Induction of a 55-kDa PKN cleavage product by ischemia/reperfusion model in the rat retina

Investigative Ophthalmology and Visual Science

Volumn 41, Issue 1, 2000, Pages 29-35

  Sumioka, Kiyoshi ^a,c   Shirai, Yasuhito ^a   Sakai, Norio ^a   Hashimoto, Takeshi ^b   Tanaka, Chikako ^b   Yamamoto, Misao ^c   Takahashi, Mikiko ^a   Ono, Yoshitaka ^a   Saito, Naoaki ^a  

^a KOBE UNIVERSITY   (Japan)

^b Hyogo Inst Aging Brain Cogn D   (Japan)

^c KOBE UNIVERSITY SCHOOL OF MEDICINE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE 3; CASPASE INHIBITOR; N METHYL DEXTRO ASPARTIC ACID; PROTEIN SERINE THREONINE KINASE; TOLONIUM CHLORIDE;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; APOPTOSIS; ARTICLE; CELL LOSS; CONTROLLED STUDY; ENZYME ASSAY; ENZYME DEGRADATION; HISTOPATHOLOGY; INTRAOCULAR HYPERTENSION; MALE; NONHUMAN; PRIORITY JOURNAL; RAT; REPERFUSION INJURY; RETINA CELL; RETINA ISCHEMIA;

ANIMALS; APOPTOSIS; CASPASE 3; CASPASES; DISEASE MODELS, ANIMAL; FLUORESCENT ANTIBODY TECHNIQUE, INDIRECT; IMMUNOBLOTTING; MALE; MOLECULAR WEIGHT; N-METHYLASPARTATE; OLIGOPEPTIDES; PROTEIN-SERINE-THREONINE KINASES; PROTEIN-TYROSINE KINASES; RATS; RATS, WISTAR; REPERFUSION INJURY; RETINAL DISEASES;

EID: 0033989034     PISSN: 01460404     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (53)

