德国科学家报告称，绿茶提取物（Epigallocatechin Gallate）可以减缓体内蛋白质积累,防止亨廷顿氏症的发生。
越来越多的科学家认为绿茶对人体有益。习惯饮用绿茶的人，得癌症的风险较低。绿茶能够起到有效的减肥作用，防止老年痴呆。
亨廷顿疾病，痴呆证和柏金森疾病等都属于神经性疾病，是由蛋白质突变导致的。这种不治之症与遗传有关。在15，000人当中大约有一人患有此症。德国目前已知患者约有8000位。英国提供的患者数目大约是5000人，美国为3万人。
这种疾病的特征是走路颠簸，平衡力差，步伐不稳。俗称亨廷顿夜盲症。
1993年，科学家发现了揭开蛋白质突变密码的基因，即亨廷顿蛋白质.。这一蛋白质一旦变异，便会拉长蛋白质链,使整个亨廷顿蛋白质失去正常结构。这些突变蛋白质人体无法处理，积聚在患者的大脑中，最终导致脑神经细胞中毒。
这项新研究是由中心分子医学柏林委员会的Max Delbrück中心的Erich Wanker教授发起的。根据对绿茶提取物（epigallocatechin gallate ）的综合分析发现，绿茶提取物会影响蛋白质表面的早期活动。
这项研究刊登在九月份的《人类分子遗传学》(第15部分，2743年至2751年)。由Dagmar Ehrnhoefer于本周在名为“神经退化疾病，功能基因的分子机制框架”的国际会议上提出。
“我们证明绿茶提取物有效地阻止亨廷顿蛋白质突变的产生，”Dagmar Ehrnhoefer称。
Wanker教授的实验小组进行的实验表明，绿茶提取物能够抑制亨廷顿蛋白质的表层活动，并利用果蝇基因有力的遏制蛋白质突变。后续的实验中还发现果蝇的感光和活动能力得到了改善。
Ehrnhoefer总结说：“研究结果表明绿茶提取物能够降低中介毒性。”
如果这种活性剂所需的保护可从绿茶或补充物中获得，那么，进一步的研究则显得非常必要。越来越多的研究报告提到绿茶及其提取物的益处。
绿茶中氧化剂浓度据说比红茶多出四倍（红茶是被氧化，发酵过的绿茶）。
消费者不断的意识到绿茶及其提取物的益处，相关的研究论文也不断的出现，有关报告儿茶酸的研究论文，从2000年的430篇增加到2003年的1500篇。
在欧洲，茶需求量不断增长，2003年已达500公吨。DSM公司声称拥有95%纯度的绿茶提取物，Taiyo International则拥有90%以后纯度，两家欧洲茶主要采购商在儿茶酚市场上双足鼎立。
英文原文：
Green Tea Slows Down Plaque Formation in Huntington's Disease - First Results in Model Organisms
Green tea can apparently inhibit the formation of the lethal protein aggregates that are a characteristic feature of Huntington's disease (HD). This finding was reported by Dagmar E. Ehrnhoefer, a member of the research group of Dr. Erich Wanker of the Max Delbrück Center for Molecular Medicine Berlin-Buch (MDC), Germany, at the international conference "Neurodegenerative Diseases: Molecular Mechanisms in a Functional Genomics Framework" in Berlin.
She was able to show in an in vitro experiment that the substance epigallocatechin-3-gallate (EGCG), extracted from green tea, interferes with very early events in the aggregation process of the mutant huntingtin protein. Cytoxicity is also reduced.
Moreover, the mobile function of transgenic flies carrying the Huntington's gene improved when they were fed the green tea substance.
The journal Human Molecular Genetics* has now published these research findings (Vol. 15, Nr. 18, 15. September 2006, pp. 2743-2751; advanced online access on August 7, 2006).
Dr. Wanker, who is also a professor at the Charité - Universitätsmedizin Berlin, and his colleagues hope that these findings can be a starting point for the development of a medical treatment for Huntington's disease and related diseases.
Huntington's disease, along with Alzheimer's and Parkinson's, belong to the family of neurodegenerative diseases caused by protein misfolding.
Jerky, uncontrolled movements, an unsteady gait and grimaces have given Huntington's disease (HD) its original common name that is still in use today: Huntington's chorea (Old Greek for "dance").
"Huntington's" in the name goes back to the American doctor George Huntington, who became the first to publish a detailed description of the disease in 1872.
The incurable disease is hereditary and has a prevalence of 1 in every 15,000 persons. In Germany, about 8,000 cases are currently known whereas in the US, 30,000 people have HD.
If a child inherits a mutated Huntington's gene from one affected parent, the disease inevitably develops, usually between the ages of 30 and 50. As a result, the nerve cells progressively degenerate in the areas of the brain that control movement and that are involved in memory and emotions. Ten to 30 years after the onset of the disease, Huntington's chorea leads to death.
In 1993, scientists discovered the gene that encodes the protein huntingtin. A mutation in this protein causes the disease and results in the aggregation of the mutant huntingtin protein within the cell nuclei of brain neurons.
In 1997, Dr. Wanker was able to demonstrate that these deposits or aggregates consist of misfolded huntingtin molecules. In the protein factories of the nerve cells of people with Huntington's disease, too many glutamine building blocks have been inserted into the amino acid sequence of huntingtin.
Due to the elongated polyglutamine chains which are formed, the protein loses its normal structure and can no longer be disposed of. Scientists hypothesize that these protein aggregates are toxic to nerve cells.
According to the findings of Dagmar Ehrnhoefer and Dr. Wanker, however, the substance epigallocatechin-3-gallate (EGCG) extracted from green tea slows down this aggregation process.
The research group hopes that these findings will be the starting point for developing a novel drug treatment for HD and related diseases in which misfolded proteins occur.
At the four-day conference, which began in Berlin-Buch on September 6th, around 200 genome researchers and clinicians from Canada, Europe, Japan, and the US discuss the latest findings on neurodegenerative diseases achieved with the aid of gene and protein research.
The organizers of the conference under the umbrella of the National Genome Research Network (NGFN), which is sponsored by the German Federal Ministry for Education and Research, were the MDC, the Charité - University Medical School, and the University of Bonn.
