Matrix metalloproteinase profile in patients with Creuztfeldt-Jakob disease

International Journal of Clinical Practice

Volumn 57, Issue 6, 2003, Pages 475-478

  Kettlun, A ^a   Collados, L ^a   Garcia L ^a   Cartier, L A ^b   Wolf, M E ^c   Mosnaim, A D ^d   Valenzuela, M Antonieta ^a  

^a UNIVERSITY OF CHILE   (Chile)

^b UNIVERSITY OF CHILE   (Chile)

^c International Neuropsychiatry Consultants   (United States)

^d ROSALIND FRANKLIN UNIVERSITY OF MEDICINE AND SCIENCE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GELATINASE A; GELATINASE B; MATRIX METALLOPROTEINASE; MATRIX METALLOPROTEINASE INHIBITOR; PRION PROTEIN; STROMELYSIN;

ADULT; AGED; ARTICLE; CEREBROSPINAL FLUID; CLINICAL ARTICLE; CONTROLLED STUDY; CORRELATION COEFFICIENT; CREUTZFELDT JAKOB DISEASE; ENZYME ACTIVITY; FEMALE; HUMAN; IMMUNOBLOTTING; MALE; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN CEREBROSPINAL FLUID LEVEL; STATISTICAL SIGNIFICANCE; ZYMOGRAPHY;

14-3-3 PROTEINS; ADULT; AGED; CASE-CONTROL STUDIES; CREUTZFELDT-JAKOB SYNDROME; FEMALE; HUMANS; MALE; MATRIX METALLOPROTEINASES; MIDDLE AGED; TISSUE INHIBITOR OF METALLOPROTEINASES; TYROSINE 3-MONOOXYGENASE;

EID: 0043065378     PISSN: 13685031     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (23)

1. Brown P, Galvez S, Goldfarb LG et al. Familial Creutzfeldt-Jakob disease in Chile is associated with the codon 200 mutation of the PRNP amyloid precursor gene on chromosome 20. J Neurol Sci 1992; 112: 65-67.
2. Cartier L. Epidemiology of Creutzfeldt-Jakob in Chile. Bol Acad Chilena Med 1999; 36: 10-16.
3. Goldfarb LG, Brown P, Mitrova E et al. Creutzfeldt-Jakob disease (spongiform encephalopathy) associated with the PRNP codon 200 Lys mutation: an analysis of 45 families. Eur J Epidemiol 1991; 7: 477-486.
4. Gibbs CJ Jr, Gajdusek DC, Asher DM et al. Creutzfeldt-Jakob disease (spongiform encephalopathy): transmission to the chimpanzee. Science 1968; 161: 388-389.
5. Will RG, Ironside JW, Zeidler M et al. A new variant of Creutzfeld-Jakob disease in the UK. Lancet 996; 347: 921-925.
6. Prusiner SB. Prion diseases and the BSE crisis. Science 1977; 278: 245-251.
7. Prusiner SB. Prions. Proc Natl Acad Sci USA 1998; 95: 13363-13383.
8. Johnson RT, Gibbs CJ Jr. Creutzfeldt-Jakob disease and related transmissible spongiform encephalopathies. N Engl J Med 1998; 339: 1994-2004.
9. Collinge J. Prion diseases of human and animals: their causes and molecular basis. Ann Rev Neurosci 2001; 24: 519-550.
10. Valenzuela MA, Cartier L, Collados L et al. Gelatinase activity of matrix metalloproteinases in the cerebrospinal fluid of various patient populations. Res Comm Molec Pathol Pharmacol 1999; 104: 42-52.
11. Hsich G, Kenney K, Gibbs CJ Jr et al. The 14-3-3 brain protein in cerebrospinal fluid as a marker for transmissible spongiform encephalopathies. N Engl J Med 1996; 335: 924-930.
12. Soto C. Protein misfolding and disease; protein refolding and therapy. FEBS Letter 2001; 498: 204-207.
13. Galvez S, Masters C, Gajdusek C. Descriptive epidemiology of Creutzfeldt-Jakob disease in Chile. Arch Neurol 1980; 37: 11-14.
14. Kolb SA, Lahrtz F, Paul R et al. Matrix metalloproteinases and tissue inhibitors of metalloproteinases in viral meningitis: upregulation of MMP-9 and TIMP-1 in cerebrospinal fluid. J Neuroimmunol 1998; 84: 143-150.
15. Rosenberg GA, Dencoff JE, Correa N Jr et al. Effect of steroids on CSF matrix metalloproteinases in multiple sclerosis: relation to blood-brain barrier injury. Neurology 1996; 46: 11626-1632.
16. Leppert D, Ford J, Stabler G et al. Matrix metalloproteinsase-9 (gelatinase B) is selectively elevated in CSF during relapses and stable phases of multiple sclerosis. Brain 1998; 121: 2327-2334.
17. Valenzuela MA, Collados L, Kettlun AM et al. Increased activity of matrix metalloproteinases and their tissue inhibitors in cerebrospinal fluid of patients with HTLV-1 associated tropical spastic paraparesis. Rev Med Chile 2000; 128: 585-592.
18. Gomez DE, Alonso DF, Yoshiji H et al. Tissue inhibitors of metalloproteinases: structure, regulation and biological functions. Eur J Cell Biol 1997; 74: 111-122.
19. DeArmond SJ, Mobley WC, DeMott DL et al. Changes in the localization of brain prion proteins during scrapie infection. Neurology 1987; 37: 1271-1280.
20. Sabono GP, Soto C, Kascsak RJ et al. Cell-lysate conversion of prion protein into its protease-resistant isoform suggests the participation of a cellular chaperone. Biochem Biophys Res Commun 1999; 258: 470-475.
21. Jimenez-Hueste A, Lievens PMJ, Vidal R et al. Endogenous proteolytic cleavage of normal and disease-associated isoforms of the human prion protein in neural and non-neural tissues. Am J Pathol 1998; 153: 1561-1572.
22. Beaudry P, Cohen JP, Brandel N et al. 14-3-protein, neuron-specific enolase, and S-100 protein in cerebrospinal fluid of patients with Creutzfeldt-Jakob disease. Dement Geriatr Cogn Disord 1999; 10: 40-46.
23. Choe L, Green A, Knight RS et al. Apolipoprotein E and other cerebrospinal fluid proteins differentiate ante mortem variant Creutzfeldt-Jakob disease from ante mortem sporadic Creutzfeldt-Jakob disease. Electrophoresis 2002; 23: 2242-2246.