Mammalian D-aspartyl endopeptidase: A scavenger for noxious racemized proteins in aging

Biochemical and Biophysical Research Communications

Volumn 314, Issue 3, 2004, Pages 730-736

  Kinouchi, Tadatoshi ^a   Ishiura, Shoichi ^b   Mabuchi, Yoko ^b   Urakami Manaka, Yasuko ^b   Nishio, Hideki ^c   Nishiuchi, Yuji ^c   Tsunemi, Masahiko ^c   Takada, Katsumi ^c   Watanabe, Masatomo ^d   Ikeda, Masashi ^d   Matsui, Hisao ^d   Tomioka, Shigeo ^b   Kawahara, Hiroyuki ^b,e   Hamamoto, Toshiro ^a   Suzuki, Koichi ^b,f   Kagawa, Yasuo ^a,g  

^a JICHI MEDICAL UNIVERSITY   (Japan)

^b UNIVERSITY OF TOKYO   (Japan)

^c Peptide Institute Inc   (Japan)

^d DOKKYO MEDICAL UNIVERSITY   (Japan)

^e HOKKAIDO UNIVERSITY   (Japan)

^f TORAY INDUSTRIES INC   (Japan)

^g Kochi Women's University   (Japan)

Author keywords

Aging; D amino acid; D aspartic acid; Mitochondria; Peptidase; Protease; Protease inhibitor; Proteinase; Racemization

Indexed keywords

ACID PROTEINASE; ASPARTIC ACID; ASPARTIC PROTEINASE; BENZOYLARGINYLHISTIDYL(DEXTRO ASPARTIC ACID)METHYL CHLORIDE; CYSTEINE PROTEINASE; DEXTRO ASPARTIC ACID; DEXTRO ASPARTYL ENDOPEPTIDASE; ENZYME INHIBITOR; LACTACYSTIN; OLIGOPEPTIDE; PROTEASOME; PROTEIN; PROTEINASE; PROTEINASE INHIBITOR; SCAVENGER; UNCLASSIFIED DRUG;

AGING; ANIMAL; ANIMAL TISSUE; ARTICLE; CAENORHABDITIS ELEGANS; CHEMISTRY; COMPLEX FORMATION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME SPECIFICITY; ENZYMOLOGY; ESCHERICHIA COLI; FEMALE; GENETICS; IC 50; ISOLATION AND PURIFICATION; ISOMERISM; LIVER MITOCHONDRION; MALE; MAMMAL; METABOLISM; MITOCHONDRIAL MEMBRANE; MOLECULAR WEIGHT; MOUSE; MOUSE STRAIN; NONHUMAN; PRIORITY JOURNAL; RABBIT; SACCHAROMYCES CEREVISIAE;

CAENORHABDITIS; CAENORHABDITIS ELEGANS; ESCHERICHIA COLI; MAMMALIA; ORYCTOLAGUS CUNICULUS; SACCHAROMYCES; SACCHAROMYCES CEREVISIAE;

EID: 9144273777     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2003.12.147     Document Type: Article

References (25)