1. Kitagawa M, Shibata H, Toshimori M, Mukai H, Ono Y. The role of the unique motifs in the amino-terminal region of PKN on its enzymatic activity. Biochem Biophys Res Commun. 1996;220: 963-968.
2. Mukai H, Ono Y. A novel protein kinase with leucine zipper-like sequences: its catalytic domain is highly homologous to that of protein kinase C. Biochem Biophys Res Commun. 1994;199:897-904.
3. Mukai H, Kitagawa M, Shibata H, et al. Activation of PKN, a novel 120-kDa protein kinase with leucine zipper-like sequences, by unsaturated fatty acids and by limited proteolysis. Biochem Biophys Res Commun. 1994;204:348-356.
4. Amano M, Mukai H, Ono Y, et al. Identification of a putative target for Rho as the serine-threonine kinase protein kinase N. Science. 1996;271:648-650.
5. Shibata H, Mukai H, Inagaki Y, et al. Characterization of the interaction between RhoA and the amino-terminal region of PKN. FEBS Lett. 1996;385:221-224.
6. Watanabe G, Saito Y, Madaule P, et al. Protein kinase N (PKN) and PKN-related protein rhophilin as targets of small GTPase Rho. Science. 1996;271:645-648.
7. Takahashi M, Mukai H, Toshimori M. Miyamoto M. Ono Y. Proteolytic activation of PKN by caspase-3 or related protease during apoptosis. Proc Natl Acad Sci USA. 1998;95:11566-11571.
8. Raff MC. Social controls on cell survival and cell death. Nature. 1992;356:397-400.
9. Wyllie AH. The genetic regulation of apoptosis. Curr Opin Genet Dev. 1995;5:97-104.
10. Darzynkiewicz Z, Li X, Gong J. Assays of cell viability: discrimination of cells dying by apoptosis. Methods Cell Biol. 1994;41:15-38.
11. Martin SJ, Green DR. Protease activation during apoptosis: death by a thousand cuts? Cell. 1995;82:349-352.
12. Salvesen GS, Dixit VM. Caspases: intracellular signaling by proteolysis. Cell. 1997;91:443-446.
13. Alnemri ES, Livingston DJ, Nicholson DW, et al. Human ICE/CED-3 protease nomenclature [letter]. Cell. 1996;87:171.
14. Fraser A, Evan G. A license to kill. Cell. 1996;85:781-784.
15. Nagata S. Apoptosis by death factor. Cell. 1997;88:355-365.
16. Wang S, Miura M, Jung YK, et al. Murine caspase-11, an ICE-interacting protease, is essential for the activation of ICE. Cell. 1998;92:501-509.
17. Thornberry NA, Rano TA, Peterson EP, et al. A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis. J Biol Chem. 1997;272:17907-17911.
18. Li P, Nijhawan D. Budihardjo I, et al. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell. 1997;91:479-489.
19. Zou H, Henzel WJ, Liu X, Lutschg A, Wang X. Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3 [see comments], Cell. 1997;90:405-413.
20. Zhivotovsky B, Gahm A, Orrenius S. Two different proteases are involved in the proteolysis of lamin during apoptosis. Biochem Biophys Res Commun. 1997;233:96-101.
21. Wen LP, Fahrni JA, Troie S, et al. Cleavage of focal adhesion kinase by caspases during apoptosis. J Biol Chem. 1997;272:26056-26061.
22. Yang F, Sun X, Beech W, et al. Antibody to caspase-cleaved actin detects apoptosis in differentiated neuroblastoma and plaque-associated neurons and microglia in Alzheimer's disease [see comments]. Am J Pathol. 1998;152:379-389.
23. Nicholson DW, Ali A, Thornberry NA, et al. Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis [see comments]. Nature. 1995;376:37-43.
24. Hughes WF. Quantitation of ischemic damage in the rat retina. Exp Eye Res. 1991;53:573-582.
25. Buchi ER. Cell death in the rat retina after a pressure-induced ischaemia-reperfusion insult: an electron microscopic study, I: ganglion cell layer and inner nuclear layer. Exp Eye Res. 1992;55: 605-613.
26. Kuroiwa S, Katai N, Shibuki H, et al. Expression of cell cycle-related genes in dying cells in retinal ischemic injury. Invest Ophthalmol Vis Sci. 1998;39:610-617.
27. Mukai H, Toshimori M, Shibata H, et al. Interaction of PKN with alpha-actinin. J Biol Chem. 1997;272:4740-4746.
28. ω-nitro-L-arginine methyl ester protects retinal neurons against N-methyl-D-aspartate-induced neurotoxicity in vivo. Eur J Pharmacol. 1997;328:45-49.
29. Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970;227:680-685.
30. Lombardi G, Moroni F. Glutamate receptor antagonists protect against ischemia-induced retinal damage. Eur J Pharmacol. 1994; 271:489-495.
