Background
This study aimed to investigate the expression of neuritin in four common cancers, and to explore the association between neuritin expression and the occurrence and development of cancer.
Methods
We initially examined neuritin expression in human cervical, endometrial, oesophageal, and lung cancer tissues by immunohistochemistry (IHC). Based on these results, we further examined its expression in lung squamous cell carcinoma (LUSC) tissues by IHC and reverse transcription-polymerase chain reaction (RT-PCR).
Results
Neuritin expression levels were higher in all cancer tissues compared with normal control tissues. Neuritin protein and gene expression levels were significantly higher in LUSC tissues compared with normal lung tissues (P<0.001), according to IHC and RT-PCR, respectively. Neuritin expression levels decreased significantly with increased clinical TNM stage (I-IV) and distant metastasis (P<0.05).
Conclusion
Neuritin may have clinical value as a novel diagnostic and prognostic marker in patients with LUSC.
Objective: To obtain the long-acting protein neuritin we fused the carboxyl-terminal peptide (CTP) to the C-terminal of neuritin and expressed it in Chinese hamster ovarian (CHO) cells.
Methods:The plasmid was constructed by fusion PCR. Affinity chromatography is used for protein purification. Thermal stability and serum stability were used to evaluate protein stability.
Results: The molecular weight of the neuritin-CTP was determined to be approximately 20 kDa. Subsequent functional analysis showed that the purified neuritin-CTP promoted neurite outgrowth in PC12 cells at a rate equivalent to that observed with neuritin. The stability experiments showed that the degradation rate of neuritin was 100% after incubation at 37°C for 72 h, whereas only approximately 20% of the neuritin-CTP was degraded under the same conditions. Similarly, the serum stability analysis results showed that neuritin degraded by approximately 90% and neuritin-CTP degraded by approximately 30% after incubation at 37°C for 72 h.
Conclusions: Fusion with CTP can effectively increase the stability of neuritin without affecting its secretion and activity. These results provide a basis for the construction of long-acting neuritin proteins.
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