【摘 要】
：
Misfolded proteins,and the associated endoplasmic reticulum (ER) stress,are emerging as hallmarks of age-and neurodegeneration-related disorders such as Huntingtons disease (HD),Alzheimers disease (AD
【机 构】
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Department of Chemistry at University of Texas-El Paso USA
【出 处】
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2008中国深圳蛋白质和多肽科学大会
论文部分内容阅读
Misfolded proteins,and the associated endoplasmic reticulum (ER) stress,are emerging as hallmarks of age-and neurodegeneration-related disorders such as Huntingtons disease (HD),Alzheimers disease (AD),Parkinsons disease (PD) and Amyotrophic Lateral Sclerosis (ALS).Recent and compelling evidence has linked nitrosative stress and resulting S-nitrosylation of the ER-resident oxidoreductase,protein disulfide isomerase (PDI),to the pathogenesis of PD and AD.Over-expression of PDI has been found to reduce the formation of polyubiquitinated proteins,making PDI an important target for therapeutic intervention in PD,AD and other age-and neurodegeneration-related disorders.Our laboratory has demonstrated that the biphenolic phytochemicals curcumin and masoprocol possess NO-scavenging ability.Furthermore,our data indicate that both polyphenols intervene in S-nitrosylation of PDI by a model NO-donor and rescue the oxidoreductase from lethal nitrosative damage.I.e.,catalytic activity of PDI is retained in spite of high nitrosative stress.Importantly,both etlmopharmaceuticals and their nitrated derivatives accelerate oxidative regeneration of ER-processed proteins through novel non-redox mechanisms and prevent accumulation of cell debris.Their therapeutic potential in the prevention/mitigation of age-and neurodegeneration-related disorders is discussed.
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