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Article
Perlecan: a Major IL-2-Binding Proteoglycan in Murine Spleen
Immunology and Cell Biology
  • John D. Miller
  • Elliot T. Stevens
  • Deandra R. Smith
  • Thomas N. Wight
  • Lucile E. Wrenshall, Wright State University - Main Campus
Document Type
Article
Publication Date
2-1-2008
Abstract
Although interleukin-2 (IL-2) is typically considered a soluble cytokine, our laboratory has shown that the availability of IL-2 in lymphoid tissues is regulated, in part, by an association with heparan sulfate glycosaminoglycan. Heparan sulfate is usually found in proteoglycan form, in which the heparan sulfate chains are covalently linked to a specific core protein. We now show that perlecan is one of the major IL-2-binding heparan sulfate proteoglycans in murine spleen. IL-2 binds perlecan via heparan sulfate chains, as enzymatic removal of heparan sulfate from splenic perlecan abolishes its ability to bind IL-2. Furthermore, we demonstrate that perlecan-bound IL-2 supports the proliferation of an IL-2-dependent cell line. Identification of perlecan as a major heparan sulfate proteoglycan that binds IL-2 has implications for both the localization and regulation of IL-2 in vivo.
DOI
10.1038/sj.icb.7100128
Citation Information
John D. Miller, Elliot T. Stevens, Deandra R. Smith, Thomas N. Wight, et al.. "Perlecan: a Major IL-2-Binding Proteoglycan in Murine Spleen" Immunology and Cell Biology Vol. 86 Iss. 2 (2008) p. 192 - 199 ISSN: 08189641
Available at: http://works.bepress.com/lucile_wrenshall/51/