The collateral damage of the metalloproteinase/toxicity-removal process is the degraded fragments of ECM constituents such as hyaluronic acid, teanscin-c, decorin,
biglycan, and aggrecan.
(23) in a study on human pancreatic carcinoma cells observed that DPI (a pharmacological inhibitor of Noxs) suppressed TGF-[beta]-induced
biglycan expression and p38 activation.
Immunohistochemical localization of the proteoglycans decorin,
biglycan and versican and transforming growth factor-beta in human post-burn hypertrophic and mature scars.
(iii) Expression of tendon specific ECM (type I collagen, type III collagen, decorin, tenascin-C, and
biglycan) was significantly higher at 14 days in the nanoyarn group.
These include the subgroup lecticans (comprising aggrecan, brevican, versican, and neurocan), small leucine-rich proteoglycans (including
biglycan and decorin), phosphacan/ receptor-type-protein-tyrosine phosphatase [beta] (RPTP[beta]), and other proteoglycans, including NG2 and neuroglycanC [159].
Moreover,
biglycan, a kind of leucine-rich repeat proteoglycan, can also activate NLRP3 inflammasomes through interaction with TLR2/4 and purine P2X4/P2X7 receptors on macrophages [32].
Studies of cartilage explants report decreases in the density of glycosaminoglycan within the proteoglycan molecule, decreases in aggrecan molecule size and density, and increases in cartilage matrix degradation products such as low molecular weight hyaluronic acid and
biglycan (25).
(7) In trigger finger tendons, collagen type 1A1 and 3A1, aggrecan, and
biglycan are up-regulated, while metalloproteinase inhibitor 3 (TIMP-3) and matrix metallopeptidase (3) (MMP-3) are down-regulated, a situation also described in Achilles tendinosis.