Journal: Neoplasia (New York, N.Y.)

Article Title: PIK3CA mutant cervical cancer is selectively suppressed by PI3Kα inhibition (Alpelisib/BYL-719 and Inavolisib/GDC-0077) and cooperates with HPV directed T cell therapy

doi: 10.1016/j.neo.2026.101305

Figure Lengend Snippet: Impact of BYL-719 on the expression of target proteins in cervical cancer cell lines. ( A, B) CaSki cells treated with BYL-719 show reduced levels of PD-L1, YAP1, EGFR, CTGF, Integrin, and HPV16 E7. In Panel B cells were treated with 5uM BYL-719, washed at 24 h and place in 0, 1 or 5uM drug. (exposure time, 2 min). (C) BYL-719-treated ME180 cells show decreased levels of PD-L1 and CTGF. (D) SNU-17 cells also show reduced levels of these proteins after treatment (exposure time, 5 min). (E) SiHa ( PIK3CA WT) shows no reduction ofHPV16 E7 after treatment with BYL-719 (exposure time, 3 min). (F) Cell proliferation plot of SNU-17 cells treated with BYL-719. (G) SiHa cells treated with BYL719. *=P < 0.05, **=P < 0.01, ***=P < 0.001.

Article Snippet: CC cell lines, including CaSki (ATCC Cat# CRM-CRL-1550_Ca Ski, RRID: CVCL_1100), SiHa (ATCC Cat# HTB-35_SiHa, RRID: CVCL_0032), and ME180 (ATCC Cat# HTB-33_ME-180, RRID: CVCL_1401), C33A (ATCC CRM-HTB-31, RRID:CVCL_1094) were obtained from ATCC.

Techniques: Expressing

Journal: Cell Reports Medicine

Article Title: Early-stage multi-cancer detection through a plasma extracellular vesicle protein signature

doi: 10.1016/j.xcrm.2026.102694

Figure Lengend Snippet: Transformation-induced changes to the protein composition of cell-derived sEVs (A) The morphology of isolated sEVs was assessed using transmission electron microscopy. Images of normal and transformed HBEC-derived sEVs (scale bars, 200 nm). (B) Nanoparticle analysis using tunable resistive pulse sensing of sEVs isolated from HBECs demonstrates that the majority of sEVs have a size range between 30 and 150 nm, and that transformation does not result in an increase in sEV secretion. (C) Western blot of sEVs from HBECs demonstrating the presence of sEV proteins HSP70 and CD63 and the absence of the cell marker calnexin. (D) Label-free mass spectrometry identified 148 proteins with greater abundance in sEVs derived from transformed HBECs (FDR <0.02), of which 15 were annotated as extracellular proteins. (E) Mass spectrometry results were confirmed using ELISA for THBS1, NID1, PTX3, and VCAN in sEVs derived from normal and transformed HBECs. (F) sEVs derived from 22 cancer cell lines including NSCLC (SKMES1, H1650, HCC4006, and H2170), glioblastoma ([GBM], D54, D270, U87, and U118), colorectal cancer ([CRC], HT29 and SW620), breast cancer ([BCa], BT549, MDA231, and MDA436), prostate cancer ([PCa], PC3 and LNCaP), melanoma ([MEL], A375, MAMEL65, and SKMEL28), esophageal cancer ([ECa], OE19), and ovarian cancer ([OVA], A2780, CAOV3, IGROV1, and OVCAR8) showed a clear increase in expression of THBS1, NID1, PTX3, and VCAN in relation to the average levels of sEVs from normal cells ([HBEC] 30KT, HOSE 6.3, and HOSE 17.1). Samples in mass spectrometry and ELISA were measured in triplicate. See also and .

Article Snippet: SKMES1 , ATCC , HTB-58; RRID: CVCL_0630.

Techniques: Transformation Assay, Derivative Assay, Isolation, Transmission Assay, Electron Microscopy, Tunable Resistive Pulse Sensing, Western Blot, Marker, Mass Spectrometry, Enzyme-linked Immunosorbent Assay, Expressing