A novel peptide sequence in perlecan domain IV supports cell adhesion, spreading and FAK activation.

Perlecan/HSPG2 is a large, multi-domain, multifunctional heparan sulfate proteoglycan with a wide tissue distribution. With the exception of its unique domain I, each of perlecan's other four domains shares sequence similarity to other protein families including low density lipoprotein (LDL) receptor, laminin alpha chain, neural cell adhesion molecule (NCAM), immunoglobulin (Ig) superfamily members, and epidermal growth factor (EGF). Previous studies demonstrated that glycosaminoglycan-bearing perlecan domain I supports early chondrogenesis and growth factor delivery.

Chondrogenic differentiation on perlecan domain I, collagen II, and bone morphogenetic protein-2-based matrices.

Extracellular matrix (ECM) molecules in cartilage cooperate with growth factors to regulate chondrogenic differentiation and cartilage development. Domain I of perlecan (Pln) bears heparan sulfate chains that bind and release heparin binding growth factors (HBGFs). We hypothesized that Pln domain I (PlnDI) might be complexed with collagen II (P-C) fibrils to improve binding of bone morphogenetic protein-2 (BMP-2) and better support chondrogenesis and cartilage-like tissue formation in vitro.

Heparan sulfate proteoglycans: coordinators of multiple signaling pathways during chondrogenesis.

Heparan sulfate proteoglycans are abundantly expressed in the pericellular matrix of both developing and mature cartilage. Increasing evidence indicates that the action of numerous chondroregulatory molecules depends on these proteoglycans. This review summarizes the current understanding of the interactions of heparan sulfate chains of cartilage proteoglycans with both soluble and nonsoluble ligands during the process of chondrogenesis.

HIP/RPL29 down-regulation accompanies terminal chondrocyte differentiation.

HIP is a heparin/heparan sulfate (Hp/HS) binding protein identical to ribosomal protein L29 that displays diverse biological functions. There is strong evidence that abnormal expression and quantitative deficiencies of essential molecules such as extracellular matrix (ECM) proteins, transcription factors, and ribosomal proteins can seriously impair embryonic development. As observed for HS-bearing molecules, high levels of HIP/RPL29 are found in proliferating chondrocytic precursors and chondrocytes of developing growth plate.