Journal: Advanced Science
Article Title: O‐GalNAc Glycosylation Activates MBL‐Mediated Complement and Coagulation Cascades to Drive Organotropic Metastasis
doi: 10.1002/advs.202504809
Figure Lengend Snippet: High MBL pathway activity is enriched in PCa liver metastasis and GalNAc is a major glycosylation form on NEPC cell surface. a) The KEGG analysis showing that the “complement and coagulation cascades” is most upregulated signature in liver metastasis versus primary prostate tumors of rb1 Δ/Δ p53 Δ/Δ NEPC tumor‐bearing mice (n = 3, mice). b,c) GSEA plots reveal that “complement and coagulation cascade” (b) and “MBL pathway activity” are significantly elevated in liver metastatic lesions compared to metastasis in other anatomic sites based on analysis of the SU2C prostate cancer dataset. d) Kaplan–Meier survival analysis of the SU2C prostate cancer dataset reveal that PCa patients with high MBL activity (n = 39) exhibit significantly shorter survival compared to PCa patients with low MBL activity (n = 39). The log rank‐test was applied for statistics. e,f) GSEA plots showing that the “cell surface glycosylation” is significantly elevated in NEPC compared to PrAD based on analysis of Beltran and SU2C prostate cancer datasets. g) Lectin microarray results that the O‐GalNAc glycosylation, as revealed by the strongest signal of vicia villosa (VVA) lectin toward the membrane fraction extracted from murine rb1 Δ/Δ p53 Δ/Δ NEPC organoids.
Article Snippet: Utilizing a commercial lectin microarray kit (RayBiotech, GA‐Lectin‐70‐14) including a total of 70 lectin proteins, an analysis on glycan expression profiles was conducted using murine rb1 Δ/Δ p53 Δ/Δ NEPC cells, based on the manufacturer's guidelines.
Techniques: Activity Assay, Glycoproteomics, Coagulation, Microarray, Membrane