Proteomics and transcriptome analysis coupled with pharmacological test reveals the diversity of anti-thrombosis proteins from the medicinal insect, Eupolyphaga sinensis
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Updated: May 21, 2026

Affinity Purification of a Fibrinolytic Enzyme from Sipunculus nudus
Published on: June 2, 2023
Ying Wang1, Hongli Yan, Yipeng Wang
1Key Laboratory of Animal Models and Human Disease Mechanisms, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming, Yunnan 650223, China.
Abstract:
The insect of Eupolyphaga sinensis Walker has been used as traditional anti-thrombosis medicine without bleeding risk for several hundreds years in eastern countries. Our previous work has identified a bi-functional anti-thrombosis protein containing both direct-acting fibrin(ogen)olytic and plasminogen-activating activities from the insect. By proteomics and transcriptome analysis, 105 serine proteases belonging to four families were identified from the ground beetle, E. sinensis and the classification is for serine proteases of this organism. Pharmacological test indicated that 5 (eupolytin 1-5) of them have the abilities to hydrolyze fibrin(ogen) and/or activate plasminogen. The current work revealed the extreme diversity of anti-thrombosis components in E. sinensis and anti-thrombosis molecular mechanisms of the traditional medicinal insect, and provided many templates for the development of new thrombolytic agents. Especially, these proteins, which contain both plasmin- and PA (plasminogen-activating)-like activities, are excellent candidates for anti-thrombosis medicines.
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