Recombinant Rat Chondroitin sulfate proteoglycan 4 (Cspg4), partial

Function

Proteoglycan playing a role in cell proliferation and migration which stimulates endothelial cells motility during microvascular morphogenesis. May also inhibit neurite outgrowth and growth cone collapse during axon regeneration. Cell surface receptor for collagen alpha 2(VI) which may confer cells ability to migrate on that substrate. Binds through its extracellular N-terminus growth factors, extracellular matrix proteases modulating their activity. May regulate MPP16-dependent degradation and invasion of type I collagen participating in melanoma cells invasion properties. May modulate the plasminogen system by enhancing plasminogen activation and inhibiting angiostatin. Also functions as a signal transducing protein by binding through its cytoplasmic C-terminus scaffolding and signaling proteins. May promote retraction fiber formation and cell polarization through Rho GTPase activation. May stimulate alpha-4, beta-1 integrin-mediated adhesion and spreading by recruiting and activating a signaling cascade through CDC42, ACK1 and BCAR1. May activate FAK and ERK1/ERK2 signaling cascades

Subcellular Location

Cell membrane (Single-pass type I membrane protein); Apical cell membrane (Single-pass type I membrane protein); Cell projection, lamellipodium membrane (Single-pass type I membrane protein); Cell surface

Tissue Specificity

Neural cells and also extraneural tissues, especially in the developing mesenchyme

Subunit

Interacts with GRIP1, GRIP2 and GRIA2. Forms a ternary complex with GRIP1 and GRIA2. Interacts with ITGA4 through its chondroitin sulfate glycosaminoglycan. Interacts with BCAR1, CDC42 and ACK1. Interacts with MMP16 (By similarity). Interacts with the first PDZ domain of MPDZ. Interacts with PRKCA. Interacts with LGALS3 and the integrin composed of ITGB1 and ITGA3. Binds TNC, laminin-1, COL5A1 and COL6A2. Interacts with PLG and angiostatin. Binds FGF2 and PDGFA

• Nishiyama A. et al. The primary structure of NG2, a novel membrane-spanning proteoglycan. — J. Cell Biol. (1991)
• Nishiyama A. et al. PubMed: CI-109FOPJ3GH1QR — J. Cell Biol. (1999)
• Leger O. et al. The chondroitin sulfate proteoglycan NG2 is a tumour-specific antigen on the chemically induced rat chondrosarcoma HSN. — Int. J. Cancer (1994)
• Stallcup W.B. et al. Interaction of the NG2 chondroitin sulfate proteoglycan with type VI collagen. — J. Cell Biol. (1990)
• Nishiyama A. et al. Expression of NG2 proteoglycan causes retention of type VI collagen on the cell surface. — Mol. Biol. Cell (1993)
• Nishiyama A. et al. Generation of truncated forms of the NG2 proteoglycan by cell surface proteolysis. — Mol. Biol. Cell (1995)
• Burg M.A. et al. Binding of the NG2 proteoglycan to type VI collagen and other extracellular matrix molecules. — J. Biol. Chem. (1996)
• Burg M.A. et al. A central segment of the NG2 proteoglycan is critical for the ability of glioma cells to bind and migrate toward type VI collagen. — Exp. Cell Res. (1997)