Cysteine proteinases are responsible for characteristic transketolase alterations in Alzheimer fibroblasts

Journal of Cellular Physiology

Volumn 172, Issue 1, 1997, Pages 63-68

  Paoletti, Francesco ^a   Mocali, Alessandra ^a   Tombaccini, Donatella ^a  

^a UNIVERSITY OF FLORENCE   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

CATHEPSIN H; CYSTEINE PROTEINASE; CYSTEINE PROTEINASE INHIBITOR; N [N (3 CARBOXYOXIRANE 2 CARBONYL)LEUCYL]AGMATINE; N ACETYLLEUCYLLEUCYLNORLEUCINAL; TRANSKETOLASE; UNCLASSIFIED DRUG;

ALZHEIMER DISEASE; ARTICLE; ENZYME ACTIVITY; FIBROBLAST; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN METABOLISM;

ALZHEIMER DISEASE; ANIMALS; CATHEPSIN B; CATHEPSINS; CELLS, CULTURED; CYSTEINE ENDOPEPTIDASES; HUMANS; LIVER; RATS; TRANSKETOLASE;

EID: 0030788993     PISSN: 00219541     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-4652(199707)172:1<63::AID-JCP7>3.0.CO;2-B     Document Type: Article

References (37)

1. Anastasi, A., Brown, M.A., Kembhavi, A.A., Nicklin, M.J.H., Sayers, C.A., Sunter, D.C., and Barrett, A.J. (1983) Cystatin, a protein inhibitor of cysteine proteinases. Biochem. J., 211:129-138.
2. Bajkoswki, A.S., and Frankfater, A. (1975) Specific spectrophotometric assays for cathepsin B1. Anal. Biochem., 68:119-127.
3. Banner, C.D.B., and Nixon, R.A., eds. (1992) Proteases and Protease Inhibitors in Alzheimer's Disease Pathogenesis. The New York Academy of Sciences, New York, Vol. 674, pp. 1-252.
4. Barrett, A.J. (1987) The cystatins: A new class of peptidase inhibitors. Trends Biochem. Sci., 12:193-196.
5. Barrett, A.J., and Kirschke, H. (1981) Cathepsin B, cathepsin H, and cathepsin L. Proteolytic enzymes, part C. In: Methods in Enzymology. L. Lorand, ed. Academic Press Inc., New York, Vol. 80, pp. 535-561.
6. Barrett, A.J., Kembhavi, A.A., Brown, M.A., Kirschke, H., Knight, C.G., Tamai, M., and Hanada, K. (1982) L-trans-epoxy-succinylleucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L. Biochem. J., 201:189-198.
7. Blessed, G., Tomlinson, B.E., and Roth, M. (1968) The association between quantitative measures of dementia and senile change in the cerebral grey matter of elderly subjects. Br. J. Psychiatry, 114:797-811.
8. Bradford, M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72:248-254.
9. Cataldo, A.N., and Nixon, R.A. (1990) Enzymatically active lysosomal proteases are associated with amyloid deposits in Alzheimer brain. Proc. Natl. Acad. Sci. U. S. A., 87:3861-3865.
10. Esch, F.S., Keim, E.C., Beattie, R.W., Blacher, A.R., Culwell, T., Oltersdorf, D., McClure, D., and Ward, P. (1990) Cleavage of amyloid β-peptide during constitutive processing of its precursor. Science, 248:1122-1124.
11. Etcheberrigaray, R., Ito, E., Oka, K., Tofrl-Grehl, B., Gibson, G.E., and Alkon, D.L. (1993) Potassium channel dysfunction in fibroblasts identifies patients with Alzheimer disease. Proc. Natl. Acad. Sci. U. S. A., 90:8209-8213.
12. Haass, C., Koo, E.H., Mellon, A., Hung, A.Y., and Selkoe, D.J. (1992) Targeting of cell-surface β-amyloid precursor protein to lysosomes: Alternative processing into amyloid-bearing fragments. Nature, 357-500-503.
13. Hasilik, A., and von Figura, K. (1984) Processing of lysosomal enzymes in fibroblasts. In: Lysosomes in Biology and Pathology. J.T. Dingle, R.T. Dean, and W.S. Sly, eds. Elsevier Scientific Publishing Co., Amsterdam, Vol. 7, pp. 3-16.
14. Horecker, B.L., and Smyrniotis, P.Z. (1953) The coenzyme function of thiamine pyrophosphate in pentose phosphate metabolism. J. Am. Chem. Soc., 75:1009-1010.
