Mature human thymocytes migrate on laminin-5 with activation of metalloproteinase-14 and cleavage of CD44

J Immunol. 2004 Feb 1;172(3):1397-406. doi: 10.4049/jimmunol.172.3.1397.

Abstract

We have previously shown that laminin-5 is expressed in the human thymic medulla, in which mature thymocytes are located. We now report that laminin-5 promotes migration of mature medullary thymocytes, whereas it has no effect on cortical immature thymocytes. Migration was inhibited by blocking mAbs directed against laminin-5 integrin receptors and by inhibitors of metalloproteinases. Interactions of thymocytes with laminin-5 induced a strong up-regulation of active metalloproteinase-14. However, we found that thymocytes did not cleave the laminin-5 gamma(2) chain, suggesting that they do not use the same pathway as epithelial cells to migrate on laminin-5. Interactions of thymocytes with laminin-5 also induced the release of a soluble fragment of CD44 cell surface molecule. Moreover, CD44-rich supernatants induced thymocyte migration in contrast with supernatants depleted in CD44 by immunoadsorption. CD44 cleavage was recently reported to be due to metalloproteinase-14 activation and led to increased migration in cancer cells. Thus, in this study, we show that laminin-5 promotes human mature thymocyte migration in vitro via a multimolecular mechanism involving laminin-5 integrin receptors, metalloproteinase-14 and CD44. These data suggest that, in vivo, laminin-5 may function in the migration of mature thymocytes within the medulla and be part of the thymic emigration process.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Adhesion Molecules / physiology*
  • Cell Communication / immunology
  • Cell Differentiation / immunology
  • Cell Movement / immunology*
  • Cells, Cultured
  • Enzyme Activation / immunology
  • Humans
  • Hyaluronan Receptors / metabolism*
  • Hyaluronan Receptors / physiology
  • Hydrolysis
  • Immunophenotyping
  • Infant
  • Integrin alpha3beta1 / physiology
  • Integrin alpha6beta4 / physiology
  • Kalinin
  • Laminin / metabolism
  • Matrix Metalloproteinases, Membrane-Associated
  • Metalloendopeptidases / metabolism*
  • Metalloendopeptidases / physiology
  • Peptide Fragments / metabolism
  • Protein Processing, Post-Translational / immunology
  • Protein Subunits / metabolism
  • Solubility
  • T-Lymphocyte Subsets / cytology*
  • T-Lymphocyte Subsets / enzymology
  • T-Lymphocyte Subsets / immunology
  • T-Lymphocyte Subsets / metabolism*
  • Thymus Gland / cytology*
  • Thymus Gland / enzymology
  • Thymus Gland / immunology
  • Thymus Gland / metabolism*

Substances

  • Cell Adhesion Molecules
  • Hyaluronan Receptors
  • Integrin alpha3beta1
  • Integrin alpha6beta4
  • LAMC2 protein, human
  • Laminin
  • Peptide Fragments
  • Protein Subunits
  • Matrix Metalloproteinases, Membrane-Associated
  • Metalloendopeptidases