更新于：2024-11-01

enteropeptidase

更新于：2024-11-01

基本信息

别名

Enterokinase、Enteropeptidase、Enteropeptidase catalytic light chain

+ [11]

简介

Responsible for initiating activation of pancreatic proteolytic proenzymes (trypsin, chymotrypsin and carboxypeptidase A). It catalyzes the conversion of trypsinogen to trypsin which in turn activates other proenzymes including chymotrypsinogen, procarboxypeptidases, and proelastases.

关联

项与 enteropeptidase 相关的药物

Sucunamostat

靶点

enteropeptidase

作用机制

enteropeptidase抑制剂

在研机构

SCOHIA PHARMA, Inc.初创企业

原研机构

Takeda Pharmaceutical Co., Ltd.

在研适应症

同型半胱氨酸尿症 [+2]

非在研适应症

2型糖尿病 [+2]

最高研发阶段临床1期

首次获批国家/地区-

首次获批日期1800-01-20

WO2023141744

专利挖掘

靶点

ADHs x ALDH2 x enteropeptidase

作用机制-

在研机构

中国科学院动物研究所

原研机构

中国科学院动物研究所

在研适应症

物质滥用

非在研适应症-

最高研发阶段药物发现

首次获批国家/地区-

首次获批日期1800-01-20

OBE-2001

靶点

enteropeptidase

作用机制

enteropeptidase抑制剂

在研机构-

原研机构

Obe Therapy Biotechnology SAS

在研适应症-

非在研适应症

2型糖尿病 [+1]

最高研发阶段无进展

首次获批国家/地区-

首次获批日期1800-01-20

项与 enteropeptidase 相关的临床试验

JPRN-JapicCTI-205109 / Completed临床2期

A Randomized, Multi-center, Double-blind, Placebo-controlled, Parallel-group Comparison, Phase 2a Study to Evaluate the Safety, Tolerability and Efficacy of SCO-792 in Subjects with Type 2 Diabetes and Albuminuria.

开始日期2020-06-11

申办/合作机构

SCOHIA PHARMA, Inc.初创企业

JPRN-jRCT1080225017 / Completed临床2期

开始日期2020-06-11

申办/合作机构

SCOHIA PHARMA, Inc.初创企业

JPRN-JapicCTI-194848 / Completed临床2期

开始日期2019-11-28

申办/合作机构

SCOHIA PHARMA, Inc.初创企业

100 项与 enteropeptidase 相关的临床结果

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100 项与 enteropeptidase 相关的转化医学

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0 项与 enteropeptidase 相关的专利（医药）

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727

项与 enteropeptidase 相关的文献（医药）

2024-11-01·Protein Expression and Purification

Preparation of recombinant neuritin protein

Article

作者: Sun, Jiawei ; Meng, Pingping ; Li, Yuanyuan ; Wei, Yu ; Guo, Jiatong ; Zhu, Liyan ; Zhu, Jingling

Neuritin plays an important role in promoting nerve injury repair and maintaining synaptic plasticity, making it a potential therapeutic target for the treatment of nerve injury and neurodegenerative diseases. The present study aimed to obtain an active, unlabeled neuritin protein. Initially, a neuritin protein expression system with an enterokinase site was constructed in Escherichia coli. After optimizing induction conditions and screening for high expression, a neuritin recombinant protein with purity exceeding 85 % was obtained through Ni-affinity chromatography. Subsequently, unlabeled neuritin with a molecular weight of 11 kDa was obtained through the enzymatic cleavage of the His label using an enterokinase. Furthermore, a neuritin recombinant protein with purity exceeding 95 % was obtained using gel chromatography. Functional investigations revealed that neurite outgrowth of PC12 cells was stimulated by the isolated neuritin. This study establishes a method to obtain active and unlabeled neuritin protein, providing a foundation for subsequent research on its biological functions.

2024-11-01·Journal of Invertebrate Pathology

Bombyx mori serpin 3 is involved in innate immunity by interacting with serine protease 7 to regulate prophenoloxidase activation

Article

作者: Kong, Wei-Wei ; Wang, Jie ; Ayaz, Sadaf ; Wang, Yu-Ling ; Toufeeq, Shahzad ; Cao, Hui-Hua ; Xu, Jia-Ping ; Liu, Shi-Huo

A subfamily of conserved proteins called serpins plays crucial roles in various physiological functions, particularly in the activation pathway of the serine protease cascade, an essential component of insect innate immunity. Here, we found Bombyx mori serpin 3 (BmSerpin3) was most highly expressed in the fat body, and was up-regulated after exposure to bacteria, fungus and virus. Further, the expression of BmSerpin3 in the hemocytes, fat body, midgut of silkworm larvae, and BmN cells was up-regulated upon Bombyx mori nucleopolyhedrovirus (BmNPV) infection. Through Bac-to-Bac expression system, we obtained the active protein of BmSerpin3, and the enzyme activity assay showed that BmSerpin3 significantly inhibited the activity of both subtilisin and trypsin. In addition, BmSerpin3 could inhibit the activation of prophenoloxidase (PPO) in larvae. The knockdown of BmSerpin3 showed increased phenoloxidase (PO) activity compared to control after BmNPV infection. Ultimately, we confirmed that BmSerpin3 interacts with B. mori Serine Protease 7 (BmSP7). Hence, we hypothesize that BmSerpin3 is involved in innate immunity by interacting with BmSP7 to regulate the PPO activation cascade. Taken together, these results showed that BmSerpin3 play a role in silkworm innate immunity and lay a foundation for studying its functions.

2024-10-08·Analytical Chemistry

Development of an Ultrasensitive Competitive Double-Enzyme Cascade Fluorescence Signal Amplification Method for Factor XIa Inhibitor Screening

Article

作者: Zhan, Yujuan ; Ding, Ya ; Shu, Chang ; Yan, Zelong ; Chen, Haotian ; Ning, Jiangyue ; Bao, Xingyan ; Ding, Li ; Hu, Penghui

Coagulation factor XIa (FXIa) is associated with a low risk of bleeding and has been identified as an effective and safe target for the development of novel anticoagulant drugs. In this study, we established an ultrasensitive competitive dual-enzyme cascade signal amplification method for the quantitative analysis and screening of FXIa inhibitors. Due to the specific recognition of FXIa's active site by the aptamer AptE40, the AptE40-QDs-EK recognition probe modified with enterokinase (EK) and the aptamer AptE40, was attached to the MNPs-FXIa capture probe. When FXIa inhibitor was present, it competed with AptE40 for binding to FXIa, resulting in the detachment of AptE40-QDs-EK from MNPs-FXIa. After magnetic separation, the enterokinase of AptE40-QDs-EK in the supernatant hydrolyzed N-terminal hexapeptide of trypsinogen, leading to the production of a large amount of trypsin as part of the first-stage signal cascade amplification. Next, trypsin could hydrolyze the hexameric arginine peptide (RRRRRR, R6), leading to the dissociation of RQDs from the R6-RQDs signal probe; this resulted in a dramatic increase in the fluorescence intensity of the supernatant as the second-stage signal cascade was amplified. The feasibility of the method was investigated using the FXIa inhibitor aptamer FELIAP as a positive model drug. Furthermore, the method was applied to screen the FXIa inhibitors in Eupolyphaga sinensis Walker. Two fractions with more active anticoagulated ingredients were successfully identified and validated via the conventional method, and the results were consistent. The established method provides a key technique for the sensitive detection, high-throughput analysis, and screening of the FXIa inhibitors.