Abstract
Neuritin is a vital neurotrophin that plays an essential role in recovery from nerve injury and neurodegenerative diseases and may become a new target for treating these conditions. However, improving neuritin protein stability is an urgent problem. In this study, to obtain active and stable neuritin proteins, we added a carboxyl-terminal peptide (CTP) sequence containing four O-linked glycosylation sites to the C-terminus of neuritin and cloned it into the Chinese hamster ovary (CHO) expression system. The neuritin-CTP protein was purified using a His-Tag purification strategy after G418 screening of stable high-expression cell lines. Ultimately, we obtained neuritin-CTP protein with a purity >90%. Functional analyses showed that the purified neuritin-CTP protein promoted the neurite outgrowth of PC12 cells, and stability experiments showed that neuritin stability was increased by adding CTP. These results indicate that neuritin protein-CTP fusion effectively increases stability without affecting secretion and activity. This study offers a sound strategy for improving the stability of neuritin protein and provides material conditions for further study of the function of neuritin.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.