A rat model of human FENIB (familial encephalopathy with neuroserpin inclusion bodies)

Biochemical and Biophysical Research Communications

Volumn 346, Issue 3, 2006, Pages 1040-1047

  Takano, Katsura ^a,c   Kitao, Yasuko ^a   Inagi, Reiko ^f   Momoi, Takashi ^e   Matsuyama, Tomohiro ^d   Miyata, Toshio ^f   Yoneda, Yukio ^c   Iso, Hiroyuki ^d   Stern, David M ^g   Hori, Osamu ^a   Ogawa, Satoshi ^a,b  

^a KANAZAWA UNIV SCHOOL OF MEDICINE   (Japan)

^b The 21st Century COE Program on Innovative Brain Sciences for Development   (Japan)

^c KANAZAWA UNIVERSITY   (Japan)

^d HYOGO COLLEGE OF MEDICINE   (Japan)

^e NATIONAL INSTITUTE OF NEUROSCIENCE   (Japan)

^f TOKAI UNIVERSITY   (Japan)

^g UNIVERSITY OF CINCINNATI COLLEGE OF MEDICINE   (United States)

Author keywords

Neuronal cell death; Neuroserpin; Oxidant stress; Oxygen glucose regulated protein (ORP GRP); Protein malfolding

Indexed keywords

BRAIN EXTRACT; CASPASE 12; CASPASE 3; HEAT SHOCK PROTEIN; MEGSIN; SERINE PROTEINASE INHIBITOR; UNCLASSIFIED DRUG;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; BRAIN CORTEX; BRAIN DISEASE; CELL DENSITY; CELL FUNCTION; CELL LOSS; CELL POPULATION; CELL SPECIFICITY; CELL VIABILITY; CONTROLLED STUDY; DOPAMINERGIC NERVE CELL; ENDOPLASMIC RETICULUM; ENZYME ACTIVATION; FAMILIAL ENCEPHALOPATHY WITH NEUROSERPIN INCLUSION BODIES; GENE OVEREXPRESSION; HIPPOCAMPUS; MOTOR COORDINATION; NONHUMAN; PERIODIC ACID SCHIFF STAIN; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN EXPRESSION; RAT; SUBSTANTIA NIGRA; TRANSGENIC ANIMAL;

ANIMALS; ANIMALS, GENETICALLY MODIFIED; BRAIN; CELL DEATH; DISEASE MODELS, ANIMAL; DISEASE SUSCEPTIBILITY; ENDOPLASMIC RETICULUM; HIPPOCAMPUS; HUMANS; INCLUSION BODIES; NEURONS; NEUROPEPTIDES; RATS; SERPINS;

EID: 33745204166     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.06.016     Document Type: Article

References (26)

