IL-7 activates α4β1 integrin in murine thymocytes

Haruki Kitazawa, Kathrin Muegge, Raffaele Badolato, Ji Ming Wang, William E. Fogler, Douglas K. Ferris, Chong Kil Lee, Serge Candéias, Mark R. Smith, Joost J. Oppenheim, Scott K. Durum

Research output: Contribution to journalArticlepeer-review

42 Citations (Scopus)


IL-7, a cytokine produced by thymic epithelium, was shown to induce adhesion of murine thymocytes to gelatin-coated membranes. A major binding component of gelatin was identified as fibronectin. IL-7-induced adhesion was observed for all of the major thymocyte subsets, including double-negative, double-positive, and single-positive cells, and specific IL-7R were verified on each subset. Fibronectin binding was mediated via α4β1 integrin (VLA-4), which is expressed at high levels on thymocytes. VLA-4 surface expression was not increased following IL-7 treatment, but was shown to undergo rapid tyrosine phosphorylation on the β1 subunit. This tyrosine phosphorylation was blocked by genistein, which also blocked IL-7-induced adhesion. IL-7 was detected on the extracellular matrix of the thymus, suggesting that it could promote matrix association through an integrin pathway.

Original languageEnglish
Pages (from-to)2259-2264
Number of pages6
JournalJournal of Immunology
Issue number5
Publication statusPublished - 1997


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