小分子用于损害癌症中的内质网膜
Tripti Mishra1, Navneet Dubey1, Sudipta Basu1
1Department of Chemistry, Indian Institute of Technology (IIT) Gandhinagar, Palaj, Gandhinagar, Gujarat, 382355, India. Sudipta.basu@iitgn.ac.in.
Organic & biomolecular chemistry
|October 7, 2024
概括
这篇评论探讨了内质网膜 (ER) 压力,这是细胞对未折叠蛋白质的反应. 用小分子和金属复合体准ER压力为癌症治疗提供了一个有前途的治疗策略.
科学领域:
- 细胞生物学 细胞生物学
- 生物化学 生物化学
- 在瘤学瘤学.
背景情况:
- 细胞内膜网膜 (ER) 对于蛋白质平衡和 (Ca2+) 调节至关重要.
- ER应激或未折叠蛋白质反应 (UPR) 是由未折叠蛋白质的积累激活的.
- 虽然ER压力支持癌细胞存活,但持续的压力可以诱导细胞死亡,从而成为治疗点.
研究的目的:
- 审查诱导ER压力的小分子,金属复合物和其他化合物.
- 探索这些药物向ER应激传感器,蛋白质降解和陪伴者的机制.
- 讨论ER向癌症治疗的挑战和未来方向.
主要方法:
- 对针对ER压力的小分子的文献综述.
- 对金属复合物和各种化合物诱导ER压力的审查.
- 分析ER压力诱导和治疗潜力的机制.
主要成果:
- 各种小分子,金属复合物和化合物可以调节ER应力路径.
- 这些药物针对ER应激反应的关键组件,包括传感器,降解机器和陪伴者.
- 诱导持续的ER压力是癌症治疗的可行策略.
结论:
- 针对ER压力代表了癌症治疗的重要治疗途径.
- 需要进一步的研究,以克服开发下一代ER向疗法的挑战.
- 小分子和金属复合体显示出新型癌症治疗策略的潜力.
相关概念视频
Targeted Cancer Therapies
7.5K
The targeted cancer therapies, also known as “molecular targeted therapies,” take advantage of the molecular and genetic differences between the cancer cells and the normal cells. It needs a thorough understanding of the cancer cells to develop drugs that can target specific molecular aspects that drive the growth, progression, and spread of cancer cells without affecting the growth and survival of other normal cells in the body.
There are several types of targeted therapies against...
There are several types of targeted therapies against...
7.5K
Post-translational Translocation of Proteins to the RER
5.6K
A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
5.6K
Role of ER in the Secretory Pathway
5.3K
Eukaryotic cells have a special pathway that enables communication between various intracellular membrane-bound compartments and also with the extracellular environment. This pathway is termed as the secretory pathway.
Components of the secretory pathway
About a third of proteins synthesized in the cell are sorted via the secretory route. They shuffle between different compartments in membrane-bound vesicles until they reach their final destination. The main intracellular compartments involved...
Components of the secretory pathway
About a third of proteins synthesized in the cell are sorted via the secretory route. They shuffle between different compartments in membrane-bound vesicles until they reach their final destination. The main intracellular compartments involved...
5.3K
Directing Proteins to the Rough Endoplasmic Reticulum
7.2K
The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
7.2K
The Endoplasmic Reticulum
12.3K
The endoplasmic reticulum or ER makes up for more than half of the membranes in a cell and accounts for 10% of total cell volume. It is also the primary protein and lipid synthesis factory for most cell organelles, such as the Golgi apparatus, lysosomes, secretory vesicles, and the plasma membrane. Despite being the most extensive and functionally complex subcellular organelle, ER was the last to be discovered. After years of deliberation, Keith Porter and George Palade in the year 1954,...
12.3K
Tail-anchoring of Proteins in the ER Membrane
3.1K
Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
3.1K


