An N-terminal fragment of ProSAAS (a granin-like neuroendocrine peptide precursor) is associated with tau inclusions in Pick's disease

Biochemical and Biophysical Research Communications

Volumn 308, Issue 3, 2003, Pages 646-654

  Kikuchi, Kenji ^a   Arawaka, Shigeki ^a   Koyama, Shingo ^a   Kimura, Hideki ^a   Ren, Chang Hong ^a   Wada, Manabu ^a   Kawanami, Toru ^a   Kurita, Keiji ^a   Daimon, Makoto ^a   Kawakatsu, Shinobu ^a   Kadoya, Toshihiko ^b   Goto, Kaoru ^a   Kato, Takeo ^a  

^a YAMAGATA UNIVERSITY   (Japan)

^b KIRIN BREWERY CO LTD   (Japan)

Author keywords

Neurodegeneration; Pick body; Pick's disease; ProSAAS; Tau; Tauopathy

Indexed keywords

BRAIN EXTRACT; DIACYLGLYCEROL KINASE; DIACYLGLYCEROL KINASE ZETA; ENZYME ANTIBODY; POLYCLONAL ANTIBODY; PROTEIN PRECURSOR; PROTEIN PROSAAS; TAU PROTEIN; UBIQUITIN; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ANTIGEN BINDING; ARTICLE; CELL INCLUSION; CONTROLLED STUDY; CROSS REACTION; EMBRYO; HUMAN; HUMAN CELL; HUMAN TISSUE; MASS SPECTROMETRY; MOLECULAR WEIGHT; NERVE CELL; NERVE DEGENERATION; NIEMANN PICK DISEASE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN STRUCTURE; TWO DIMENSIONAL GEL ELECTROPHORESIS; WESTERN BLOTTING;

EID: 0042164989     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(03)01391-3     Document Type: Article

References (35)

