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. Author manuscript; available in PMC: 2021 Aug 1.
Published in final edited form as: Matrix Biol. 2020 Mar 12;90:79–108. doi: 10.1016/j.matbio.2020.02.004

Fig. 3. The production and assembly of fibrotic ECM PCS require fibronectin expression by LCs.

Fig. 3.

At 0 h PCS, only low levels of fibrotic ECM proteins (collagen I and tenascin C) and the enzymatic ECM crosslinker Lysyl oxidase (Lox) are detected in both WT and FNcKO LCs. Both WT and FNcKO LCs significantly upregulate collagen I protein expression by 48 h PCS (WT ***P ≤ 0.001; FNcKO ***P ≤ 0.001) although FNcKO LCs exhibit less association with collagen I fibrils compared to WT (**P ≤ 0.009). By 5 days PCS, WT LCs expressing αSMA are associated with a robust matrix of collagen I (***P ≤ 0.001) while this is absent in the area surrounding FNcKO lens cells (WT vs FNcKO ***P ≤ 0.001). Similarly, Lox protein upregulates in both WT and FNcKO LCs at 48 h PCS (WT **P = 0.004; FNcKO *P = 0.020) while this signal is much less pronounced in FNcKO LCs compared to WT (***P ≤ 0.001). There is a significant increase in tenascin C fibrils surrounding WT LCs both at 48 h (**P = 0.005) and 5 days (***P ≤ 0.001) PCS compared to 0 h PCS. However, FNcKO lens cells are associated with significantly less tenascin C fibrils both at 48 h PCS (***P ≤ 0.001) and 5 days PCS (***P ≤ 0.001) compared to WT. Collagen I, Tenascin C, and Lox (red), αSMA (green), are merged with DNA detected by Draq5 (blue). Scale bars: 35 μm. LC, remnant lens epithelial cells/lens cells; C, lens capsule. All experiments had N = 3. Values are expressed as mean ± SEM. Asterisks (*) indicate statistically significant MFI between WT and FNcKO at a PCS or between two PCS time points.