中文摘要：

Huntingtin (Htt ) 变化原因亨廷顿的疾病。 Httrevealed 的顺序分析在 Htt.In 顺序的N终端区域的一个可能的凝血酵素劈开地点如果凝血酵素能劈开 Htt ，调查，我们表示了N终端碎片( 1-969 )野类型( wt )在 MCF-7 房间的 Htt ( Htt1-969 )并且在 vitro.An 表示 plasmidpcDNA3-Htt-18Q-969 由凝血酵素学习了它的劈开模式习惯于 transfect MCF房间， Htt 1-969 表示被证实 withimmunofluorescence.Cell lysates 与凝血酵素被孵化( 1 U/ml ， 10 U/ml ，并且 30 U/ml )为 1 h 当面或 hirudin 的缺席，凝血酵素 inhibitor.Htt 碎裂被 sodiumdodecylsulfate-polyacrylamide 凝胶电泳(SDS页)分开并且与约 80 kDa 的分子的质量与 anti-Htt antibodies.AnHtt 碎片检测了在这 Htt 碎片的孵化 withthrombin.The 尺寸被分子的集体产生 调停fromthrombin 的劈开在氨基酸期望以后，被生产 183 在 80 kDa 的 Htt.Production 碎片被 hirudin.This 学习禁止提供 Htt 被凝血酵素在 vitroat 氨基酸 183 劈开的第一条证据。如果内长的凝血酵素在 vivo 劈开 Htt，生理的意义 Htt 的调停 ofthrombin 的劈开应该进一步被调查。

英文摘要：

Huntingtin （Htt） mutation causes Huntington＇s disease. Sequence analysis of Htt revealed a possible thrombin cleavage site in the N-terminal region of Htt. In order to investigate if thrombin can cleave Htt, we expressed the N-terminal fragment （1-969） of wild-type （wt） Htt （Htt 1-969） in MCF-7 cells and studied its cleavage pattern by thrombin in vitro. An expression plasmid pcDNA3-Htt-18Q-969 was used to transfect MCF-cells and Htt 1-969 expression was confirmed with immunofluorescence. Cell lysates were incubated with thrombin （1 U/ml, 10 U/ml, and 30 U/ml） for 1 h in the presence or absence of hirudin, a thrombin inhibitor. Htt fragments were separated by sodium dodecylsulfate-polyacrylamide gel electrophoresis （SDS-PAGE） and detected with anti-Htt antibodies. An Htt fragment with molecular mass of approximately 80 kDa was produced after incubation with thrombin. The size of this Htt fragment was anticipated by molecular mass generated from thrombin-mediated cleavage at the amino acid 183 in the Htt. Production of an 80 kDa fragment was inhibited by hirudin. This study provides the first evidence that Htt is cleaved by thrombin in vitro at amino acid 183. If endogenous thrombin cleaves Htt in vivo, the physiological significance of thrombin-mediated cleavage of Htt should be further investigated.