Versican (chondroitin sulfate proteoglycan 2) is a large extracellular matrix proteoglycan involved in cell growth
and differentiation. Important as a structural molecule,
versican creates loose and hydrated matrices during key
events in development and disease. The protein contains
hyaluronic acid and glycosminoglycan-binding domains,
epidermal growth factor-like repeats, a Lectinlike
sequence and a complement regulatory protein-like
domain. Splice variants differ greatly in length and
degree of modification by glycoaminoglycan chains.
Accumulation around smooth muscle cells in lesions of
athero-sclerosis suggests a role for versican in
atherogenesis. Versican, differentially expressed in
human melanoma, plays a role in tumor development
and may be a reliable marker for clinical diagnosis. The
organization of HA- and versican-rich pericellular
matrices may faciliatate migration and mitosis by
diminishing cell surface adhesivity and affecting cell
shape through steric exclusion and the viscous properties of HA proteoglycan gels.