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Physical association and functional interaction between beta1 integrin and CD98 on human T lymphocytesCD98 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-beta1 integrin specific mAb 18D3. These results indicated a functional association of CD98 and beta1 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-beta1 integrin mAb. Therefore, CD98-dependent lymphocyte proliferation and adhesion may involve integrins. Competitive binding assays and fluorescence colocalization analysis suggested that CD98 and beta1 integrin were physically associated. Differential extraction techniques and immunoprecipitations provided the first evidence that the alpha4beta1 integrin and CD98 are specifically associated on human T lymphocytes.
Document ID
20040087900
Acquisition Source
Legacy CDMS
Document Type
Reprint (Version printed in journal)
Authors
Miyamoto, Yuko J.
(The University of Texas M.D. Anderson Cancer Center 1515 Holcombe Blvd., Unit 180, Houston, TX 77030, United States)
Mitchell, Jason S.
McIntyre, Bradley W.
Date Acquired
August 21, 2013
Publication Date
January 1, 2003
Publication Information
Publication: Molecular immunology
Volume: 39
Issue: 12
ISSN: 0161-5890
Subject Category
Life Sciences (General)
Funding Number(s)
CONTRACT_GRANT: CA 62596
CONTRACT_GRANT: CA 09598
Distribution Limits
Public
Copyright
Other
Keywords
NASA Discipline Cell Biology
Non-NASA Center

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