Summary: The Unfolded Protein Response Is Activated In Alzheimer’S Disease
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Read the summary and the most important questions on The unfolded protein response is activated in Alzheimer’s disease
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1 Introduction
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How can AD be characterized at the protein level?
It is a disease characterized by the accumulation of misfolded proteins (b amyloid and p-tau) -
How is the unfolded protein response triggered?
By the sensing of unfolded proteins in the ER, through binding of BiP to the misfolded protein. -
To which structures is BiP bound under normal physiological circumstances?
- PERK
- ATF-6
- IRE-1
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What happens to the to BiP bound structures when BiP binds a misfolded protein?
BiP is released from PERK, ATF-6 and IRE-1 -
WHat are the consequences of the unfolded protein response in the short term?
- Reduction of translation (downregulation of eIF2a)
- Increased protein degradation
- Increased production of BiP
- Reduction of translation (downregulation of eIF2a)
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What may be the fate of cells under prolonged ER stress?
Cell apoptosis -
What makes the UPR relevant to AD?
In AD the current hypothesis is that both amyloid beta and p-tau (which are intracellular and extracellular misfolded proteins) are at the core of pathogenesis. deficient UPR may play a big role in the onset of AD. -
How was the UPR studied?
By BiP and PERK as markers for UPR activation. -
2 Material and Methods
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What kind of species were investigated?
Elderly humans with AD and elderly humans without AD AND dementia -
3 Results
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3.1 Expression levels of BiP/GRP78 are increased in AD temporal cortex and hippocampus
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What might be a pre-eliminary conclusion based on the results for BiP?
BiP expression is increased in higher stages of AD, this may indicate a relationship between BiP expression and AD progression.
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