Since O-Glycosylation occurs in all domains of life, the enzymatic release of O-glycosylated protein is a key segment in glycomics research. CD BioGlyco integrates various advanced technologies to develop an efficient and accurate release strategy of O-glycosylated proteins. Welcome clients from all over the world to cooperate with us!
Glycoproteins are proteins that contain oligosaccharide chains (glycans) covalently linked to amino acid side chains. The most common types of glycoproteins are N-linked and O-linked glycoproteins, which differ by structural differences. Glycans are attached to specific amino acid residue side chains of proteins in a co-translational or post-translational manner, a process known as glycosylation. These post-translationally linked glycans have multiple roles, such as cell recognition, adhesion, signaling, and more. O-Glycosylation is a post-translational event in which the carbohydrate is covalently attached to the hydroxyl group of serine (Ser) or threonine (Thr). O-Glycosylation provides ligands for selectins, resists proteolysis, and is involved in recognition phenomena. O-Glycoproteins change their glycosylation patterns when expressed in new cellular systems resulting in impaired protein function. In addition, O-glycosylation has implications for the biotechnology industry. Therefore, it is of interest to know the location and type of O-glycosylation in a given glycoprotein.
Various forms of O-glycosylation are abundant in organisms and play important roles in many cellular functions. Changes in O-glycosylation are also closely associated with a variety of diseases, such as Alzheimer's disease, diabetes, and cancer. O-Glycosylation changing of Mucin 1 (MUC1) is one of the striking features of oncogenic mucins. Studies have shown that the cancer-associated glycoform of MUC1 contributes to the progression, invasion, and metastasis of epithelial tumors. In conclusion, understanding these O-glycosylation changes in cancer cells may lead to new diagnostic and therapeutic opportunities.
Fig.1 Molecular roles of O-glycans in homeostasis and disease. (Magalhães, et al., 2021)
To better understand these O-glycosylation changes in cancer cells, a reliable method must be identified to separate O-glycosylated proteins from native glycoproteins before analysis. At CD BioGlyco, we have developed an advanced Enzymatic Release platform. We provide clients with efficient and accurate release services of native mucin-type O-glycosylated proteins via O-protease. We high-specifically hydrolyze peptide bonds in proteins at the N-terminus of O-glycans at Ser or Thr to release intact native core 1 O-glycosylated proteins. In addition, we provide clients with fast and sensitive O-glycosylated protein characterization services.
Fig.2 The process of enzymatic release of O-glycosylated protein. (CD BioGlyco)
With first-class experimental platforms, CD BioGlyco provides global enterprises and scientific research institutions with efficient and high-quality enzymatic release services. Our strategy will greatly accelerate the project progress of our clients. Please contact us for more detailed information if you need scientific assistance.
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