1. Geiger T., Clarke S. Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. Succinimide-linked reactions that contribute to protein degradation. J. Biol. Chem. 262:1987;785-794.
2. Muraoka S., Fujii N., Tamanoi I., Harada K. Characterization of a protein containing D-aspartic acid in aged mouse lens. Biochem. Biophys. Res. Commun. 146:1987;1432-1438.
3. McFadden P.N., Clarke S. Methylation at D-aspartyl residues in erythrocytes: possible step in the repair of aged membrane proteins. Proc. Natl. Acad. Sci. USA. 79:1982;2460-2464.
4. Aswad D.W. Stoichiometric methylation of porcine adrenocorticotropin by protein carboxyl methyltransferase requires deamidation of asparagine 25. Evidence for methylation at the alpha-carboxyl group of atypical L-isoaspartyl residues. J. Biol. Chem. 259:1984;10714-10721.
5. Shapira R., Austin G.E., Mirra S.S. Neuritic plaque amyloid in Alzheimer's disease is highly racemized. J. Neurochem. 50:1988;69-74.
6. Tomiyama T., Asano S., Furiya Y., Shirasawa T., Endo N., Mori H. Racemization of Asp23 residue affects the aggregation properties of Alzheimer amyloid beta protein analogues. J. Biol. Chem. 269:1994;10205-10208.
7. Iwatsubo T., Saido T.C., Mann D.M., Lee V.M., Trojanowski J.Q. Full-length amyloid-beta (1-42(43)) and amino-terminally modified and truncated amyloid-beta 42(43) deposit in diffuse plaques. Am. J. Pathol. 149:1996;1823-1830.
8. Kenessey A., Yen S.H., Liu W.K., Yang X.R., Dunlop D.S. Detection of D-aspartate in tau proteins associated with Alzheimer's paired helical filaments. Brain Res. 675:1995;183-189.
9. Fujii N., Ishibashi Y., Satoh K., Fujino M., Harada K. Simultaneous racemization and isomerization at specific aspartic acid residues in alpha B-crystallin from the aged human lens. Biochim. Biophys. Acta. 1204:1994;157-163.
10. Powell J.T., Vine N., Crossman M. On the accumulation of D-aspartate in elastin and other proteins of the ageing aorta. Atherosclerosis. 97:1992;201-208.
11. Shapiro S.D., Endicott S.K., Province M.A., Pierce J.A., Campbell E.J. Marked longevity of human lung parenchymal elastic fibers deduced from prevalence of D-aspartate and nuclear weapons-related radiocarbon. J. Clin. Invest. 87:1991;1828-1834.
12. Fisher G.H., Garcia N.M., Payan I.L., Cadilla-Perezrios R., Sheremata W.A., Man E.H. D-Aspartic acid in purified myelin and myelin basic protein. Biochem. Biophys. Res. Commun. 135:1986;683-687.
13. Cloos P.A., Fledelius C. Collagen fragments in urine derived from bone resorption are highly racemized and isomerized: a biological clock of protein aging with clinical potential. Biochem. J. 345(Pt 3):2000;473-480.
14. Weber D.J., McFadden P.N., Caughey B. Measurement of altered aspartyl residues in the scrapie associated form of prion protein. Biochem. Biophys. Res. Commun. 246:1998;606-608.
15. Mori H., Ishii K., Tomiyama T., Furiya Y., Sahara N., Asano S., Endo N., Shirasawa T., Takio K. Racemization: its biological significance on neuropathogenesis of Alzheimer's disease. Tohoku J. Exp. Med. 174:1994;251-262.
16. Shimizu T., Watanabe A., Ogawara M., Mori H., Shirasawa T. Isoaspartate formation and neurodegeneration in Alzheimer's disease. Arch. Biochem. Biophys. 381:2000;225-234.
17. Man E.H., Sandhouse M.E., Burg J., Fisher G.H. Accumulation of D-aspartic acid with age in the human brain. Science. 220:1983;1407-1408.
18. Fisher G.H., D'Aniello A., Vetere A., Padula L., Cusano G.P., Man E.H. Free D-aspartate and D-alanine in normal and Alzheimer's brain. Brain Res. Bull. 26:1991;983-985.
19. Watanabe T., Kera Y., Matsumoto T., Yamada R.H. Purification and kinetic properties of a D-amino-acid peptide hydrolyzing enzyme from pig kidney cortex and its tentative identification with renal membrane dipeptidase. Biochim. Biophys. Acta. 1298:1996;109-118.
20. Lee J.M., Petrucelli L., Fisher G., Ramdath S., Castillo J., Di Fiore M.M., D'Aniello A. Evidence for D-aspartyl-beta-amyloid secretase activity in human brain. J. Neuropathol. Exp. Neurol. 61:2002;125-131.
21. Seeger M., Gordon C., Ferrell K., Dubiel W. Characteristics of 26S proteases from fission yeast mutants, which arrest in mitosis. J. Mol. Biol. 263:1996;423-431.
22. Kanayama H.O., Tamura T., Ugai S., Kagawa S., Tanahashi N., Yoshimura T., Tanaka K., Ichihara A. Demonstration that a human 26S proteolytic complex consists of a proteasome and multiple associated protein components and hydrolyzes ATP and ubiquitin-ligated proteins by closely linked mechanisms. Eur. J. Biochem. 206:1992;567-578.
23. Ishiura S., Mabuchi Y., Urakami-Manaka Y., Isobe K., Tagawa K., Maruyama K., Sorimachi H., Suzuki K. Proteases involved in the processing of the Alzheimer's disease amyloid precursor protein. Hopsu-Havu V.K., Järvinen M., Kirschke H. Proteolysis in Cell Functions. 1997;507-512 IOS Press.
24. Omura S., Ikeda H., Tanaka H. Selective production of specific components of avermectins in Streptomyces avermitilis. J. Antibiot. (Tokyo). 44:1991;560-563.
25. Nagata Y., Fukuda A., Sakai M., Iida T., Kawaguchi-Nagata K. D-Amino acid contents of mitochondria and some purple bacteria. J. Mol. Catal. B Enzymat. 12:2001;109-113.