Fig 2: PVRL2 overexpression in high grade serous ovarian cancer. (A,B) Transcript levels of PVRL2 vs. PD-L1 in our cohort and TCGA cohort. p-values were determined by two-tailed paired student t-test. (C) Heat map of Spearman rank correlations between PVRL2 and individual immune cell subsets and top differentially expressed immune response genes in WIHRI and TCGA cohorts. Spearman r values are indicated by color. (D) Representative immunohistochemistry staining of PVRL2 in HGSOC and normal/benign ovaries. Negative control is secondary antibody alone. (E,F) Mean and maximum PVRL2 intensity (pixels) in serous ovarian cancer vs. normal/benign tissue.

Fig 3: The co-localization of 6 indicators (CD155, NECTIN2, CEACAM1, HMGB1, SIGLEC6, CD44), CD45 and gastric cancer CKpan.Multi-colour immunofluorescence staining of anti-CKpan and CD45 antibodies with CD155, NECTIN2, CEACAM1, HMGB1, SIGLEC6 or CD44 antibodies. Scale bar = 200 μm.

Fig 4: The recruitment of LAMP3+ DCs by tumor cells promotes PTC clinical progression. Heatmaps (A) and circle (B) plots show the comparison of interaction quantity and interaction strength between thyrocytes and cDCs between non-progressive PTC and progressive PTC. Red indicated that the increase of communication in the latter. (C) The interaction between thyrocytes and cDCs is more numerous and stronger in Group B. (D) Summary of selected ligand-receptor interactions between thyrocytes and cDC-C3 cells in the two groups. (E) Circle plots showing the interaction between NECTIN3-NECTIN2 ligand-receptor pairs in the cDCs and thyrocytes. (F) The expression level of S100A2 is positively correlated with LAMP3. (G) Representative immunofluorescence images illustrating the interaction between thyrocytes and cDC_C3 in two groups (A1 and B9). The small panels show the magnification of the selected region highlighted in red. Scale bars correspond to 50 µm in the large panel. (H) Schematic showing the crosstalk among thyrocytes, LAMP3+ DCs, CD8+ T cells, and Tregs involved in the recruitment of immune cells and the formation of an immunosuppressive microenvironment in the progressive PTC. cDC. conventional DC; DC, dendritic cell; CTLA-4, cytotoxic T-lymphocyte associated protein 4; ICAM, intercellular adhesion molecule 1; LAMP3, lysosomal associated membrane protein 3; PTC, papillary thyroid cancer; SPN, sialophorin; TME, tumor microenvironment; Treg, regulatory T cell.

Fig 5: Uncovering the senescence‐associated surface proteome. (a) SA‐β‐Gal activity was analyzed in WI‐38 fibroblasts at ~PDL24 (proliferating, P), after reaching replicative exhaustion at ~PDL54 (RS), or after exposure to 10 Gy of ionizing radiation and culture for an additional 10 days (IRIS). (b) Workflow for cell‐surface protein biotinylation and isolation for proteomic analysis; prepared using BioRender. (c) Overlap of the cell surface proteins elevated in RS vs P (green) and IRIS vs P (pink) after processing as in panels (a, b). (d) Top significantly (FDR <0.05) enriched GO Molecular Function terms after ShinyGO analysis performed on the shared cell surface proteins upregulated in senescent cells. (e) Heatmap illustrating the magnitude of induction in a subset of surface proteins, comparing RS to P cells and IRIS to P cells that were prepared as explained in (a). In the heatmap, 5NTD, ICAM1, DPP4, NECT2, and ITA1 are CD73, CD54, CD26, CD112, and CD49A, respectively. (f) WI‐38 cells were processed as in (a), and the levels of CD49A, CD73, CD109, CD54, CD112, CD44, HLA‐ABC, CD26, and loading control β‐Actin (ACTB) were assessed in Input (whole‐cell proteins) and Surface (cell‐surface proteins) by western blot analysis. “Input”, 10 μg of the protein lysate before pulldown; “Surface”, 5% of the eluted protein volume after pulldown. As the lysis buffer did not fully solubilize membrane proteins, only “Surface” proteins are quantified (ImageJ). Data are representative of three independent replicates.