메뉴 건너뛰기




Volumn 389, Issue , 1996, Pages 177-185

Participation of cathepsins B, H, and L in perikaryal condensation of CA1 pyramidal neurons undergoing apoptosis after brief ischemia

Author keywords

[No Author keywords available]

Indexed keywords

CATHEPSIN; CATHEPSIN B; CATHEPSIN H; CATHEPSIN L; CYSTEINE PROTEINASE; ENZYME PRECURSOR; PROTEINASE; AMYLOID BETA PROTEIN;

EID: 0030329963     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4613-0335-0_22     Document Type: Article
Times cited : (25)

References (31)
  • 1
    • 0022742338 scopus 로고
    • Purification and tissue distribution of rat cathepsin L
    • Bando, Y., Kominami, E., and Katunuma, N., 1986, Purification and tissue distribution of rat cathepsin L, J. Biochem. 100: 35-42.
    • (1986) J. Biochem. , vol.100 , pp. 35-42
    • Bando, Y.1    Kominami, E.2    Katunuma, N.3
  • 2
    • 0020076028 scopus 로고
    • Double immunocytochemical labelling applying the protein A-gold technique
    • Bendayan, M., 1982, Double immunocytochemical labelling applying the protein A-gold technique, J. Histochem. Cytochem. 30: 81-85.
    • (1982) J. Histochem. Cytochem. , vol.30 , pp. 81-85
    • Bendayan, M.1
  • 4
    • 0024412132 scopus 로고
    • Cathepsin B immunoreactive neurons in rat brain. A combined light and electron microscopic study
    • Bernstein, H.-G., Sormunen, R., Järvinen, M., Kloss, P., Kirschke, H., and Rinne, A., 1989, Cathepsin B immunoreactive neurons in rat brain. A combined light and electron microscopic study, J. Hirnforsch. 30: 313-317.
    • (1989) J. Hirnforsch. , vol.30 , pp. 313-317
    • Bernstein, H.-G.1    Sormunen, R.2    Järvinen, M.3    Kloss, P.4    Kirschke, H.5    Rinne, A.6
  • 5
    • 0025271381 scopus 로고
    • Selective vulnerability in the gerbil hippocampus: Morphological changes after 5-min ischemia and long survival times
    • Bonnekoh, P., Barbier, A., Oschlies, U., and Hossmann, K.-A., 1990, Selective vulnerability in the gerbil hippocampus: Morphological changes after 5-min ischemia and long survival times, Acta Neuropathol. (Berl.) 80: 18-25.
    • (1990) Acta Neuropathol. (Berl.) , vol.80 , pp. 18-25
    • Bonnekoh, P.1    Barbier, A.2    Oschlies, U.3    Hossmann, K.-A.4
  • 6
    • 0025195944 scopus 로고
    • Enzymatically active lysosomal proteases are associated with amyloid deposits in Alzheimer brain
    • Cataldo, A.M. and Nixon, R.A., 1990. Enzymatically active lysosomal proteases are associated with amyloid deposits in Alzheimer brain. Proc. Natl. Acad. Sci. USA 87: 3861-3865.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3861-3865
    • Cataldo, A.M.1    Nixon, R.A.2
  • 7
    • 0026327404 scopus 로고
    • Lysosomal hydrolases of different classes are abnormally distributed in brains of patients with Alzheimer disease
    • Cataldo, A.M., Paskevich, P.A., Kominami, E. and Nixon R.A., 1991, Lysosomal hydrolases of different classes are abnormally distributed in brains of patients with Alzheimer disease, Proc. Natl. Acad. Sci. USA 88: 10998-11002.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10998-11002
    • Cataldo, A.M.1    Paskevich, P.A.2    Kominami, E.3    Nixon, R.A.4
  • 8
    • 0025355591 scopus 로고
    • Lysosomal proteinase antigens are prominently localized within senile plaques of Alzheimer's disease: Evidence for a neuronal origin
    • Cataldo, A.M., Thayer C.Y., Bird, E.D., Wheelock, T.R. and Nixon, R.A., 1990, Lysosomal proteinase antigens are prominently localized within senile plaques of Alzheimer's disease: evidence for a neuronal origin, Brain Res. 513: 181-192.
    • (1990) Brain Res. , vol.513 , pp. 181-192
    • Cataldo, A.M.1    Thayer, C.Y.2    Bird, E.D.3    Wheelock, T.R.4    Nixon, R.A.5
  • 9
    • 0025283961 scopus 로고
    • Developmental cell death: Morphological diversity and multiple mechanisms
