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Fig. 3 | Cell & Bioscience

Fig. 3

From: β-amyloid protein induces mitophagy-dependent ferroptosis through the CD36/PINK/PARKIN pathway leading to blood–brain barrier destruction in Alzheimer’s disease

Fig. 3

Aβ1-40 increases the permeability of the BBB, and downregulating the expression of CD36 can improve the BBB changes caused by Aβ1-40. A TEER detects the BBB tightness of Aβ1-40-treated cells (100 nM and 1 µM) in monolayer and coculture models for 6 h. B TEER detects the tightness of the BBB between the Aβ1-40 (100 nM and 1 µM)-treated pericyte si-CD36 coculture group and the control group after 6 h [*p < 0.05 in A and B compared with the same group, #p < 0.05 compared with the BEC single-layer model CTR group, Δp < 0.05 compared with the BEC/PC (A) or BEC/PC si-NC (B) coculture model CTR group, n = 3]. C The fluorescence microplate reader detects the normalized permeability of FITC-dextran after 1 µM Aβ1-40 treatment of the coculture model. D The fluorescence microplate reader detects the normalized permeability of FITC-Aβ1-40 after 1 µM Aβ1-40 treatment of the coculture model. (##p < 0.01 vs. the BEC/PC group, *p < 0.05 vs. the BEC/PC si-NC group, n = 3). BEC bEnd.3 is cultured alone, BEC/PC bEnd.3/pericyte coculture, si-NC empty vector control

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