bp(MESH:Autophagy)
to a(HBP:"Tau aggregates")
Stimulating autophagy either through serum withdrawal or rapamycin treatment in SH-SY5Y cells overexpressing P301L tau that had been induced to aggregate led to substantial reduction in aggregates that was prevented by 3-MA (70).
bp(MESH:Autophagy) decreases a(HBP:"Tau aggregates")
32e5888006
This is supported by evidence that full-length tau, which has a lower propensity for aggregating, is cleared by the proteasome while caspase- cleaved tau, which is more aggregate prone, goes through autophagy (72). Also, aggregated tau can be cleared by inducing autophagy (70, 96).
bp(MESH:Autophagy) increases deg(a(HBP:"Tau aggregates"))
19829e0630
Soluble, monomeric tau is an ideal proteasomal substrate. Indeed, it has been clearly demonstrated that tau can be degraded by the proteasome (65–67, 73). It thus can be suggested that under physiologic circumstances much of tau is degraded in this manner, with select modified forms being cleared by autophagy.However, within the context of the AD milieu, additional tau modifications and degradative impairments may cause the balance to shift away from proteasomal degradation toward autophagy.
bp(MESH:Autophagy) increases deg(a(HBP:"Tau aggregates"))
e4543d37d9
For example, as discussed above, certain modified forms of tau, such as caspase-cleaved tau, have a stronger tendency to aggregate. As tau begins to assemble into oligomers, it may become increasingly undesirable as a proteasomal substrate. These low-order, soluble oligomers may be preferentially degraded by autophagy.
bp(MESH:Autophagy) increases deg(a(HBP:"Tau aggregates"))
d5a9090147
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