    • Clarke, P. G. H., 1990, Developmental cell death: morphological diversity and multiple mechanisms. Anat. Embryol. 181: 195-213.
    • (1990) Anat. Embryol. , vol.181 , pp. 195-213
    • Clarke, P.G.H.1
  • 10
    • 0027485950 scopus 로고
    • Temporal analysis of events associated with programmed cell death (apoptosis) of sympathetic neurons deprived of nerve growth factor
    • Deckwerth, T. L., and Johnson, E. M. Jr., 1993, Temporal analysis of events associated with programmed cell death (apoptosis) of sympathetic neurons deprived of nerve growth factor, J. Cell Biol. 123: 1207-1222.
    • (1993) J. Cell Biol. , vol.123 , pp. 1207-1222
    • Deckwerth, T.L.1    Johnson Jr., E.M.2
  • 11
    • 0026648674 scopus 로고
    • Identification of programmed cell death in situ via specific labeling of nuclear DNA fragmentation
    • Gavrieli, Y., Sherman, Y., and Ben-Sasson, A. J., 1992, Identification of programmed cell death in situ via specific labeling of nuclear DNA fragmentation, J. Cell Biol. 119: 493-501.
    • (1992) J. Cell Biol. , vol.119 , pp. 493-501
    • Gavrieli, Y.1    Sherman, Y.2    Ben-Sasson, A.J.3
  • 12
    • 0022379602 scopus 로고
    • The immunochemical detection and quantitation of intracellular ubiquitin-protein conjugates
    • Haas, A. and Bright, P.M., 1985, The immunochemical detection and quantitation of intracellular ubiquitin-protein conjugates, J. Biol. Chem. 260: 12464-12473.
    • (1985) J. Biol. Chem. , vol.260 , pp. 12464-12473
    • Haas, A.1    Bright, P.M.2
  • 14
    • 0016743902 scopus 로고
    • Experimental cerebral ischemia in Mongolian gerbils. 1. Light microscopic observations
    • Ito, U., Spatz, M., Walker, J. T., and Klatzo, I., 1975, Experimental cerebral ischemia in Mongolian gerbils. 1. Light microscopic observations, Acta Neuropathol. (Berl.) 32: 209-223.
    • (1975) Acta Neuropathol. (Berl.) , vol.32 , pp. 209-223
    • Ito, U.1    Spatz, M.2    Walker, J.T.3    Klatzo, I.4
  • 15
    • 0020688213 scopus 로고
    • Structures and functions of lysosomal thiol proteinases and their endogenous inhibitors
    • Katunuma, N., and Kominami, E., 1983, Structures and functions of lysosomal thiol proteinases and their endogenous inhibitors. Curr. Top. Cell Regul. 22: 71-101.
    • (1983) Curr. Top. Cell Regul. , vol.22 , pp. 71-101
    • Katunuma, N.1    Kominami, E.2
  • 17
    • 0020051129 scopus 로고
    • Delayed neuronal death in the gerbil hippocampus following ischemia
    • Kirino, T., 1982, Delayed neuronal death in the gerbil hippocampus following ischemia. Brain Res. 239: 57-69.
    • (1982) Brain Res. , vol.239 , pp. 57-69
    • Kirino, T.1
  • 18
    • 0021368367 scopus 로고
    • Selective vulnerability in the gerbil hippocampus following transient ischemia
    • Kirino, T., and Sano, K., 1984a. Selective vulnerability in the gerbil hippocampus following transient ischemia, Acta Neuropathol. (Berl.) 62: 201-208.
    • (1984) Acta Neuropathol. (Berl.) , vol.62 , pp. 201-208
    • Kirino, T.1    Sano, K.2
  • 19
    • 0021358671 scopus 로고
    • Fine structural nature of delayed neuronal death following ischemia in the gerbil hippocampus
    • Kirino, T., and Sano, K., 1984b, Fine structural nature of delayed neuronal death following ischemia in the gerbil hippocampus, Acta Neuropathol. (Berl.) 62: 209-218.
    • (1984) Acta Neuropathol. (Berl.) , vol.62 , pp. 209-218
    • Kirino, T.1    Sano, K.2
  • 20
    • 0018685250 scopus 로고
    • Lysosomal cysteine proteinases
    • Protein degradation in health and disease (Evered D, Whelan J eds), Amsterdam: Excerpta Medica
    • Kirschke, H., Langer, J., Riemann, S., Wiederanders, B., Ansorge, S., and Bohley, P., 1980, Lysosomal cysteine proteinases. In Protein degradation in health and disease (Evered D, Whelan J eds), Ciba Foundation Symposium 75, pp 15-35. Amsterdam: Excerpta Medica.
    • (1980) Ciba Foundation Symposium , vol.75 , pp. 15-35
