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Il-7 Activates Alpha(4)Beta(1) Integrin in Murine Thymocytes

  1. Author:
    Kitazawa, H.
    Muegge, K.
    Badolato, R.
    Wang, J. M.
    Fogler, W. E.
    Ferris, D. K.
    Lee, C. K.
    Candeias, S.
    Smith, M. R.
    Oppenheim, J. J.
    Durum, S. K.

  2. Author Address

    Durum SK NCI MOL IMMUNOREGULAT LAB FREDERICK CANC RES FACIL NIH BLDG 560 ROOM 31-45 FREDERICK, MD 21702 USA NCI MOL IMMUNOREGULAT LAB FREDERICK CANC RES FACIL NIH FREDERICK, MD 21702 USA NCI SCI APPLICAT INT CORP NIH FREDERICK, MD 21702 USA NCI EXPT IMMUNOL LAB NIH FREDERICK, MD 21702 USA
    1. Year: 1997
  2. Journal: Journal of Immunology
    1. 159
    2. 5
    3. Pages: 2259-2264
  4. Type of Article: Article
  1. Abstract:

    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 alpha(4) beta(1) 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 beta(1) 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. [References: 25]

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