Identification and characterization of endogenous langerin ligands in murine extracellular matrix

Yayoi Tada, Elisabeth Riedl, Mark S. Lowenthal, Lance A. Liotta, David M. Briner, Erika C. Crouch, Mark C. Udey

Research output: Contribution to journalArticlepeer-review

15 Scopus citations

Abstract

Langerin is a C-type lectin that is expressed by Langerhans cells (LC) and related immune cells, and believed to play an important role in antigen recognition and uptake. To determine if Langerin has endogenous ligands, we generated S protein binding, bacterial recombinant, mouse soluble Langerin, and utilized it as a probe. Recombinant soluble Langerin did not bind to lymph node or spleen cells, or keratinocytes as assessed via flow cytometry. However, Langerin did bind to surfaces of primary skin fibroblasts and NIH3T3 cells. "Ligand blotting" of fibroblast membrane-enriched fractions with Langerin revealed reproducible binding to 140 and 240 kDa proteins resolved in reduced denaturing gels. Characterization of these proteins using mass spectrometry suggested types I and III procollagen and fibronectin as candidate ligands. Langerin bound to type I procollagen that was immunoprecipitated from fibroblast lysates, but did not bind to fibronectin that was immunoprecipitated from fibroblast-conditioned media or mouse plasma fibronectin. These results indicate that Langerin selectively interacts with at least one ligand in extracellular matrix (type I procollagen). Langerin may have an unanticipated role in cell-matrix interactions that modulate LC development, localization, or function.

Original languageEnglish
Pages (from-to)1549-1558
Number of pages10
JournalJournal of Investigative Dermatology
Volume126
Issue number7
DOIs
StatePublished - Jul 2006

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