27
    • 0019423594 scopus 로고
    • The use of avidin-biotin-peroxidase complex (ABC) in immunoperoxidase techniques: A comparison between ABC and unlabelled antibody (PAP) procedures
    • Hsu, S.M., Raine, L., and Fanger, H. (1981) The use of avidin-biotin-peroxidase complex (ABC) in immunoperoxidase techniques: a comparison between ABC and unlabelled antibody (PAP) procedures. J. Histochem. Cytochem. 29, 577-580
    • (1981) J. Histochem. Cytochem. , vol.29 , pp. 577-580
    • Hsu, S.M.1    Raine, L.2    Fanger, H.3
  • 28
    • 0019309226 scopus 로고
    • Human erythrocyte ankyrin. Purification and properties
    • Bennett, V. and Stenbuck, P.J. (1980) Human erythrocyte ankyrin. Purification and properties. J. Biol. Chem. 255, 2540-2548
    • (1980) J. Biol. Chem. , vol.255 , pp. 2540-2548
    • Bennett, V.1    Stenbuck, P.J.2
  • 29
    • 0029877917 scopus 로고    scopus 로고
    • Differential inhibition of calpain and proteasome activities by peptidyl aldehydes of di-leucine and tri-leucine
    • Tsubuki, S., Saito, Y., Tomioka, M., Ito, H., and Kawashima, S. (1996) Differential inhibition of calpain and proteasome activities by peptidyl aldehydes of di-leucine and tri-leucine. J. Biochem. 119, 572-576
    • (1996) J. Biochem. , vol.119 , pp. 572-576
    • Tsubuki, S.1    Saito, Y.2    Tomioka, M.3    Ito, H.4    Kawashima, S.5
  • 30
    • 0021253387 scopus 로고
    • Globin (ankyrin) in striated muscle: Identification of the potential membrane receptor for erythroid spectrin in muscle cells
    • Nelson, W.J. and Lazarides, E. (1984) Globin (ankyrin) in striated muscle: Identification of the potential membrane receptor for erythroid spectrin in muscle cells. Proc. Natl. Acad. Sci. USA 81, 3292-3296
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 3292-3296
    • Nelson, W.J.1    Lazarides, E.2
  • 31
    • 0023196746 scopus 로고
    • Regulatory domains of erythrocyte ankyrin
    • Hall, T.G. and Bennett, V. (1987) Regulatory domains of erythrocyte ankyrin. J. Biol. Chem. 262, 10537-10545
    • (1987) J. Biol. Chem. , vol.262 , pp. 10537-10545
    • Hall, T.G.1    Bennett, V.2
  • 34
    • 0027532185 scopus 로고
    • Ankyrin-binding proteins related to nervous system cell adhesion molecules: Candidates to provide transmembrane and intercellular connections in adult brain
    • Davis, J.Q., McLaughlin, T., and Bennett, V. (1993) Ankyrin-binding proteins related to nervous system cell adhesion molecules: Candidates to provide transmembrane and intercellular connections in adult brain. J. Cell Biol. 121, 121-133
    • (1993) J. Cell Biol. , vol.121 , pp. 121-133
    • Davis, J.Q.1    McLaughlin, T.2    Bennett, V.3
  • 35
    • 0023681280 scopus 로고
    • Identification and partial purification of ABGP205, an integral membrane glycoprotein from brain that binds ankyrin
    • Treharne, K.J., Rayner, D., and Baines, A.J. (1988) Identification and partial purification of ABGP205, an integral membrane glycoprotein from brain that binds ankyrin. Biochem. J. 253, 345-350
    • (1988) Biochem. J. , vol.253 , pp. 345-350
    • Treharne, K.J.1    Rayner, D.2    Baines, A.J.3
  • 36
    • 0026612705 scopus 로고
    • 2+ exchanger protein in mammalian cardiac myocytes: An immunofluorescence and immunocolloidal gold-labeling study
    • 2+ exchanger protein in mammalian cardiac myocytes: An immunofluorescence and immunocolloidal gold-labeling study. J. Cell Biol. 117, 337-345
    • (1992) J. Cell Biol. , vol.117 , pp. 337-345
    • Frank, J.S.1    Mottino, G.2    Reid, D.3    Molday, R.S.4    Philipson, K.D.5
  • 37
    • 0023644484 scopus 로고
    • Purification of the ryanodine receptor and identity with feet structures of junctional terminal cisternae of sarcoplasmic reticulum from fast skeletal muscle
    • Inui, M., Saito, A., and Fleischer, S. (1987) Purification of the ryanodine receptor and identity with feet structures of junctional terminal cisternae of sarcoplasmic reticulum from fast skeletal muscle. J. Biol. Chem. 262, 1740-1747
    • (1987) J. Biol. Chem. , vol.262 , pp. 1740-1747
    • Inui, M.1    Saito, A.2    Fleischer, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.