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URL of this page: https://medlineplus.gov/genetics/gene/vcan/

VCAN gene

versican

Normal Function

The VCAN gene provides instructions for making a protein called versican core protein. Versican core protein is a large protein that is found in the extracellular matrix of many different tissues and organs. The extracellular matrix is the intricate lattice of proteins and other molecules that forms in the spaces between cells. Versican core protein interacts with these molecules to provide structure and support to the extracellular matrix. Within the eye, versican core protein helps maintain the gel-like consistency of the thick, clear fluid that fills the eyeball (the vitreous).

Researchers have proposed several additional functions for the versican core protein. This protein likely helps regulate the activity of several growth factors, which are proteins that play an important role in cell processes such as cell growth and division, cell maturation (differentiation), the attachment of cells to one another (cell adhesion), and cell movement (migration). Studies suggest that the versican core protein is also involved in wound healing, inflammation, forming new blood vessels (angiogenesis), and preventing the growth of cancerous tumors.

Several different versions (isoforms) of the versican core protein are produced from the VCAN gene. These isoforms vary in size and are found in different locations in the body.

Health Conditions Related to Genetic Changes

Wagner syndrome

Genetic changes that cause disease are called pathogenic variants. Pathogenic variants in the VCAN gene cause Wagner syndrome, a condition that is characterized by vision loss that worsens over time. Most of the pathogenic variants in the VCAN gene that cause Wagner syndrome disrupt the way the gene's instructions are used to make the versican core protein. These pathogenic variants typically occur in two areas of the gene called intron 7 and intron 8. Pathogenic variants in these regions lead to changes in the type and amount of the various isoforms that are produced within the vitreous. Researchers believe that having the wrong combination of versican core protein isoforms within the vitreous impairs the protein's ability to interact with other molecules. This disrupts the gel-like consistency of the vitreous, which affects the specialized light-sensitive tissue that lines the back of the eye (retina) and contributes to the vision problems that are characteristic of this condition. Researchers are working to to learn more about how pathogenic variants in the VCAN gene affect other tissues. 

More About This Health Condition

Other Names for This Gene

  • chondroitin sulfate proteoglycan 2
  • chondroitin sulfate proteoglycan core protein
  • CSPG2
  • PG-M
  • versican proteoglycan

Additional Information & Resources

Tests Listed in the Genetic Testing Registry

Scientific Articles on PubMed

Catalog of Genes and Diseases from OMIM

Gene and Variant Databases

References

  • Araujo JR, Tavares-Ferreira J, Estrela-Silva S, Rocha P, Brandao E, Faria PA, Falcao-Reis F, Rocha-Sousa A. WAGNER syndrome: anatomic, functional and genetic characterization of a Portuguese family. Graefes Arch Clin Exp Ophthalmol. 2018 Jan;256(1):163-171. doi: 10.1007/s00417-017-3800-0. Epub 2017 Oct 25. Citation on PubMed
  • Ghoraba HH, Sears J, Traboulsi EI. Hereditary Vitreoretinopathies: Molecular Diagnosis, Clinical Presentation and Management. Clin Exp Ophthalmol. 2025 Apr;53(3):281-291. doi: 10.1111/ceo.14494. Epub 2025 Jan 21. Citation on PubMed
  • Kloeckener-Gruissem B, Bartholdi D, Abdou MT, Zimmermann DR, Berger W. Identification of the genetic defect in the original Wagner syndrome family. Mol Vis. 2006 Apr 17;12:350-5. Citation on PubMed
  • Mukhopadhyay A, Nikopoulos K, Maugeri A, de Brouwer AP, van Nouhuys CE, Boon CJ, Perveen R, Zegers HA, Wittebol-Post D, van den Biesen PR, van der Velde-Visser SD, Brunner HG, Black GC, Hoyng CB, Cremers FP. Erosive vitreoretinopathy and wagner disease are caused by intronic mutations in CSPG2/Versican that result in an imbalance of splice variants. Invest Ophthalmol Vis Sci. 2006 Aug;47(8):3565-72. doi: 10.1167/iovs.06-0141. Citation on PubMed
  • Rahmani M, Wong BW, Ang L, Cheung CC, Carthy JM, Walinski H, McManus BM. Versican: signaling to transcriptional control pathways. Can J Physiol Pharmacol. 2006 Jan;84(1):77-92. doi: 10.1139/y05-154. Citation on PubMed
  • Ronan SM, Tran-Viet KN, Burner EL, Metlapally R, Toth CA, Young TL. Mutational hot spot potential of a novel base pair mutation of the CSPG2 gene in a family with Wagner syndrome. Arch Ophthalmol. 2009 Nov;127(11):1511-9. doi: 10.1001/archophthalmol.2009.273. Citation on PubMed or Free article on PubMed Central
  • Szeligowski T, Cehajic-Kapetanovic J, Raji S, Purohit R, Amin H, Patel CK, Xue K. Multimodal Evaluation and Management of Wagner Syndrome-Three Patients from an Affected Family. Genes (Basel). 2024 Sep 8;15(9):1178. doi: 10.3390/genes15091178. Citation on PubMed
  • Theocharis DA, Skandalis SS, Noulas AV, Papageorgakopoulou N, Theocharis AD, Karamanos NK. Hyaluronan and chondroitin sulfate proteoglycans in the supramolecular organization of the mammalian vitreous body. Connect Tissue Res. 2008;49(3):124-8. doi: 10.1080/03008200802148496. Citation on PubMed
  • Wight TN. Versican: a versatile extracellular matrix proteoglycan in cell biology. Curr Opin Cell Biol. 2002 Oct;14(5):617-23. doi: 10.1016/s0955-0674(02)00375-7. Citation on PubMed
  • Wu YJ, La Pierre DP, Wu J, Yee AJ, Yang BB. The interaction of versican with its binding partners. Cell Res. 2005 Jul;15(7):483-94. doi: 10.1038/sj.cr.7290318. Citation on PubMed

The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health.