15. Horecker, B.L., Gibbs, M., Klenow, H., and Smyrniotis, P.Z. (1954) The mechanism of pentose phosphate conversion to hexose mono phosphate. I. With a rat liver enzyme preparation. J. Biol. Chem., 207:393-403.
16. Kay, D.W.K. (1991) The epidemiology of dementia: A review of recent work. Rev. Clin. Geront., 1:55-66.
17. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriphage T4. Nature, 227:680-685.
18. Lemere, C.A., Munger, J.S., Shi, G.-P., Natkin, L., Haass, C., Chapman, H.A., and Selkoe, D.J. (1995) The lysosomal cystein protease, cathepsin S, is increased in Alzheimer's disease and Down syndrome brain. Am. J. Pathol., 146:848-860.
19. McKhann, G., Drachman, D., Folstein, M., Katzman, R., Price, D., and Stadlan, E.M. (1984) Clinical diagnosis of Alzheimer's disease: Report of the NINCDS-ADRDA Work Group under the auspices of Department of Health and Human Services Task Force on Alzheimer's disease. Neurology, 34:939-944.
20. Mocali, A., and Paoletti F. (1989) Transketolase from human leukocytes. Isolation, properties and induction of polyclonal antibodies. Eur. J. Biochem., 180:213-219.
21. Munger, J.S., Haass, C., Lemere, C.A., Shi, G.-P., Wong, W.S.F., Teplow, D.B., Selkoe, D.J., and Chapman, H.A. (1995) Lysosomal processing of amyloid precursor protein to β-peptides: A distinct role for cathepsin S. Biochem. J., 311:299-305.
22. Murachi, T. (1983) Calpain and calpastatin. Trends Biochem. Sci., 8:167-169.
23. Paoletti, F. (1983) Purification and properties of transketolase from fresh rat liver. Arch. Biochem. Biophys., 222:489-496.
24. Paoletti, F., and Mocali, A. (1991) Enhanced proteolytic activities in cultured fibroblasts of Alzheimer patients are revealed by peculiar transketolase alterations. J. Neurol. Sci., 105:211-216.
25. Paoletti, F., Mocali, A., Marchi, M., Sorbi, S., and Piacentini, S. (1990) Occurrence of transketolase abnormalities in extracts of foreskin fibroblasts from patients with Alzheimer's disease. Biochem. Biophys. Res. Commun., 172:396-401.
26. Pharmacia Fine Chemicals (1974) Activated Thiol-Sepharose 4B. Bromma, Sweden.
27. Price, D.L. (1986) New perspectives on Alzheimer s disease. Annu. Rev. Neurosci., 9:489-512.
28. Sasaki T. (1990) Inhibitory effect of di- and tripeptidyl aldehydes on calpains and cathepsins. J. Enzym. Inhib., 3:195-201.
29. Scott, R.B. (1993) Extraneuronal manifestations of Alzheimer's disease. J. Am. Geriatr. Soc., 41:268-276.
30. Selkoe, D.J. (1989a) Biochemistry of altered brain protein in Alzheimer's disease. Annu. Rev. Neurosci., 12:463-490.
31. Selkoe, D.J. (1989b) Amyloid β-protein precursor in the pathogenesis of Alzheimer's disease. Cell, 58:611-612.
32. Sisodia, S.S., Koo, E.H., Beyreuther, K., Unterbeck A., and Price, D.L. (1990) Evidence that β-amyloid protein in Alzheimer's disease is not derived by normal processing. Science, 248:492-495.
33. Terry, R.D. (1963) The fine structure of neurofibrillary tangles in Alzheimer's disease. J. Neuropathol. Exp. Neurol., 22:629-641.
34. Tombaccini, D., Mocali, A., and Paoletti, F. (1994) Characteristic transketolase alteration in dermal fibroblatsts of Alzheimer patients are modulated by culture conditions. Exp. Mol. Pathol., 60:140-146.
35. Wilcox, D., and Mason, R.W. (1992) Inhibition of cysteine proteinases in lysosomes and whole cells. Biochem. J., 285:495-502.
36. Willnow, P. (1984) Fructose-1,6-bisphosphate aldolase In: Methods in Enzymatic Analysis. H.U. Bergmeyer, ed. VCH Verlag Chemie GmbH, Weinheim, Vol. 4, 3rd ed., pp. 346-353.
37. Zhang, H., Sternberger, N., Rubinstein, L.J., Herman, M.M., Binder, L.I., and Sternberger, L.A. (1989) Abnormal processing of multiple proteins in Alzheimer disease. Proc. Natl. Acad. Sci. U. S. A., 86:8045-8049.