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Cell:阿尔茨海默氏症研究获进展

2012-04-10 Kun Ping Lu 《细胞》

近日,来自哈佛医学院柏斯以色列狄肯尼斯医学中心(BIDMC)的研究人员领导的一个研究小组近日在新研究中开发出了一种新型抗体技术,利用这一技术识别了阿尔茨海默氏症的早期致病Tau蛋白。这一成果提高了在疾病早期阶段采用免疫治疗策略的可能性。相关研究论文发布在3月30日的Cell杂志上。 领导这一研究的是美国哈佛大学医学院的卢坤平(Kun Ping Lu)教授和周震晓(Xiao Zhen Zhou)教

近日,来自哈佛医学院柏斯以色列狄肯尼斯医学中心(BIDMC)的研究人员领导的一个研究小组近日在新研究中开发出了一种新型抗体技术,利用这一技术识别了阿尔茨海默氏症的早期致病Tau蛋白。这一成果提高了在疾病早期阶段采用免疫治疗策略的可能性。相关研究论文发布在3月30日的Cell杂志上。

领导这一研究的是美国哈佛大学医学院的卢坤平(Kun Ping Lu)教授和周震晓(Xiao Zhen Zhou)教授。卢坤平现任美国哈佛大学医学院医学系教授。其课题组的主要研究方向是阐明细胞周期和端粒维持的分子机制,并确定这些机制中的变异与癌症及早老性痴呆的联系。近年来在医学科学研究方面取得了卓越的成就,发表50多篇富有创见的文章,其中7篇发表在Nature杂志上,2篇发表在Science杂志上,4篇发表在Cell杂志上。

阿尔茨海默氏症是最常见的一种老年性痴呆病,当前在美国约有540万人罹患此病,全球有3000万人受累。随着生育高峰期出生的一代逐渐衰老,预期寿命继续延长,这些数字预计还将显著增长。有人预计到2050年,全世界将会有1.2亿人受累于此病,单美国预期花费就将超过1万亿美元。目前对于这一疾病尚无有效的治疗方法。

正常情况下,tau蛋白具有诱导与促进微管蛋白聚合成微管,防止微管解聚、维持微管功能的稳定的功能。对记忆和正常大脑功能起重要的作用。然而,近年来越来越多的研究证实在阿尔茨海默氏症和其他神经退行性疾病中,tau蛋白不仅不再发挥正常功能,还会转变为破坏脑细胞的“恶棍”因子。

卢坤平教授说:“因为阿尔茨海默氏症从发生到发展至少需要10年的时间,因此终止记忆丧失最重要的环节就是要找到疾病初始阶段tau蛋白由‘好’变‘坏’的关键时机。通过开发这项创新技术生成抗体,我们发现了一条可以特异地除去致病性tau,而不损害正常tau使其继续执行重要职责的新策略。”

在这篇文章中,BIDMC的科学家们开发出了一种新型抗体技术,清除地区分了两种tau亚型,其中一种是健康tau,另一种是致病tau。并证实在疾病极早期的阿尔茨海默氏症患者神经元中可找到这种致病性tau。这些研究发现提高了开发出仅靶向致病性tau,可用于诊断、治疗、甚至预防疾病发生的抗体和疫苗的可能。

萨克研究所的Tony Hunter博士评价这一研究说:“卢坤平和他的同事开发了一个非常聪明的策略生成了抗两种不同的磷酸化tau亚型的特异性抗体。他们的研究表明这两种tau亚型中只有一种是阿尔茨海默氏症的致病原因,这些新型抗体也有可能进一步被开发用于治疗。而利用这些新抗体分析脑脊髓液为早期诊断阿尔茨海默氏症及预测疾病严重程度带来的极大的希望。”(生物谷Bioon.com)

doi:10.1016/j.cell.2012.02.016
PMC:
PMID:

Proline Isomer-Specific Antibodies Reveal the Early Pathogenic Tau Conformation in Alzheimer"s Disease

Kazuhiro Nakamura, Alex Greenwood, Lester Binder, Eileen H. Bigio, Sarah Denial, Linda Nicholson, Xiao Zhen Zhou, Kun Ping Lu

cis-trans isomerization of proteins phosphorylated by proline-directed kinases is proposed to control numerous signaling molecules and is implicated in the pathogenesis of Alzheimer's and other diseases. However, there is no direct evidence for the existence of cis-trans protein isomers in vivo or for their conformation-specific function or regulation. Here we develop peptide chemistries that allow the generation ofcis- and trans-specific antibodies and use them to raise antibodies specific for isomers of phosphorylated tau. cis, but not trans, p-tau appears early in the brains of humans with mild cognitive impairment, accumulates exclusively in degenerated neurons, and localizes to dystrophic neurites during Alzheimer's progression. Unlike trans p-tau, the cis isomer cannot promote microtubule assembly, is more resistant to dephosphorylation and degradation, and is more prone to aggregation. Pin1 converts cis to trans p-tau to prevent Alzheimer's tau pathology. Isomer-specific antibodies and vaccines may therefore have value for the early diagnosis and treatment of Alzheimer's disease.

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    2012-09-29 维他命
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