1. Lomas D.A., and Mahadeva R. Alpha1-antitrypsin polymerization and the serpinopathies: pathobiology and prospects for therapy. J. Clin. Invest. 110 (2002) 1585-1590
2. Primhak R.A., and Tanner M.S. Alpha-1 antitrypsin deficiency. Arch. Dis. Child. 85 (2001) 2-5
3. Carrell R.W., and Lomas D.A. Conformational disease. Lancet 350 (1997) 134-138
4. Davis R.L., Shrimpton A.E., Carrell R.W., Lomas D.A., Gerhard L., Baumann B., Lawrence D.A., Yepes M., Kim T.S., Ghetti B., Piccardo P., Takao M., Lacbawan F., Muenke M., Sifers R.N., Bradshaw C.B., Kent P.F., Collins G.H., Larocca D., and Holohan P.D. Association between conformational mutations in neuroserpin and onset and severity of dementia. Lancet 359 (2002) 2242-2247
5. Davis R.L., Holohan P.D., Shrimpton A.E., Tatum A.H., Daucher J., Collins G.H., Todd R., Bradshaw C., Kent P., Feiglin D., Rosenbaum A., Yerby M.S., Shaw C.M., Lacbawan F., and Lawrence D.A. Familial encephalopathy with neuroserpin inclusion bodies. Am. J. Pathol. 155 (1999) 1901-1913
6. Miyata T., Nangaku M., Suzuki D., Inagi R., Uragami K., Sakai H., Okubo K., and Kurokawa K. A mesangium-predominant gene, megsin, is a new serpin upregulated in IgA nephropathy. J. Clin. Invest. 102 (1998) 828-836
7. Miyata T., Inagi R., Nangaku M., Imasawa T., Sato M., Izuhara Y., Suzuki D., Yoshino A., Onogi H., Kimura M., Sugiyama S., and Kurokawa K. Overexpression of the serpin megsin induces progressive mesangial cell proliferation and expansion. J. Clin. Invest. 109 (2002) 585-593
8. Inagi R., Nangaku M., Usud N., Shimizu A., Onogi H., Izuhara Y., Nakazato K., Ueda Y., Oishi H., Takahashi S., Yamamoto M., Suzuki D., Kurokawa K., van Ypersele de Strihou C., and Miyata T. A novel serpinopathy in rat kidney and pancreas induced by overexpression of megsin. J. Am. Soc. Nephrol. 16 (2005) 1339-1349
9. Inagi R., Onogi H., Nangaku M., Ueyama H., Kitao Y., Ogawa S., Kurokawa K., Couser W.G., and Miyata T. Involvement of endoplasmic reticulum (ER) stress in podocyte injury associated with a novel transgenic model of serpinopathy. Kidney Int. 68 (2005) 2639-2650
10. Kuwabara K., Matsumoto M., Ikeda J., Hori O., Ogawa S., Maeda Y., Kitagawa K., Imuta N., Kinoshita K., Stern D., Yanagi H., and Kamada T. Purification and characterization of a novel stress protein, the 150 kDa oxygen regulated protein (ORP150), from cultured rat astrocytes, and its expression in ischemic mouse brain. J. Biol. Chem. 279 (1996) 5025-5032
11. Kouroku Y., Fujita E., Jimbo A., Kikuchi T., Yamagata T., Momoi M.Y., Kominami E., Kuida K., Sakamaki K., Yonehara S., and Momoi T. Polyglutamine aggregates stimulate ER stress signals and caspase-12 activation. Hum. Mol. Genet. 11 (2002) 1505-1515
12. Ozawa K., Kondo T., Hori O., Kitao Y., Stern D., Eisenmenger W., Ogawa S., and Ohshima T. Expression of ORP150 (150 kDa oxygen regulated protein) accelerates wound healing by modulating intracellular VEGF transport. J. Clin. Invest. 108 (2001) 41-50
13. Bndo Y., Tsukamot Y., Katayama T., Ozawa K., Kitao Y., Hori O., Stern D.M., Yamauch A., and Ogawa S. ORP150/HSP12A protects renal tubular epithelium from ischemia-induced cell death. FASEB J. 18 (2004) 1401-1403
14. Wang X.Z., Lawson B., Brewer J.W., Zinszner H., Sanjay A., Mi L.J., Boorstein R., Kreibich G., Hendershot L.M., and Ron D. Signals from the stressed endoplasmic reticulum induce C/EBP-homologous protein (CHOP/GADD153). Mol. Cell. Biol. 16 (1996) 4273-4280
15. Fujikawa T., Miguchi S., Kanada N., Nakai N., Ogata M., Suzuki I., and Nakashima K. Acanthopanax senticosus Harms as a prophylactic for MPTP-induced Parkinson's disease in rats. J. Ethnopharmacol. 97 (2004) 375-381
16. Kitao Y., Ozawa K., Miyazaki M., Tamatani M., Kobayashi T., Yanagi H., Okabe M., Ikawa M., Yamashima T., Tohyama M., Stern D., Hori O., and Ogawa S. Expression of 150 kDa oxygen regulated protein (ORP150), a molecular chaperone in the endoplasmic reticulum, rescues hippocampal neurons from glutamate toxicity. J. Clin. Invest. 108 (2001) 1439-1450
17. Zhu D.Y., Liu S.H., Sun H.S., and Lu Y.M. Expression of inducible nitric oxide synthase after focal cerebral ischemia stimulates neurogenesis in the adult rodent dentate gyrus. J. Neurosci. 23 (2003) 223-229
18. Przedborski S., Jackson-Lewis V., Yokoyama R., Shibata T., Dawson V.L., and Dawson T.M. Role of neuronal nitric oxide in 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)-induced dopaminergic neurotoxicity. Proc. Natl. Acad. Sci. USA 93 (1996) 4565-4571
19. Wynn R.M., Davie J.R., Cox P.P., and Chuang D.T. Molecular chaperones: heat-shock proteins, foldases, and matchmakers. J. Lab. Clin. Med. 124 (1994) 31-36
20. Kitao Y., Hashimoto K., Matsuyama T., Iso H., Tamatani T., Hori O., Stern D.M., Kano M., Ozawa K., and Ogawa S. ORP150/HSP12A regulates Purkinje cell survival: a role for endoplasmic reticulum stress in cerebellar development. J. Neurosci. 24 (2004) 1486-1496
21. Ogawa S., Gerlach H., Esposito C., Macaulay A.P., Brett J., and Stern D. Hypoxia modulates the barrier and coagulant function of cultured bovine endothelium. J. Clin. Invest. 85 (1990) 1090-1098
22. Ozawa K., Tsukamoto Y., Hori O., Kitao Y., Yanagi H., Stern D., and Ogawa S. Regulation of tumor angiogeensis by ORP150, an inducible endoplasmic reticulum chaperone. Can. Res. 61 (2001) 4206-4213
23. Reaves B., Horn M., and Banting G. TGN38/41 recycles between the cell surface and the TGN: brefeldin A affects its rate of return to the TGN. Mol. Biol. Cell 4 (1993) 93-105
24. Hori O., Matsumoto M., Maeda M., Kuwabara K., Ueda H., Ohtsuki T., Kinishita T., Ogawa S., Kamada T., and Stern D. Exposure of astrocytes to hypoxia/reoxygenation results in intracellular glucose depletion and enhanced expression of glucose-regulated proteins (GRPs). J. Neurochem. 66 (1996) 973-979
25. Bando Y., Ogawa S., Yamaguchi A., Kuwabara K., Ozawa K., Hori O., Yanagi H., Tamatani M., and Tohyama M. The 150 kDa oxygen regulated protein (ORP150) functions as a novel molecular chaperone in the protein transport of the MDCK cells. Am. J. Physiol. (Cell. Physiol.) 278 (2000) C1172-C1182
26. Ozawa K., Kondo T., Hori O., Kitao Y., Stern D., Eisenmenger W., Ogawa S., and Ohshima T. Expression of ORP150 (150 kDa oxygen regulated protein) accelerates wound healing by modulating intracellular VEGF transport. J. Clin. Invest. 108 (2001) 41-50