Am. Orourke et Mc. Lasam, MURINE CD4(-CELLS UNDERGO TCR-ACTIVATED ADHESION TO EXTRACELLULAR-MATRIX PROTEINS BUT NOT TO NONANTIGENIC MHC CLASS-II PROTEINS() T), The Journal of immunology, 155(8), 1995, pp. 3839-3846
Engagement of the TCR modulates the avidity of several receptors that
play key roles in lymphocyte adhesion and/or signal transduction, incl
uding CD8, CD11a/CD18 (LFA-1), CD2, and several beta 1-integrins. Here
, we investigated whether CD4(+) T cells similarly undergo TCR-regulat
ed adhesion to isolated MHC class II proteins through CD4. Strong adhe
sion of a number of CD4(+) T cell clones to immobilized antigenic pept
ide/class II complexes was readily detectable. Adhesion to antigenic c
lass II proteins was CD4; dependent and inhibited by pretreatment of T
cells with the protein tyrosine kinase inhibitor herbimycin A, sugges
ting that adhesion requires TCR- and/or CD4-derived signal transductio
n. Treatment of T cells with anti-TCR Ab strongly increased subsequent
adhesion to the extracellular matrix proteins, fibronectin and vitron
ectin, but, significantly, not to immobilized nonantigenic class II pr
oteins. Suboptimal densities of antigenic peptide/class II complexes a
lso activated,adhesion of T cells to coimmobilized fibronectin or vitr
onectin, and this resulted in production of IFN-gamma to levels exceed
ing those stimulated by optimal densities of antigenic class II comple
xes alone. However, no augmentation of adhesion or cytokine secretion
occurred when self or third party class II proteins were coimmobilized
with antigenic class II complexes. The present results, therefore, su
ggest fundamental differences in the mechanism by which the TCR regula
tes coreceptor adhesion in CD4(+) and CD8(+) T cells.