Journal: bioRxiv

Article Title: Denatured Albumin Gains a Function of Regulating Platelet Activity

doi: 10.64898/2026.03.30.715112

Figure Lengend Snippet: (A) Platelets (green) adhered exclusively to the albumin-adsorbed region (magenta), but not to the casein-adsorbed region (dark). Albumin was pre-labeled with Alexa488. Platelets were stained with phalloidin to label F-actin. (B) Resting platelets, ADP-activated platelets and HeLa cells on fibronectin (FN), fibrinogen (Fg), bovine serum albumin (BSA), human serum albumin (HSA), recombinant human serum albumin (rHSA) and casein-adsorbed glass surfaces, respectively. ( C-E ) Cell spreading areas of platelets or HeLa cells on the six surfaces. Platelets in (C) were kept at a resting state prior to cell plating, whereas platelets in (D) were pre-activated by 10 µM ADP. (**** P <0.0001; ns P >0.05; Each data point represents one cell; For each condition, N = 100 cells from three independent experiments; Error bars indicate SD).

Article Snippet: Activated platelets or resting platelets at concentration of 4.0 × 10 4 /μL were seeded onto glass coverslips pre-coated with 10 μg/ml fibronectin (F1141, Sigma-Aldrich), 100 μg/mL fibrinogen (F3879, Sigma-Aldrich), 100 μg/mL ultrapure bovine serum albumin (AM2616, Invitrogen), 100 μg/mL ultrapure human serum albumin (A8763, Sigma-Aldrich), 100 μg/mL recombinant human serum albumin (HSA-H5220, Acro Biosystems) or 100 μg/ml casein, and incubated at 37 °C in a cell incubator containing 5% CO2 for 30 minutes.

Techniques: Labeling, Staining, Recombinant