Correlation Between Decrease in Protein Levels of Ubiquitin Ligase HRD1 and Amyloid-β Production

被引:22
|
作者
Saito, Ryo [1 ]
Kaneko, Masayuki [1 ]
Okuma, Yasunobu [1 ]
Nomura, Yasuyuki [2 ]
机构
[1] Chiba Inst Sci, Fac Pharmaceut Sci, Dept Pharmacol, Chiba 2880025, Japan
[2] Yokohama Coll Pharm, Lab Pharmacotherapeut, Yokohama, Kanagawa 2450066, Japan
关键词
HRD1; endoplasmic reticulum-associated degradation (ERAD); amyloid-beta; ENDOPLASMIC-RETICULUM STRESS; DEGRADATION; PARKIN; TRANSMEMBRANE; ACCUMULATION; SUBSTRATE; DISEASE; GENES;
D O I
10.1254/jphs.10118SC
中图分类号
R9 [药学];
学科分类号
1007 ;
摘要
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.
引用
收藏
页码:285 / 288
页数:4
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