在人类精液细胞外囊中的人体跨膜血清蛋白酶2 (TMPRSS2) 是蛋白质活性的活体
Emile Verhulst1, Michelle De Bruyn1, Pascale Berckmans2
1Laboratory of Medical Biochemistry, Faculty of Pharmaceutical, Biomedical and Veterinary Sciences, University of Antwerp, Wilrijk, Belgium.
Journal of extracellular vesicles
|March 17, 2025
概括
研究人员开发了一种使用来自精液细胞外囊泡 (SF-EVs) 的活跃人体跨膜血清蛋白酶2 (TMPRSS2) 的新测定方法. 该工具有助于发现针对各种疾病的针对TMPRSS2的药物.
科学领域:
- 生物化学 生化学
- 分子生物学分子生物学
- 病毒学 病毒学
背景情况:
- 人体跨膜血清蛋白酶2 (TMPRSS2) 对于病毒的进入和疾病的发病至关重要.
- 准TMPRSS2需要一个稳定,活跃的酶源用于研究和药物开发.
研究的目的:
- 在精液细胞外囊泡 (SF-EVs) 上表征原生,活跃的TMPRSS2.
- 开发一种可靠的体外试验法,用于选TMPRSS2抑制剂.
- 为了比较SF-EV相关的TMPRSS2与重组形式.
主要方法:
- 使用流细胞计和活性试验,对具有表面暴露的TMPRSS2的SF-EV进行表征.
- 人类TMPRSS2ectodomain的重组生产.
- 生物化学测试以确定催化参数和抑制概况.
- 基于SF-EV的体外查试验的开发.
主要成果:
- 现有的SF-EV具有酶活性,表面暴露的TMPRSS2.
- 重组TMPRSS2ectodomain的成功产生.
- 原生SF-EV相关和重组TMPRSS2显示了类似的活性和抑制纳法莫斯甲基酸盐.
- 为TMPRSS2抑制剂查建立了基于SF-EV的强有力的试验.
结论:
- SF-EVs提供了一个稳定的,原生源活跃的TMPRSS2.2.
- 开发的测定有助于发现针对TMPRSS2的治疗方法.
- 对SF-EV相关的TMPRSS2的生物学作用进行进一步的研究是有必要的.
相关概念视频
Translocation of Proteins into the Mitochondria
Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
SNAREs and Membrane Fusion
Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
Cotranslational Protein Translocation
Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
Insertion of Single-pass Transmembrane Proteins in the RER
Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
Insertion of Multi-pass Transmembrane Proteins in the RER
The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
Protein Translocation Machinery on the ER Membrane
The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.


