A facultative plasminogen-independent thrombolytic enzyme from Sipunculus nudus

M Mingqing Tang G Guoxing Ma C Chunyan Xu H Hui Yang H Hongjun Lin C Chao Bian C Chengjia Hu M Meiling Lu L Lei Chen W Wencai Jie Z Zhen Yue J Jianbo Jian Y Yuqing Sun (Key Laboratory of Biomedical Polymers-Ministry of Education, College of Chemistry and Molecular Sciences) H Hui Yan J Jingjing Zhou X Xianying Zhang S Shengye Liao Z Zhaofa Li (School of Chemistry, South China Normal University 1 , Guangzhou 510006,) S Shuangfeng Cai Y Yaqing Wu K Kexin Yang (School of Life Science and Technology, ShanghaiTech University) Y Yanan Xiong Y Yonggang Zhao Z Zhimin Lv X Xiaoming Xu (State Key Laboratory of Elemento-Organic Chemistry, Frontiers Science Center for New Organic Matter and College of Chemistry) C Chuang Liu (College of Chemistry and Molecular Sciences, Hubei Key Laboratory of Electrochemical Power Sources) P Pengliang Xin L Lichao Ye X Xiuling Cui Q Qiong Shi (State Key Laboratory of Virology and Biosafety, Hubei Provincial Research Center for Basic Biological Sciences, TaiKang Center for Life and Medical Sciences, College of Life Sciences, Hubei Key Laboratory of Cell Homeostasis, Frontier Science Center for Immunology and Metabolism, Department of Psychiatry, Renmin Hospital of Wuhan University, Wuhan University) X Xi Chen R Ruian Xu

Abstract

Abstract Current thrombolytic therapies primarily function by converting plasminogen into plasmin, a process dependent on the fibrin–activator complex. This dependence, coupled with the substantial molecular size of plasmin, constrains its effectiveness in degrading D-dimer and restricts its diffusion within thrombi. Here, we introduce a small facultative plasminogen-independent thrombolytic enzyme, snFPITE, isolated from Sipunculus nudus . Compared to traditional thrombolytic agents, snFPITE does not require plasminogen for thrombolysis, although its presence enhances lytic activity. This enzyme fully degrades cross-linked fibrin without leaving residual nondegradable D-dimer and generates a smaller fibrinolytic-active agent from plasminogen. A series of male rats and mice models further confirm that snFPITE is a safety injectable thrombolytic agent. Mechanistically, snFPITE activates plasminogen and degrades fibrin(ogen) in a multisite cleavage manner. snFPITE is inhibited by plasminogen activator inhibitor 1 and α2-antiplasmin via a competitive inhibition. We further identify 28 snFPITE candidate sequences, of which 10 are confirmed as functional genes.

Article Details

Volume / Issue Vol. 16, Issue 1
Published April 24, 2025
ISSN 2041-1723
Publisher Nature Portfolio

Journal Info

Nature Communications

Nature Portfolio

ISSN: 2041-1723 Open Access Life Sciences

Authors (32)

M

Mingqing Tang

G

Guoxing Ma

C

Chunyan Xu

H

Hui Yang

H

Hongjun Lin

C

Chao Bian

C

Chengjia Hu

M

Meiling Lu

L

Lei Chen

W

Wencai Jie

Z

Zhen Yue

J

Jianbo Jian

Y

Yuqing Sun

Key Laboratory of Biomedical Polymers-Ministry of Education, College of Chemistry and Molecular Sciences

H

Hui Yan

J

Jingjing Zhou

X

Xianying Zhang

S

Shengye Liao

Z

Zhaofa Li

School of Chemistry, South China Normal University 1 , Guangzhou 510006,

S

Shuangfeng Cai

Y

Yaqing Wu

K

Kexin Yang

School of Life Science and Technology, ShanghaiTech University

Y

Yanan Xiong

Y

Yonggang Zhao

Z

Zhimin Lv

X

Xiaoming Xu

State Key Laboratory of Elemento-Organic Chemistry, Frontiers Science Center for New Organic Matter and College of Chemistry

C

Chuang Liu

College of Chemistry and Molecular Sciences, Hubei Key Laboratory of Electrochemical Power Sources

P

Pengliang Xin

L

Lichao Ye

X

Xiuling Cui

Q

Qiong Shi

State Key Laboratory of Virology and Biosafety, Hubei Provincial Research Center for Basic Biological Sciences, TaiKang Center for Life and Medical Sciences, College of Life Sciences, Hubei Key Laboratory of Cell Homeostasis, Frontier Science Center for Immunology and Metabolism, Department of Psychiatry, Renmin Hospital of Wuhan University, Wuhan University

X

Xi Chen

R

Ruian Xu