Only activated fibroblasts, termed myofibroblasts, express α-smooth muscle actin and display levels of contractility, proliferation, and collagen synthesis that are enhanced compared to nonactivated fibroblast.
The activation of TLR2 and TLR4 activated renal fibroblasts to induce MCP-1/CCL2 and IL-6 mRNA within 24 hours while TGF-β, collagen-1α, and smooth muscle actin remained at baseline levels (Figure 8A).
Importantly, co-staining of p-STAT3 with smooth muscle marker proteins (α-smooth muscle actin) revealed high expression levels of p-STAT3 in neointimal SMCs and also of smooth muscle-like cells in the adventitial layer (Suppl. Fig. 1a).
We showed that an imbalance of actin levels in the skeletal muscle results in aggregates and muscle weakness.
When stained for smooth muscle actin (SMA) nonangiogenic vessels show greater levels of SMA than their less mature angiogenic counterparts.
XYXD treatment reduced CCl4-induced liver fibrosis and decreased hepatic hydroxyproline (Hyp) content, the mRNA levels of smooth muscle actin (α-SMA) and Col 1 α1) in fibrotic liver.
EMT tumors with a clearly distinguishable histological epithelial component also showed clear E-cadherin staining, whereas EMT tumors that predominantly consist of mesenchymal cells showed high levels of smooth muscle actin (SMA).
In an in vivo mouse model of hepatic fibrosis, 1 week of treatment with porcine relaxin-2 was reported to reduce collagen and smooth muscle actin content and significantly reduce serum levels of hepatic transaminases [ 77].
Furthermore, a greatly reduced vascular density was observed, along with higher levels of α-smooth muscle actin expression in stromal cells.
These epithelial changes were accompanied by increased levels of α-smooth muscle actin, vimentin and N-cadherin, and expression of transcriptional suppressors of E-cadherin (Snai1, Slug and Zeb2), and a mesenchymal metabolic protein (Dihydropyrimidine dehydrogenase).
