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N-glycosylation of Wnt3 regulates the progression of hepatocellular carcinoma by affecting Wnt/ß-catenin signal pathway.
Zhang, Xin-Zhan; Mo, Xiao-Chuan; Wang, Zhu-Ting; Sun, Rong; Sun, Da-Quan.
Afiliación
  • Zhang XZ; Department of Biochemistry and Molecular Biology & Research Center for Basic Medical Sciences, Guizhou Medical University, Guiyang 550025, Guizhou Province, China.
  • Mo XC; Department of Biochemistry and Molecular Biology & Research Center for Basic Medical Sciences, Guizhou Medical University, Guiyang 550025, Guizhou Province, China.
  • Wang ZT; Department of Biochemistry and Molecular Biology & Research Center for Basic Medical Sciences, Guizhou Medical University, Guiyang 550025, Guizhou Province, China.
  • Sun R; Department of Biochemistry and Molecular Biology & Research Center for Basic Medical Sciences, Guizhou Medical University, Guiyang 550025, Guizhou Province, China.
  • Sun DQ; Department of Biochemistry and Molecular Biology & Research Center for Basic Medical Sciences, Guizhou Medical University, Guiyang 550025, Guizhou Province, China. sundq04@sina.com.
World J Gastrointest Oncol ; 16(6): 2769-2780, 2024 Jun 15.
Article en En | MEDLINE | ID: mdl-38994173
ABSTRACT

BACKGROUND:

Wnt/FZD-mediated signaling pathways are activated in more than 90% of hepatocellular carcinoma (HCC) cell lines. As a well-known secretory glycoprotein, Wnt3 can interact with FZD receptors on the cell surface, thereby activating the Wnt/ß-catenin signaling pathway. However, the N-glycosylation modification site of Wnt3 and the effect of this modification on the biological function of the protein are still unclear.

AIM:

To investigate the effect of Wnt3 N-glycosylation on the biological function of HCC cells.

METHODS:

Site-directed mutagenesis was used to verify the Wnt3 N-glycosylation sites, actinomycin D treatment was used to detect the stability of Wnt3 after site-directed mutation, the binding of the N-glycosylation site-directed mutant Wnt3 to FZD7 was observed by laser confocal microscopy, and the effects of the N-glycosylation site-directed mutation of Wnt3 on the Wnt/ß-catenin signaling pathway and the progression of HCC cells were detected by western blot and cell function experiments.

RESULTS:

Wnt3 has two N-glycosylation-modified sites (Asn90 and Asn301); when a single site at amino acid 301 is mutated, the stability of Wnt3 is weakened; the binding ability of Wnt3 to FZD7 decreases when both sites are mutated simultaneously; and the level of proteins related to the Wnt/ß-catenin signaling pathway is downregulated. Cell proliferation, migration and invasion are also weakened in the case of single 301 site and double-site mutations.

CONCLUSION:

These results indicate that by inhibiting the N-glycosylation of Wnt3, the proliferation, migration, invasion and colony formation abilities of liver cancer cells can be weakened, which might provide new therapeutic strategies for clinical liver cancer in the future.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: World J Gastrointest Oncol Año: 2024 Tipo del documento: Article País de afiliación: China Pais de publicación: China
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: World J Gastrointest Oncol Año: 2024 Tipo del documento: Article País de afiliación: China Pais de publicación: China