Ko R C, Fan L
Department of Zoology, University of Hong Kong.
Parasitology. 1996 Jan;112 ( Pt 1):89-95. doi: 10.1017/s0031182000065112.
Heat shock proteins (HSPs) were documented for the first time in both somatic extracts and excretory/secretory (ES) products of the infective-stage larvae of Trichinella spiralis and T. pseudospiralis. Larvae recovered from muscles of infected mice were heat shocked at 37, 40, 43 and 45 degrees C in RPMI 1640 medium containing L(-)[35S]methionine. Somatic extracts and ES products of heat-shocked worms were then analysed by SDS-PAGE, autoradiography and laser densitometry. Prominent bands of HSPs were observed at 43 degrees C which is the optimal heat shock temperature. The major HSPs in somatic extracts of T. spiralis were 20, 47, 50, 70, 80 and 86 kDa. When the temperature was increased from 37 to 43 degrees C, the greatest increase in absorbance was observed in HSPs 70 and 86. In vitro translation of mRNA in a nuclease-treated rabbit reticulocyte lysate system showed an increase in the synthesis of the 80 kDa protein. This suggests that the production of HSP 80 is regulated at the transcriptional level. The major HSPs in the ES products were 11, 45, 53 and 64 kDa. In T. pseudospiralis, the major HSPs in the somatic extracts were 20, 26, 31, 50, 53, 70, 80 and 86 kDa, and in the ES products, 11, 35, 37, 41 and 64 kDa.
首次在旋毛虫和伪旋毛虫感染期幼虫的体细胞提取物以及排泄/分泌（ES）产物中记录到热休克蛋白（HSPs）。从感染小鼠肌肉中回收的幼虫在含有L(-)[35S]甲硫氨酸的RPMI 1640培养基中于37、40、43和45摄氏度进行热休克处理。然后通过SDS-PAGE、放射自显影和激光密度测定法对热休克蠕虫的体细胞提取物和ES产物进行分析。在43摄氏度（即最佳热休克温度）观察到明显的HSPs条带。旋毛虫体细胞提取物中的主要HSPs为20、47、50、70、80和86 kDa。当温度从37摄氏度升至43摄氏度时，HSPs 70和86的吸光度增加最大。在核酸酶处理的兔网织红细胞裂解物系统中对mRNA进行体外翻译显示80 kDa蛋白的合成增加。这表明HSP 80的产生在转录水平受到调控。ES产物中的主要HSPs为11、45、53和64 kDa。在伪旋毛虫中，体细胞提取物中的主要HSPs为20、26、31、50、53、70、80和86 kDa，而在ES产物中为11、35、37、41和64 kDa。