1. Lee V.M., Goedert M., Trojanowski J.Q. Neurodegenerative tauopathies. Annu. Rev. Neurosci. 24:2001;1121-1159.
2. Mirra S.S., Hyman B.T. Tau-associated disorders (Tauopathies). Graham D.I., Lantos P.L. Greenfield's Neuropathology. 2002;226-232 Edward Arnold, UK.
3. Clark L.N., Poorkaj P., Wszolek Z., Geschwind D.H., Nasreddine Z.S., Miller B., Li D., Payami H., Awert F., Markopoulou K., Andreadis A., D'Souza I., Lee V.M., Reed L., Trojanowski J.Q., Zhukareva V., Bird T., Schellenberg G., Wilhelmsen K.C. Pathogenic implications of mutations in the tau gene in pallido-ponto-nigral degeneration and related neurodegenerative disorders linked to chromosome 17. Proc. Natl. Acad. Sci. USA. 95:1998;13103-13107.
4. ′-splice-site mutations in tau with the inherited dementia FTDP-17. Nature. 393:1998;702-705.
5. Poorkaj P., Bird T.D., Wijsman E., Nemens E., Garruto R.M., Anderson L., Andreadis A., Wiederholt W.C., Raskind M., Schellenberg G.D. Tau is a candidate gene for chromosome 17 frontotemporal dementia. Ann. Neurol. 43:1998;815-825.
6. Spillantini M.G., Murrell J.R., Goedert M., Farlow M.R., Klug A., Ghetti B. Mutation in the tau gene in familial multiple system tauopathy with presenile dementia. Proc. Natl. Acad. Sci. USA. 95:1998;7737-7741.
7. Lewis J., McGowan E., Rockwood J., Melrose H., Nacharaju P., Van Slegtenhorst M., Gwinn-Hardy K., Paul Murphy M., Baker M., Yu X., Duff K., Hardy J., Corral A., Lin W.L., Yen S.H., Dickson D.W., Davies P., Hutton M. Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein. Nat. Genet. 25:2000;402-405.
8. Hong M., Zhukareva V., Vogelsberg-Ragaglia V., Wszolek Z., Reed L., Miller B.I., Geschwind D.H., Bird T.D., McKeel D., Goate A., Morris J.C., Wilhelmsen K.C., Schellenberg G.D., Trojanowski J.Q., Lee V.M. Mutation-specific functional impairments in distinct tau isoforms of hereditary FTDP-17. Science. 282:1998;1914-1917.
9. D'Souza I., Poorkaj P., Hong M., Nochlin D., Lee V.M., Bird T.D., Schellenberg G.D. Missense and silent tau gene mutations cause frontotemporal dementia with parkinsonism-chromosome 17 type, by affecting multiple alternative RNA splicing regulatory elements. Proc. Natl. Acad. Sci. USA. 96:1999;5598-5603.
10. Ihara Y. PHF and PHF-like fibrils - cause or consequence? Neurobiol. Aging. 22:2001;123-126.
11. Yoshida H., Watanabe A., Ihara Y. Collapsin response mediator protein-2 is associated with neurofibrillary tangles in Alzheimer's disease. J. Biol. Chem. 273:1998;9761-9768.
12. Ulloa L., Montejo de Garcini E., Gomez-Ramos P., Moran M.A., Avila J. Microtubule-associated protein MAP1B showing a fetal phosphorylation pattern is present in sites of neurofibrillary degeneration in brains of Alzheimer's disease patients. Mol. Brain Res. 26:1994;113-122.
13. McKee A.C., Kosik K.S., Kennedy M.B., Kowall N.W. Hippocampal neurons predisposed to neurofibrillary tangle formation are enriched in type II calcium/calmodulin-dependent protein kinase. J. Neuropathol. Exp. Neurol. 49:1990;49-63.
14. Masliah E., Iimoto D.S., Mallory M., Albright T., Hansen L., Saitoh T. Casein kinase II alteration precedes tau accumulation in tangle formation. Am. J. Pathol. 140:1992;263-268.
15. Baum L., Hansen L., Masliah E., Saitoh T. Glycogen synthase kinase 3 alteration in Alzheimer disease is related to neurofibrillary tangle formation. Mol. Chem. Neuropathol. 29:1996;253-261.
16. Kuret J., Johnson G.S., Cha D., Christenson E.R., DeMaggio A.J., Hoekstra M.F. Casein kinase 1 is tightly associated with paired-helical filaments isolated from Alzheimer's disease brain. J. Neurochem. 69:1997;2506-2515.
17. Ghoshal N., Smiley J.F., DeMaggio A.J., Hoekstra M.F., Cochran E.J., Binder L.I., Kuret J. A new molecular link between the fibrillar and granulovacuolar lesions of Alzheimer's disease. Am. J. Pathol. 155:1999;1163-1172.
18. Fricker L.D., McKinzie A.A., Sun J., Curran E., Qian Y., Yan L., Patterson S.D., Courchesne P.L., Richards B., Levin N., Mzhavia N., Devi L.A., Douglass J. Identification and characterization of proSAAS, a granin-like neuroendocrine peptide precursor that inhibits prohormone processing. J. Neurosci. 20:2000;639-648.
19. Goto K., Kondo H. A 104-kDa diacylglycerol kinase containing ankyrin-like repeats localizes in the cell nucleus. Proc. Natl. Acad. Sci. USA. 93:1996;11196-11201.
20. Kosik K.S., Orecchio L.D., Binder L., Trojanowski J.Q., Lee V.M., Lee G. Epitopes that span the tau molecule are shared with paired helical filaments. Neuron. 1:1988;817-825.
21. Goedert M., Jakes R., Crowther R.A., Six J., Lubke U., Vandermeeren M., Cras P., Trojanowski J.Q., Lee V.M. The abnormal phosphorylation of tau protein at Ser-202 in Alzheimer disease recapitulates phosphorylation during development. Proc. Natl. Acad. Sci. USA. 90:1993;5066-5070.
22. Schwab C., DeMaggio A.J., Ghoshal N., Binder L.I., Kuret J., McGeer P.L. Casein kinase 1 delta is associated with pathological accumulation of tau in several neurodegenerative diseases. Neurobiol. Aging. 21:2000;503-510.
23. Arawaka S., Hasegawa H., Tandon A., Janus C., Chen F., Yu G., Kikuchi K., Koyama S., Kato T., Fraser P.E., George-Hyslop P.H. The levels of mature glycosylated nicastrin are regulated and correlate with gamma-secretase processing of amyloid beta-precursor protein. J. Neurochem. 83:2002;1065-1071.
24. Kato T., Kurita K., Seino T., Kadoya T., Horie H., Wada M., Kawanami T., Daimon M., Hirano A. Galectin-1 is a component of neurofilamentous lesions in sporadic and familial amyotrophic lateral sclerosis. Biochem. Biophys. Res. Commun. 282:2001;166-172.
25. Jensen O.N., Podtelejnikov A., Mann M. Delayed extraction improves specificity in database searches by matrix-assisted laser desorption/ionization peptide maps. Rapid Commun. Mass Spectrum. 10:1996;1371-1378.
26. Uchihara T., Tsuchiya K., Kondo H., Hayama T., Ikeda K. Widespread appearance of Alz-50 immunoreactive neurons in the human brain with cerebral infarction. Stroke. 26:1995;2145-2148.
27. Kato T., Katagiri T., Hirano A., Kawanami T., Sasaki H. Lewy body-like hyaline inclusions in sporadic motor neuron disease are ubiquitinated. Acta Neuropathol. (Berl). 77:1989;391-396.
28. Greenberg S.G., Davies P. A preparation of Alzheimer paired helical filaments that displays distinct τ proteins by polyacrylamide gel electrophoresis. Proc. Natl. Acad. Sci. USA. 87:1990;5827-5831.
29. Mzhavia N., Berman Y., Che F.Y., Fricker L.D., Devi L.A. ProSAAS processing in mouse brain and pituitary. J. Biol. Chem. 276:2001;6207-6213.
30. Sayah M., Fortenberry Y., Cameron A., Lindberg I. Tissue distribution and processing of proSAAS by proprotein convertases. J. Neurochem. 76:2001;1833-1841.
31. Nixon R.A., Mathews P.M., Cataldo A.M. The neuronal endosomal-lysosomal system in Alzheimer's disease. J. Alzheimers Dis. 3:2001;97-107.
32. Murakami N., Oyama F., Gu Y., McLennan I.S., Nonaka I., Ihara Y. Accumulation of tau in autophagic vacuoles in chloroquine myopathy. J. Neuropathol. Exp. Neurol. 57:1998;664-673.
33. Fortenberry Y., Hwang J.R., Apletalina E.V., Lindberg I. Functional characterization of ProSAAS: similarities and differences with 7B2. J. Biol. Chem. 277:2002;5175-5186.
34. Qian Y., Devi L.A., Mzhavia N., Munzer S., Seidah N.G., Fricker L.D. The C-terminal region of proSAAS is a potent inhibitor of prohormone convertase 1. J. Biol. Chem. 275:2000;23596-23601.
35. Davidsson P., Sjogren M., Andreasen N., Lindbjer M., Nilsson C.L., Westman-Brinkmalm A., Blennow K. Studies of the pathophysiological mechanisms in frontotemporal dementia by proteome analysis of CSF proteins. Brain Res. Mol. Brain Res. 109:2002;128-133.