    • Kirschke, H.1    Langer, J.2    Riemann, S.3    Wiederanders, B.4    Ansorge, S.5    Bohley, P.6
  • 21
    • 0021684708 scopus 로고
    • Different tissue distributions of two types of thiol proteinase inhibitors from rat liver and epidermis
    • Kominami, E., Bando, Y., Wakamatsu, N., and Katunuma, N., 1984, Different tissue distributions of two types of thiol proteinase inhibitors from rat liver and epidermis, J. Biochem. 96: 1437-1442.
    • (1984) J. Biochem. , vol.96 , pp. 1437-1442
    • Kominami, E.1    Bando, Y.2    Wakamatsu, N.3    Katunuma, N.4
  • 22
    • 0021875579 scopus 로고
    • Distribution of cathepsins B and H in rat tissues and peripheral blood cells
    • Kominami, E., Tsukahara, T., Bando, Y., and Katunuma, N., 1985, Distribution of cathepsins B and H in rat tissues and peripheral blood cells, J. Biochem. 98: 87-93.
    • (1985) J. Biochem. , vol.98 , pp. 87-93
    • Kominami, E.1    Tsukahara, T.2    Bando, Y.3    Katunuma, N.4
  • 23
    • 0023390566 scopus 로고
    • Delayed hippocampal damage in human following cardiorespiratory arrest
    • Petito, C. K., Feldmann, E., Pulsinelli, W. A., and Plum, F., 1987, Delayed hippocampal damage in human following cardiorespiratory arrest, Neurology 37: 1281-1286.
    • (1987) Neurology , vol.37 , pp. 1281-1286
    • Petito, C.K.1    Feldmann, E.2    Pulsinelli, W.A.3    Plum, F.4
  • 24
    • 0018347695 scopus 로고
    • A new model of bilateral hemispheric ischemia in the unanesthetized rat
    • Pulsinelli, W. A., and Brierley, J. B., 1979, A new model of bilateral hemispheric ischemia in the unanesthetized rat. Stroke 10: 267-272.
    • (1979) Stroke , vol.10 , pp. 267-272
    • Pulsinelli, W.A.1    Brierley, J.B.2
  • 27
    • 0027457336 scopus 로고
    • Cysteine proteinases in rat dorsal root ganglion and spinal cord, with special reference to the co-localization of these enzymes with calcitonin gene-related peptide (CGRP) in lysosomes
    • Taniguchi, K., Tomita, M., Kominami, E., and Uchiyama, Y., 1993, Cysteine proteinases in rat dorsal root ganglion and spinal cord, with special reference to the co-localization of these enzymes with calcitonin gene-related peptide (CGRP) in lysosomes, Brain Res. 601: 143-153.
    • (1993) Brain Res. , vol.601 , pp. 143-153
    • Taniguchi, K.1    Tomita, M.2    Kominami, E.3    Uchiyama, Y.4
  • 28
    • 0022461293 scopus 로고
    • Persistent inhibition of protein synthesis precede delayed neuronal death in postischemic gerbil hippocampus
    • Thilmann, R., Xie, Y., Kleihues, P., and Kiessling, M., 1986, Persistent inhibition of protein synthesis precede delayed neuronal death in postischemic gerbil hippocampus, Acta Neuropathol. (Berl.) 71: 88-93.
    • (1986) Acta Neuropathol. (Berl.) , vol.71 , pp. 88-93
    • Thilmann, R.1    Xie, Y.2    Kleihues, P.3    Kiessling, M.4
  • 30
    • 0026094723 scopus 로고
    • Mechanism and regulation of lysosomal sequestration and proteolysis
    • Ueno, T. and Kominami, E., 1991, Mechanism and regulation of lysosomal sequestration and proteolysis, Biomed. Biochem. Acta 50: 365-371.
    • (1991) Biomed. Biochem. Acta , vol.50 , pp. 365-371
    • Ueno, T.1    Kominami, E.2
  • 31
    • 0023899398 scopus 로고
    • Immunohistochemical localization of cathepsins B, H, and their endogenous inhibitor, cystatin b, in islet endocrine cells of rat pancreas
    • Watanabe, M., Watanabe, T., Ishii, Y., Matsuba, H., Kimura, S., Fujita, T., Kominami, E., Katunuma, N., and Uchiyama, Y., 1988, Immunohistochemical localization of cathepsins B, H, and their endogenous inhibitor, cystatin b, in islet endocrine cells of rat pancreas, J. Histochem. Cytochem. 36: 783-791.
    • (1988) J. Histochem. Cytochem. , vol.36 , pp. 783-791
    • Watanabe, M.1    Watanabe, T.2    Ishii, Y.3    Matsuba, H.4    Kimura, S.5    Fujita, T.6    Kominami, E.7    Katunuma, N.8    Uchiyama, Y.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.