Versican

146213003ENSG00000038427ENSMUSG00000021614P13611Q86W61Q62059NM_004385NM_001126336NM_001164097NM_001164098NM_001081249NM_001134474NM_001134475NM_019389NM_172955NP_001119808NP_001157569NP_001157570NP_004376NP_001119808.1n/aVersican is a large extracellular matrix proteoglycan that is present in a variety of human tissues. It is encoded by the VCAN gene. Versican is a large extracellular matrix proteoglycan that is present in a variety of human tissues. It is encoded by the VCAN gene. Versican is a large chondroitin sulfate proteoglycan with an apparent molecular mass of more than 1000kDa. In 1989, Zimmermann and Ruoslahti cloned and sequenced the core protein of fibroblast chondroitin sulfate proteoglycan. They designated it versican in recognition of its versatile modular structure. Versican belongs to the lectican protein family, with aggrecan (abundant in cartilage), brevican and neurocan (nervous system proteoglycans) as other members. Versican is also known as chondroitin sulfate proteoglycan core protein 2 or chondroitin sulfate proteoglycan 2 (CSPG2), and PG-M. These proteoglycans share a homologous globular N-terminal, C-terminal, and glycosaminoglycan (GAG) binding regions. The N-terminal (G1) globular domain consists of Ig-like loop and two link modules, and has Hyaluronan (HA) binding properties. Versican occurs in 5 isoforms : V0, V1, V2, V3, V4.The central domain of versican V0 contains both the GAG-α and GAG-β domains. V1 isoforms has the GAG-β domain, V2 has the GAG-α domain, V3 is void of any GAG attachment domains and V4 has a portion of the GAG-β domain. The GAGs, being composed of repeating disaccharide units, contribute to the negative charge and many other properties of proteoglycans. The C-terminal (G3) globular domain consists of one or two Epidermal growth factor (EGF) repeats, a C-type lectin domain and complement regulatory protein (CRP)-like domain. The C-terminal domain binds a variety of ligands in ECM which contribute significantly to the functions of lecticans. The role of versican in cell adhesion, migration, and proliferation has been extensively studied. Versican is often considered an anti-adhesion molecule. Considering the large size (>1000 kDa) and hydration capability of versican, it is possible that the interaction of integrins (large family of cell adhesion molecules) with their cell surface receptors is sterically hindered.