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彭亨丝虫第三期幼虫小热休克蛋白的表达

Expression of small heat shock proteins by the third-stage larva of Brugia pahangi.

作者信息

Jecock R M, Devaney E

机构信息

Liverpool School of Tropical Medicine, UK.

出版信息

Mol Biochem Parasitol. 1992 Dec;56(2):219-26. doi: 10.1016/0166-6851(92)90171-f.

DOI:10.1016/0166-6851(92)90171-f
PMID:1484547
Abstract

Changes in proteins synthesised by the infective third-stage larvae (L3) of the filarial nematode Brugia pahangi were examined with respect to the temperature shift encountered by the parasite as it migrates from insect to mammal, and the presence of serum in the culture medium. While the synthesis of a number of polypeptides is regulated by the temperature shift of the L3 from 28 degrees C to 37 degrees C in vitro, there is no evidence that serum has any significant effect on protein synthesis. Two complexes of small acidic polypeptides (22-24 kDa and 18 kDa) are synthesised for a limited period only by L3 transferred to 37 degrees C. One component of each complex appears to be constitutively expressed at 28 degrees C, but its synthesis is up-regulated at 37 degrees C, while the remaining members of each complex are synthesised only at 37 degrees C. Subjection of L3 and post-infective (p.i.) L3 to heat shock (41 degrees C) also induces synthesis of both complexes, indicating that these heat-inducible polypeptides are related to the family of small heat shock proteins. The possible role of the heat shock-related proteins in this important environmental transition is considered.

摘要

针对丝状线虫彭亨布鲁线虫感染性第三期幼虫(L3)在从昆虫迁移至哺乳动物过程中所经历的温度变化以及培养基中血清的存在情况,对其合成的蛋白质变化进行了研究。虽然许多多肽的合成受L3在体外从28℃至37℃温度变化的调节,但没有证据表明血清对蛋白质合成有任何显著影响。仅在转移至37℃的L3中,两种小酸性多肽复合物(22 - 24 kDa和18 kDa)在有限时期内合成。每个复合物的一个组分似乎在28℃时组成性表达,但其合成在37℃时上调,而每个复合物的其余成员仅在37℃时合成。将L3和感染后(p.i.)的L3进行热休克处理(41℃)也会诱导这两种复合物的合成,表明这些热诱导多肽与小热休克蛋白家族有关。文中考虑了热休克相关蛋白在这一重要环境转变中的可能作用。

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