AI Article Synopsis
- Controlled cell death is crucial for immune regulation and is affected in diseases like cancer and autoimmune disorders, with the Fas receptor and Fas ligand playing key roles in this process.
- Soluble Fas ligand (sFasL), produced through ectodomain shedding, has various non-apoptotic functions and can act as a pro-survival factor.
- The study aims to create homogeneous, N-glycosylated variants of sFasL using a flexible strategy that combines chemical synthesis with enzymatic methods to understand its characteristics better.
Article Abstract
Controlled cell death is essential for the regulation of the immune system and plays a role in pathogen defense. It is often altered in pathogenic conditions such as cancer, viral infections and autoimmune diseases. The Fas receptor and its corresponding membrane-bound ligand (FasL) are part of the extrinsic apoptosis pathway activated in these cases. A soluble form of FasL (sFasL), produced by ectodomain shedding, displays a diverse but still elusive set of non-apoptotic functions and sometimes even serves as a pro-survival factor. To gather more knowledge about the characteristics of this protein and the impact N-glycosylations may have, access to homogeneous posttranslationally modified variants of sFasL is needed. Therefore, we developed a flexible strategy to obtain such homogeneously N-glycosylated variants of sFasL by applying chemical protein synthesis. This strategy can be flexibly combined with enzymatic methods to introduce more complex, site selective glycosylations.
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Controlled cell death is essential for the regulation of the immune system and plays a role in pathogen defense. It is often altered in pathogenic conditions such as cancer, viral infections and autoimmune diseases. The Fas receptor and its corresponding membrane-bound ligand (FasL) are part of the extrinsic apoptosis pathway activated in these cases.
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