In 1989, Zimmermann and Ruoslahti cloned and sequenced the core protein of fibroblast chondroitin sulfate proteoglycan.

Versican belongs to the lectican protein family, with aggrecan (abundant in cartilage), brevican and neurocan (nervous system proteoglycans) as other members.

The N-terminal (G1) globular domain consists of Ig-like loop and two link modules, and has Hyaluronan (HA) binding properties.

The GAGs, being composed of repeating disaccharide units, contribute to the negative charge and many other properties of proteoglycans.

Expression of versican is observed in various adult tissues such as blood vessels, skin, and developing heart.

This interaction in the extracellular matrix or on the cell surface is important in the formation of immobilized gradients of these factors, their protection from proteolytic cleavage, and their presentation to specific cell-surface receptors.

Different tenascin domains interact with a wide range of cellular receptors, including integrins, cell adhesion molecules and members of the syndecan and glypican proteoglycan families.

In the adult central nervous system, versican is found in perineuronal nets, where it may stabilize synaptic connections.

Increased versican expression is often observed in tumor growth in tissues such as breast, brain,[10] ovary, gastrointestinal tract, prostate, and melanoma, sarcoma, and peritoneal mesothelioma.

A fifth isoform of versican, V4, that is similar to V1 but with a shortened beta-GAG region, is present and upregulated in human breast cancer.

[11] Versican is increased in the changing tissue extracellular matrix in inflammatory lung disorders such as chronic obstructive pulmonary disease (COPD), asthma and bronchiolitis obliterans syndrome (BOS).