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Updated: May 24, 2026

Multi-Gene Single Nucleotide Polymorphism Detection in Gastric Cancer Based on Ion Semiconductor Sequencing Platform
Published on: May 10, 2024
[Interaction of SerpinB5 and MAFbx in gastric cancer cell and its action site]
Ke-feng Lei1, Yi-fei Wang, Qun-qun Wang
1Department of Surgery, Shanghai Jiaotong University School of Medicine, Shanghai, China.
Objective:
To explore the interaction between SerpinB5 and MAFbx in gastric cancer cell and to identify the interaction sites.
Methods:
The interaction between SerpinB5 and MAFbx was screened and validated by yeast two-hybrid screening and co-immunoprecipitation. The expression of MAFbx was analyzed after SerpinB5 expression being modified by RNA interference and pGBKT7-SerpinB5 transfection. The impact of SerpinB5 on the expression of MAFbx was studied in gastric cancer cell line SUN-16. A model of MAFbx was constructed by homology modeling. The related residues for interaction were analyzed by Autodock4.0.
Results:
The interaction between SerpinB5 and MAFbx was validated. The expression of MAFbx changed along with SerpinB5 expression. Amino acids including PRO261, ASN361, and LYS362 were key residue in the interaction of SerpinB5 and MAFbx.
Conclusion:
SerpinB5 interacts with MAFbx in gastric cancer cell. Amino acids including PRO261, ASN361, and LYS362 are potential binding sites.
Insights
Serine protease inhibitor B5 (SerpinB5) interacts with MAFbx in gastric cancer cells. Key amino acids PRO261, ASN361, and LYS362 were identified as crucial for this interaction.
Area of Science:
- Molecular biology
- Oncology
- Protein-protein interactions
Background:
- Gastric cancer is a significant global health concern.
- Understanding protein interactions is crucial for identifying therapeutic targets.
Purpose of the Study:
- To investigate the interaction between SerpinB5 and MAFbx in gastric cancer.
- To pinpoint the specific amino acid residues involved in this interaction.
Main Methods:
- Yeast two-hybrid screening and co-immunoprecipitation were used to validate the interaction.
- RNA interference and gene transfection were employed to study gene expression.
- Homology modeling and molecular docking (Autodock4.0) were utilized to analyze interaction sites.
Main Results:
- The interaction between SerpinB5 and MAFbx was confirmed.
- MAFbx expression levels were found to correlate with SerpinB5 expression.
- PRO261, ASN361, and LYS362 were identified as critical residues for the interaction.
Conclusions:
- SerpinB5 directly interacts with MAFbx within gastric cancer cells.
- The identified amino acids (PRO261, ASN361, LYS362) represent potential binding sites for therapeutic intervention.
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