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Purified lymphocyte function-associated antigen 3 binds to CD2 and mediates T lymphocyte adhesion.

Open access
Dustin, M L, Sanders, M E, Shaw, S, Springer, T A·1987·The Journal of experimental medicine

Abstract

CD2 is a T lymphocyte glycoprotein that functions in adhesion of T lymphocytes and also as a putative receptor for activation signals. Functional data suggest that LFA-3, a widely distributed cell surface glycoprotein, may be the biological ligand of CD2. We have purified LFA-3 from human erythrocytes and characterized the purified protein functionally. LFA-3 bound specifically to CD2+ cells, and this binding was inhibited by CD2 mAb. Conversely, purified LFA-3 inhibited binding of CD2 mAb to cells, and the concentration required for this effect suggests that LFA-3 half-saturated CD2 at 1-5 nM LFA-3. Purified LFA-3 inhibited rosetting of human and sheep erythrocytes with CD2+ T lymphoma cells and T lymphocytes, and mediated aggregation of a CD2+ T lymphoma cell line. Purified LFA-3 reconstituted into planar membranes mediated efficient CD2-dependent adhesion of T lymphoblasts. These data demonstrate that LFA-3 is a ligand for CD2 and that LFA-3 can mediate T lymphocyte adhesion.

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Metadata

Authors
Dustin, M. L., Sanders, M. E., Shaw, S., & Springer, T. A.
Venue
The Journal of experimental medicine
Published
1987-03-01
Volume
165
Issue
3
Pages
677-692
ISSN
  • 0022-1007 (ISSN-L)
  • 1540-9538
OpenAlex
W2155740187
Cited by
253
References
0
FWCI
10.05
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Purified lymphocyte function-associated antigen 3 binds to CD2 and mediates T lymphocyte adhesion. https://app.cochat.ai/papers/10.1084/jem.165.3.677
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Dustin, M. L., Sanders, M. E., Shaw, S., & Springer, T. A. (1987). Purified lymphocyte function-associated antigen 3 binds to CD2 and mediates T lymphocyte adhesion. The Journal of experimental medicine. https://doi.org/10.1084/jem.165.3.677

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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