Physical association and functional interaction between β1 integrin and CD98 on human T lymphocytes

Yuko J. Miyamoto, Jason S. Mitchell, Bradley W. McIntyre

Research output: Contribution to journalArticlepeer-review

26 Scopus citations

Abstract

CD98 is a cell surface protein previously characterized as a cell activation marker, an amino acid transporter, and has recently been implicated in integrin-related functions. Integrins are cell surface proteins, important for homotypic cell aggregation, cell adhesion, and coactivation of T lymphocytes. We have previously shown that the anti-CD98 mAb 80A10, when coimmobilized with anti-CD3 mAb OKT3, is able to mediate human T cell coactivation that is inhibited by anti-β1 integrin specific mAb 18D3. These results indicated a functional association of CD98 and β1 integrin signaling but left open the question of a physical association. We now show the induction of homotypic aggregation through CD98 among human T cells and this aggregation was inhibited by anti-β1 integrin mAb. Therefore, CD98-dependent lymphocyte proliferation and adhesion may involve integrins. Competitive binding assays and fluorescence colocalization analysis suggested that CD98 and β1 integrin were physically associated. Differential extraction techniques and immunoprecipitations provided the first evidence that the α4β1 integrin and CD98 are specifically associated on human T lymphocytes.

Original languageEnglish (US)
Pages (from-to)739-751
Number of pages13
JournalMolecular Immunology
Volume39
Issue number12
DOIs
StatePublished - Jan 2003

Bibliographical note

Funding Information:
This work was supported by National Institutes of Health grant CA62596, NASA NAG 2-1505, and the Predoctoral Cancer Immunobiology Training Program Grant CA09598.

Keywords

  • Adhesion molecules
  • Cell surface molecules
  • Cellular activation
  • Human
  • T lymphocytes

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