Brefeldin A-induced apoptosis is expressed in rat neurons with dephosphorylated tau protein
Section snippets
Acknowledgements
We thank Mrs. Autef, Mrs. Teissandier and Mrs. Forestier for technical assistance and Conseil Regional du Limousin and AFM for support.
References (23)
- et al.
The presence of calbindin in neuron in cultures protects from oxidative stress
Brain Res.
(1996) - et al.
NMDA induces apoptosis and necrosis in neuronal cultures. Increased APP immunoreactivity is linked to apoptotic cells
Neurosci. Lett.
(1997) - et al.
Cultured neurons expressing phosphorylated tau are more resistant to apoptosis induced by NMDA or serum deprivation
Mol. Brain Res.
(1997) - et al.
Brefeldin A's effects on endosomes, lysosomes, and the TGN suggest a general mechanism for regulating organelle structure and membrane traffic
Cell
(1991) - et al.
Aberrant tau phosphorylation and neurite retraction during NGF deprivation in PC12 cells
Biochem. Biophys. Res. Commun.
(1997) Multiple targets for Brefeldin A
Cell
(1991)- et al.
Brefeldin A is a potent inducer of apoptosis in human cancer cells independently of p53
Exp. Cell Res.
(1996) - et al.
Apoptosis and necrosis: two distinct events induced, respectively, by mild and intense insults with N-methyl-D-aspartate or nitric oxide/superoxide in cortical cell cultures
Proc. Natl. Acad. Sci. USA,
(1995) - et al.
Neuronal localization of presenilin-1 and association with amyloid plaques and neurofibrillary tangles in Alzheimer's disease
J. Neurosci.
(1997) - et al.
Increased amyloid-β 42(43) in brains of mice expressing mutant presenilin 1
Nature
(1996)
Processing of the amyloid protein precursor to potentially amyloidogenic derivatives
Science
Cited by (23)
Lipopolysaccharide prevents apoptosis induced by brefeldin A, an endoplasmic reticulum stress agent, in RAW 264.7 cells
2006, Biochemical and Biophysical Research CommunicationsCitation Excerpt :Cycloheximide did not significantly influence the preventive effect of LPS, suggesting no requirement of newly synthesized proteins (data not shown). Since brefeldin A is known to cause cell death via apoptotic cell death [14–16], we examined whether LPS inhibited brefeldin A-induced cell death via apoptotic cell death or not. First, the effect of LPS on DNA fragmentation in brefeldin A-treated RAW 264.7 cells was examined (Fig. 3A).
Alzheimer's disease as a disorder of dynamic brain self-organization
2005, Progress in Brain ResearchCitation Excerpt :Furthermore, tau in its hyperphosphorylated, aggregated form (PHF-tau) might disturb neuronal viability by interfering with axonal transport. On the other hand, a moderate elevation of the expression and phosphorylation state of tau has been associated with neuroprotection against apoptotic cell death (Lesort et al., 1997; Nagy and Esiri, 1997; Arendt et al., 1998a; Esclaire et al., 1998; Mills et al., 1998; Yardin et al., 1998). Tau protein is more highly phosphorylated during mitosis (Pope et al., 1994; Preuss et al., 1995).
Neurodegeneration and plasticity
2004, International Journal of Developmental NeuroscienceCitation Excerpt :The present results, thus, support the suggestion that hyperphosphorylation of tau might reflect a protective mechanism in a unfavorable enviroment (Ihara, 2001). Recent studies investigating tau phosphorylation in relation to neuronal susceptibility for apoptosis have indeed suggested, that a modest increase in tau phosphorylation correlates with increased protection of neurons against cell death (Arendt et al., 1998b; Esclaire et al., 1998; Lesort et al., 1997; Mills et al., 1998; Nagy and Esiri, 1997; Yardin et al., 1998). Hyperphosphorylation might confer tau resistance to proteases and could, thus, be a mechanism to stabilize its structure.