LFA-1-mediated Adhesion Is Regulated by Cytoskeletal Restraint and by a Ca2+-dependent Protease, Calpain

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J. Cell Biol., Volume 140, Number 3, February 9, 1998 699-707

LFA-1-mediated Adhesion Is Regulated by Cytoskeletal Restraint and by a Ca²⁺-dependent Protease, Calpain

Mairi P. Stewart, Alison McDowall, and Nancy Hogg

Leukocyte Adhesion Laboratory, Imperial Cancer Research Fund, Lincoln's Inn Fields, London WC2A 3PX, United Kingdom

The activity of integrins on leukocytes is kept under tight control to avoid inappropriate adhesion while these cells arecirculating in blood or migrating through tissues. Using lymphocytefunction-associated antigen-1 (LFA-1) on T cells as a model, wehave investigated adhesion to ligand intercellular adhesion molecule-1induced by the Ca²⁺ mobilizers, ionomycin, 2,5-di-t-butylhydroquinone, and thapsigargin,and the well studied stimulators such as phorbol ester and cross-linkingof the antigen-specific T cell receptor (TCR)- CD3 complex. Wereport here that after exposure of T cells to these agonists,integrin is released from cytoskeletal control by the Ca²⁺-induced activation of a calpain-like enzyme, and adhesive contactbetween cells is strengthened by means of the clustering of mobilizedLFA-1 on the membrane. We propose that methods of leukocyte stimulationthat cause Ca²⁺ fluxes induce LFA-1 adhesion by regulation of calpain activity.These findings suggest a mechanism whereby engagement of the TCRcould promote adhesion strengthening at an early stage of interactionwith an antigen-presenting cell.

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