Enhancement of MTT, a tetrazolium salt, exocytosis by amyloid β- protein and chloroquine in cultured rat astrocytes

Neuroscience Letters

Volumn 266, Issue 2, 1999, Pages 129-132

  Isobe, Ichiro ^a   Michikawa, Makoto ^a   Yanagisawa, Katsuhiko ^a  

^a NATIONAL CENTER FOR GERIATRICS AND GERONTOLOGY   (Japan)

Author keywords

amyloid; 3 (4,5 dimethylthiazol 2 yl) 2,5 diphenyltetrazolium bromide; Alzheimer's disease; Astrocyte; Chloroquine

Indexed keywords

AMYLOID BETA PROTEIN; BAFILOMYCIN A1; CHLOROQUINE; TETRAZOLIUM;

ALZHEIMER DISEASE; ANIMAL CELL; ARTICLE; ASTROCYTE; DEGENERATIVE DISEASE; EXOCYTOSIS; NERVE CELL CULTURE; NEUROLOGIC DISEASE; NONHUMAN; PRIORITY JOURNAL; RAT;

AMYLOID BETA-PROTEIN; ANIMALS; ASTROCYTES; CELLS, CULTURED; CHLOROQUINE; COLORING AGENTS; EXOCYTOSIS; RATS; RATS, SPRAGUE-DAWLEY; TETRAZOLIUM SALTS; THIAZOLES;

EID: 0033532236     PISSN: 03043940     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0304-3940(99)00282-7     Document Type: Article

References (16)

1. Abe K., Saito H. Amyloid β protein inhibits cellular MTT reduction not by suppression of mitochondrial succinate dehydrogenase but by acceleration of MTT formazan exocytosis in cultured rat cortical astrocytes. Neurosci. Res. 31:1998;295-305.
2. Cataldo A.M., Hamilton D.J., Barnett J.L., Paskevich P.A., Nixon R.A. Properties of the endosomal-lysosomal system in the human central nervous system: disturbances mark most neurons in populations at risk to degenerate in Alzheimer's disease. J. Neurosci. 16:1996;186-199.
3. Claus V., Jahraus A., Tjelle T., Berg T., Kirschke H., Faulstich H., Griffiths G. Lysosomal enzyme trafficking between phagosomes, endosomes, and lysosomes in J774 macrophages. Enrichment of cathepsin H in early endosomes. J. Biol. Chem. 273:1998;9842-9851.
4. Ishiyama M., Miyazono Y., Sasamoto K. A highly water-soluble disulfonated tetrazolium salt as a chromogenic indicator for NADH as well as cell viability. Talanta. 44:1997;1299-1305.
5. Johnson L.S., Dunn K.W., Pytowski B., McGraw T.E. Endosome acidification and receptor trafficking: bafilomycin A1slows receptorexternalization by a mechanism involving the receptor's internalization motif. Mol. Biol. Cell. 4:1993;1251-1266.
6. Kato M., Saito H., Abe K. Nanomolar amyloid β protein-induced inhibition of cellular redox activity in cultured astrocytes. J. Neurochem. 68:1997;1889-1895.
7. Lippincott-Schwartz J., Fambrough D.M. Cycling of the integral membrane glycoprotein, LEP100, between plasma membrane and lysosomes: kinetic and morphological analysis. Cell. 49:1987;669-677.
8. Liu Y., Schubert D. Cytotoxic amyloid peptides inhibit cellular 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) reduction by enhancing MTT formazan exocytosis. J. Neurochem. 69:1997;2285-2293.
9. Liu Y., Peterson D.A., Kimura H., Schubert D. Mechanism of cellular 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) reduction. J. Neurochem. 69:1997;581-593.
10. Mosmann M.P. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J. Immunol. Methods. 65:1983;55-63.
11. Murakami N., Ihara Y., Nonaka I. Chloroquine treated rat: a possible model for Alzheimer's disease. Muscle Nerve. 18:1995;123-125.
12. Roher B.A., Gray E.G., Paula-Barbosa M. Alzheimer's disease: coated vesicles, coated pits and the amyloid-related cell. Proc. R. Soc. Lond. 232:1988;367-373.
13. Shearman M.S., Hawtin S.R., Tailor V.J. The intracellular component of cellular 3-(4,5-dimethylthiazol-2-yl)-2, 5-diphenyltetrazolium bromide (MTT) reduction is specifically inhibited by β-amyloid peptides. J. Neurochem. 65:1995;218-227.
14. Shearman M.S., Ragan C.I., Iversen L.L. Inhibition of PC12 cell redox activity is a specific, early indicator of the mechanism of β-amyloid-mediated cell death. Proc. Natl. Acad. Sci. USA. 91:1994;1470-1474.
15. Tsuzuki K., Fukatu R., Takamaru Y., Yoshida T., Mafune N., Kobayashi K., Fujii N., Takahata N. Co-localization of amyloid-associated proteins with amyloid beta in rat soleus muscle in chloroquine-induced myopathy: a possible model for amyloid β formation in Alzheimer's disease. Brain. Res. 699:1995;260-265.
16. Yang A.J., Chandswangbhuvana D., Margol L., Glabe C.G. Loss of endosomal/lysosomal membrane impermeability is an early event in amyloid Aβ1-42 pathogenesis. J. Neurosci. Res. 52:1998;691-698.