31. Mosinger JL, Price MT, Bai HY, et al. Blockade of both NMDA and non-NMDA receptors is required for optimal protection against ischemic neuronal degeneration in the in vivo adult mammalian retina. Exp Neurol. 1991;113:10-17.
32. Kihara S, Shiraishi T, Nakagawa S, Toda K, Tabuchi K. Visualization of DNA double strand breaks in the gerbil hippocampal CAI following transient ischemia. Neurosci Lett. 1994;175:133-136.
33. Nitatori T, Sato N, Waguri S, et al. Delayed neuronal death in the CA1 pyramidal cell layer of the gerbil hippocampus following transient ischemia is apoptosis. J Neurosci. 1995;15:1001-1011.
34. Kaneda K, Kashii S, Kurosawa T, et al. Apoptotic DNA fragmentation and upregulation of Bax induced by transient ischemia of the rat retina. Brain-Res. 1999;815:11-20.
35. Adachi K, Fujita Y, Morizane C, et al. Inhibition of NMDA receptors and nitric oxide synthase reduces ischemic injury of the retina. Eur J Pharmacol. 1998;350:53-57.
36. Billig H, Furuta I, Rivier C, et al. Apoptosis in testis germ cells: developmental changes in gonadotropin dependence and localization to selective tubule stages [see comments]. Endocrinology. 1995;136:5-12.
37. Murphy KM, Heimberger AB, Loh DY. Induction by antigen of intrathymic apoptosis of CD4+CD8+TCRlo thymocytes in vivo. Science. 1990;250:1720-1723.
38. Parry SL, Hasbold J, Holman M, Klaus GG. Hypercross-linking surface IgM or IgD receptors on mature B cells induces apoptosis that is reversed by costimulation with IL-4 and anti-CD40. J Immunol. 1994;152:2821-2829.
39. Tenneti L, D'Emilia DM, Troy CM, Lipton SA. Role of caspases in N-methyl-D-aspartate-induced apoptosis in cerebrocortical neurons. J Neurochem. 1998;71:946-959.
40. Du Y, Bales KR, Dodel RC, et al. Activation of a caspase 3-related cysteine protease is required for glutamate-mediated apoptosis of cultured cerebellar granule neurons. Proc Natl Acad Sci USA. 1997;94:11657-11662.
41. Hartveit E, Brandstatter JH, Sassoe Pognetto M, et al. Localization and developmental expression of the NMDA receptor subunit NR2A in the mammalian retina. J Camp Neurol. 1994;348:570-582.
42. Wenzel A, Benke D, Monler H, Fritschy JM. N-methyl-D-aspartate receptors containing the NR2D subunit in the retina are selectively expressed in rod bipolar cells. Neuroscience. 1997; 78:1105-1112.
43. + ATPase and NMDA receptor subunit I. Vision Res. 1998;38:1455-1477.
44. Brandstatter JH, Harveit E, Sassoe PM, Wassle H. Expression of NMDA and high-affinity kainate receptor subunit mRNAs in the adult rat retina. Eur J Neurosci. 1994;6:1100-1112.
45. Peng B, Morrice NA, Groenen LC, Wettenhall RE. Phosphorylation events associated with different states of activation of a hepatic cardiolipin/protease-activated protein kinase. Structural identity to the protein kinase N-type protein kinases. J Biol Chem. 1996;27: 32233-32240.
46. Cardone MH, Salvesen GS, Widmann C, Johnson G, Frisch SM. The regulation of anoikis: MEKK-1 activation requires cleavage by caspases. Cell. 1997;90:315-323.
47. Rudel, T, Bokoch, G. M, Cryns, VL, et al. Membrane and morphological changes in apoptotic cells regulated by caspase-mediated activation of PAK2. Science. 1997;276:1571-1574.
48. Emoto Y, Manome Y, Meinhardt G, et al. Proteolytic activation of protein kinase C delta by an ICE-like protease in apoptotic cells. EMBO J. 1995;14:6148-6156.
49. Matsuzawa K, Kosako H, Inagaki N, et al. Domain-specific phosphorylation of vimentin and glial fibrillary acidic protein by PKN. Biochem Biophys Res Commun. 1997;234:621-625.
50. Mukai H, Toshimori M, Shibata H, et al. PKN associates and phosphorylates the head-rod domain of neurofilament protein. J Biol Chem. 1996;271:9816-9822.
51. Brancolini C, Benedetti M, Schneider C. Microfilament reorganization during apoptosis: the role of Gas2, a possible substrate for ICE-like proteases. EMBO J. 1995;14:5179-5190.
52. Martin SJ, O'Brien GA, Nishioka WK, et al. Proteolysis of fodrin (non-erythroid spectrin) during apoptosis. J Biol Chem. 270;6425-6428.
53. Kothakota S, Azuma T, Reinhard C, et al. Caspase-3-generated fragment of gelsolin: effector of morphological change in apoptosis Science. 1997;278:294-298.