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紧接节调节融合 (ADT-6) 通过Caco-2细胞系中的细胞通道提高了GFP蛋白的透性:一种体外研究
Salimeh Hassani1, Keyvan Nedaei1, Rahim Jafari2
1Department of Medical Biotechnology, Faculty of Medicine, Zanjan University of Medical Sciences, Zanjan, Iran.
Reports of biochemistry & molecular biology
|May 7, 2025
概括
这项研究表明,ADT-6可以通过暂时打开细胞结口来增强口服药物输送,改善蛋白质和的药物吸收通过肠道屏障.
科学领域:
- 制药科学 制药科学
- 生物技术是生物技术.
- 分子生物学分子生物学
背景情况:
- 由于肠道和血脑屏障 (BBB),口服和蛋白质的输送具有挑战性.
- 这些屏障限制了大型的水性分子通过跨细胞和细胞路径的通行.
- 细胞间紧密的结局限制了细胞间运输.
研究的目的:
- 调查ADT-6,一种调节E-cadherin的,用于增强治疗剂的透.
- 评估ADT-6在改善口服药物输送方面的疗效.
主要方法:
- 构建了一个融合蛋白:ADT-6与绿色光蛋白 (GFP) 结合.
- 在大肠杆菌中表达了GFP-ADT-6结构.
- 使用分子模拟和Caco-2细胞单层评估运输和活动.
主要成果:
- 分子模拟证实了融合蛋白的完整性和灵活性.
- ADT-6剂量依赖性降低了横体电阻 (TEER).
- 在用GFP-ADT-6治疗的Transwell系统中,GFP传染和检测的显著增加.
结论:
- 而ADT-6则促进了通过半细胞路径的蛋白质输送.
- 通过调节细胞与细胞之间的相互作用来提高药物药物的生物可用性.
- 为口服药物输送系统提供了新的策略.
相关概念视频
Contact-dependent Signaling
Contact-dependent signaling, as the name suggests, requires that communicating cells be in direct contact with each other. This is achieved either through receptor-ligand interactions or by specialized cytoplasmic channels that allow the flow of small molecules between cells. In animal cells, channels called gap junctions facilitate contact-dependent signaling in certain tissues, whereas, plasmodesmata perform a similar function in plants.
Gap Junctions
In animal cells, gap junctions are formed...
Gap Junctions
In animal cells, gap junctions are formed...
Overview of Cell-Matrix Interactions
The extracellular matrix or ECM holds cells together to form a tissue and allows the cells within the tissue to communicate. ECM comprises proteins such as fibronectin, collagen, laminin, etc. The most abundant protein in this space is collagen. Collagen fibers are interwoven with carbohydrate-containing protein molecules called proteoglycans. ECM allows cell migration and provides a structural scaffold at cell adhesion that anchors the cell when the extracellular matrix proteins interact with...
Overview of Cell-Cell Junctions
The complex three-dimensional arrangement of cells in any multicellular organism is defined and maintained by interactions of cells with each other and the extracellular matrix. Cell-cell junctions are specialized structures where the multi-protein complexes on one cell interact with the multi-protein complexes on another cell. These cell junctions are classified into three main types based on their function — occluding, anchoring, and gap junctions.
Occluding or Tight Junctions
Tight...
Occluding or Tight Junctions
Tight...
Adherens Junctions
Strong contact points between adjacent cells anchor them to each other, forming tissues. Such anchoring junctions are of two types – adherens junctions and desmosomes. Adherens junctions are abundant in tissues such as epithelium and endothelium, forming a continuous zone of adhesion called the adhesion belt. In other tissues, such as heart muscle, they appear as clusters, linking the cells to produce coordinated heart muscle contraction.
Adherens Junctions are Dynamic
The endothelial cells...
Adherens Junctions are Dynamic
The endothelial cells...
Tight Junctions
Tight junctions are molecular seals between cells that prevent the leaking of fluids, ions, and other small solutes across cavities and compartments in multicellular organisms. They are mainly composed of claudin and occludin transmembrane proteins, and other proteins such as tricellulin and JAM (junctional adhesion molecule). All these proteins are 4-pass transmembrane proteins, except JAM, which is a single-pass transmembrane protein belonging to the immunoglobulin superfamily. The...
Gap Junctions
The cytoplasm of adjacent animal cells can exchange small molecules, ions, and secondary messengers via the communication channels which form the gap junctions. These junctions comprise a few hundred to thousands of molecular channels, each made of two halves, called the connexon hemichannel. A connexon is a hexamer of six transmembrane connexin proteins, which assemble radially, thus forming a pore or channel in the center. One connexon hemichannel docks with a corresponding connexon on the...

