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August 1, 1981The Journal of Immunology

A novel lymphocyte function-associated antigen (LFA-1): cellular distribution, quantitative expression, and structure.

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Authors

KKK. KürzingerTechnische Universität IlmenauTRTim ReynoldsCalifornia Institute of TechnologyRGR N GermainNational Institutes of Health

Discussion

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Implication

Laboratory study demonstrates the selective expression and heterodimeric structure of LFA-1 in murine lymphoid cells, indicating its distinct role in cytotoxic T cell-mediated immune responses.

Key Points

  • Characterize the cellular distribution, surface abundance, and molecular structure of the novel lymphocyte function-associated antigen 1 (LFA-1) identified by the M7/14 monoclonal antibody.
  • Assessed LFA-1 distribution across murine T and B cell lineages, bone marrow cells, exudate macrophages, and nonlymphoid tissues using the M7/14 monoclonal antibody.
  • Quantified surface binding sites per cell on unstimulated spleen cells and cytolytic T lymphocyte preparations (CTLP) in comparison with H-2, Thy-1, and Lyt-2 markers.
  • Analyzed the biochemical structure and molecular weight composition of the LFA-1 antigen using protein characterization techniques.
  • LFA-1 was present on T and B lymphocytes and a substantial fraction of bone marrow cells, but was completely absent on exudate macrophages and nonlymphoid tissues.
  • Binding assays revealed approximately 1.5 × 10⁴ LFA-1 sites per spleen cell and 7.0 × 10⁴ sites per CTLP cell, binding in quantities 2.5-fold and 10.4-fold lower than H-2 and Thy-1 despite specifically blocking cytolytic activity.
  • Structural analysis identified LFA-1 as a glycoprotein consisting of two noncovalently associated polypeptide chains with molecular weights of 180,000 and 95,000 Mr.

Cite This Study

Kürzinger et al. (1981) studied this question.

synapsesocial.com/papers/6a6fbe88439bab0cabc2e637https://doi.org/10.4049/jimmunol.127.2.596
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