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.
In addition, (S)-[6]-Gingerol is proposed as an anti-atherosclerotic agent due to its ability to inhibit
biglycan synthesis, which is an early mediator of lipid binding in atherosclerosis (Kamato et al.
HTRA1 is responsible for degradation of pericellular matrix components, including fibronectin, matrilin 3, collagenoligometric matrix protein,
biglycan, fibromodulin, and type VI collagen [25].
The ground substance contains glycosaminoglycans like dermatan sulphate and hyaluronic acid, the proteoglycans like decorin and
biglycan.
2) The cartilage tissue of the patients with osteoarthritis and rheumatoid arthritis include
biglycan fragments obtained due to breakdown of proteoglycans by ADAMTSs.
Asporin is a member of the sub family of small leucine-rich proteoglycans that also includes decorin and
biglycan.
Research provides ample evidence that Small Leucine-Rich Proteoglycans (SLRPs) such as decorin,
biglycan, fibromodulin, and lumican in the extracellular matrix are deeply involved in the regulation of inflammatory and fibrotic renal disorders and are the binding partners of [TGF-[beta].
A second group includes proteoglycans containing leucine-rich repeat domains, such as decorin,
biglycan, fibromodulin and kerotocan, The leucine-rich domains of these proteoglycans mediate protein-protein interactions, contributing to the organization of the collagen network.
3)
Biglycan and decorin belong to the family of small leucine-rich proteoglycans (SLRPs).
They also found significant increased mRNA expression of extracellular matrix proteins
biglycan and decorin and concluded that PRP appears to enhance the healing of meniscal defects.
The key protein
Biglycan restores the muscle-strengthening presence of a protein called utrophin, which is normally prevalent only in very young children.
