Journal
JOURNAL OF PHARMACOLOGICAL SCIENCES
Volume 113, Issue 3, Pages 285-288Publisher
JAPANESE PHARMACOLOGICAL SOC
DOI: 10.1254/jphs.10118SC
Keywords
HRD1; endoplasmic reticulum-associated degradation (ERAD); amyloid-beta
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Funding
- Ministry of Education, Culture, Sports, Science, and Technology, Japan [21790089, 21300142, 20659013]
- Grants-in-Aid for Scientific Research [20659013, 21790089, 21300142] Funding Source: KAKEN
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Endoplasmic reticulum-associated degradation (ERAD) is a quality control mechanism in which unfolded proteins are retro-translocated to the cytosol for degradation. Our recent study showed that suppression of expression of ubiquitin ligase HRD1, which is involved in ERAD, caused amyloid precursor protein (APP) accumulation and amyloid-beta (A beta) production. Furthermore, HRD1 protein levels were significantly lower in the cerebral cortex of Alzheimer's disease (AD) patients. To assess whether HRD1 is involved in AD pathology, we analyzed the relationship between HRD1 protein levels and A beta production. We found that the HRD1 level was negatively correlated with the A beta level, suggesting the possible involvement of HRD1 in A beta generation.
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