Abstract
The CA1 pyramidal neurons in the hippocampus are known to be selectively vulnerable to brief ischemia of the global cerebrum, resulting in delayed neuronal death several days after ischemic insult (Ito et al., 1975; Pulsinellie et al., 1979;Kirino, 1982;Kirino andSano, 1984a, b; Petito et al., 1987;Bonnekoh et al., 1990). It remains, however, unknown whether this delayed neuronal death is necrosis or apoptosis. According to the morphological criteria of apoptosis, dying cells show chromatin condensation and cell shrinkage, followed by heterophagocytosis (Kerr et al, 1987; Clarke, 1990). In the course of the study of the delayed death of the CA1 pyramidal neurons after transient ischemia, we noticed that shrinkage of these neurons suddenly occurs 3 or 4 days after ischemic insult. This suggests the possibility that delayed death of the CA1 pyramidal neurons after brief ischemia is not necrotic but apoptotic.
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References
Bando, Y., Kominami, E., and Katunuma, N., 1986, Purification and tissue distribution of rat cathepsin L, J. Biochem. 100:35–42.
Bendayan, M., 1982, Double immunocytochemical labelling applying the protein A-gold technique, J. Histochem. Cytochem. 30: 81–85.
Bernstein, H.-G., Kirschke, H., Roskoden, T, and Wiederanders, B., 1990, Distribution of cathepsin L in rat brain as revealed by immunohistochemistry, Acta Histochem. Cytochem. 23: 203–207.
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.
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. (Bed.) 80: 18–25.
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.
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.
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.
Clarke, P. G. H., 1990, Developmental cell death: morphological diversity and multiple mechanisms, Anat. Embryol. 181: 195–213.
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.
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.
Haas, A. and Bright, P.M., 1985, The immunochemical detection and quantitation of intracellular ubiquitin-protein conjugates, J. Biol. Chem. 260: 12464–12473.
Ishii, Y., Hashizume, Y., Watanabe, T., Waguri, S., Sato, N., Yamamoto, M., Hasegawa, S., Kominami, E., and Uchiyama, Y., 1991, Cysteine proteinases in bronchoalveolar epithelial cells and lavage fluid of rat lung, J. Histochem. Cytochem. 39: 461–468.
Ito, U., Spatz, M., Walker, J. T., and Klatzo, I., 1975, Experimental cerebral ischemia in Mongolian gerbils. I. Light microscopic observations. Acta Neuropathol. (Bed.) 32: 209–223.
Katunuma, N., and Kominami, E., 1983, Structures and functions of lysosomal thiol proteinases and their endogenous inhibitors, Curr. Top. Cell Regul. 22: 71–101.
Kerr, J. F. R., Searle, J., Harmon, B. V., and Bishop, C. J., 1987, Apoptosis. In: Perspectives on mammalian cell death (Potten CS ed), pp 93–128. Oxford: Oxford University Press.
Kirino, T., 1982, Delayed neuronal death in the gerbil hippocampus following ischemia. Brain Res. 239: 57–69.
Kirino, T., and Sano, K., 1984a, Selective vulnerability in the gerbil hippocampus following transient ischemia, Acta Neuropathol. (Berl.) 62: 201–208.
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.
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.
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.
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.
Petito, C. K., Feldmann, E., Pulsinelli, W. A., and Plum, F., 1987, Delayed hippocampal damage in human following cardiorespiratory arrest, Neurology 37: 1281–1286.
Pulsinelli, W. A., and Brierley, J. B., 1979, A new model of bilateral hemispheric ischemia in the unanesthetized rat, Stroke 10: 267–272.
Sambrook, J., Fritsch, E. F., and Maniatis, T., 1989, Molecular cloning: A laboratory manual. 2nd ed. Cold Spring Harbor, NY: Cold Spring Habor Press, B.20, E.2.
Takio, K., Kominami, E., Wakamatsu, N., Katunuma, and Titani, K., 1983, Amino acid sequence of rat liver thiol proteinase inhibitor, Biochem. Biophys. Res. Commun. 115: 902–908.
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.
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.
Uchiyama, Y., Nakajima, M., Muno, D., Watanabe, T., Ishii, Y., Waguri, S., Sato, N., and Kominami, E., 1990, Immunocytochemical localization of cathepsins B and H in corticotrophs and melanotrophs of rat pituitary gland, J. Histochem. Cytochem. 38: 633–639.
Ueno, T. and Kominami, E., 1991, Mechanism and regulation of lysosomal sequestration and proteolysis, Biomed. Biochem. Acta 50: 365–371.
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.
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© 1996 Plenum Press, New York
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Nitatori, T., Sato, N., Kominami, E., Uchiyama, Y. (1996). Participation of Cathepsins B, H, and L in Perikaryal Condensation of CA1 Pyramidal Neurons Undergoing Apoptosis After Brief Ischemia. In: Suzuki, K., Bond, J.S. (eds) Intracellular Protein Catabolism. Advances in Experimental Medicine and Biology, vol 389. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0335-0_22
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DOI: https://doi.org/10.1007/978-1-4613-0335-0_22
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