TY - JOUR
T1 - T lymphocyte adhesion to the fibronectin and laminin components of the extracellular matrix is regulated by the CD4 molecule
AU - Hershkoviz, Rami
AU - Miron, Shmuel
AU - Cohen, Iran R.
AU - Miller, Ariel
AU - Lider, Ofer
PY - 1992/1
Y1 - 1992/1
N2 - The adhesion of T cells to components of the extracellular matrix (ECM) is mediated by the β1 subfamily of integrin receptors, designated VLA. It has been recently demonstrated that the binding of VLA receptors to protein components of the ECM is rapidly augmented by the activation of the T cells without, however, any actual change in the level of expression of the VLA receptors for fibronectin (FN) or laminin (LN). Thus, it is likely that activation of existing VLA receptors is required for binding. The activation must be regulated by T cell surface molecules capable of transducing signals into the cell. We studied the role of the CD4 molecule in the binding of rat CD4+ T cells to the FN and LN components of the ECM. We now report that the CD4 molecule appears to play a major role in regulating T cell interactions with ECM. This conclusion is based on the following observations: (a) monoclonal antibodies directed against the CD4 molecule inhibited T cell adhesion to both FN and LN; (b) down‐regulation of the CD4 molecule resulted in partial loss of the ability of CD4+ T cells to adhere to FN and LN; (c) a CD4+ T cell clone adhered to both FN and LN while a CD4−CD8− clone expressing an identical T cell receptor bound weakly to both proteins and (d) treatment of the CD4+ T cells with an inhibitor of the CD4‐associated tyrosine protein kinase activity inhibited T cell adhesion to both ECM proteins.
AB - The adhesion of T cells to components of the extracellular matrix (ECM) is mediated by the β1 subfamily of integrin receptors, designated VLA. It has been recently demonstrated that the binding of VLA receptors to protein components of the ECM is rapidly augmented by the activation of the T cells without, however, any actual change in the level of expression of the VLA receptors for fibronectin (FN) or laminin (LN). Thus, it is likely that activation of existing VLA receptors is required for binding. The activation must be regulated by T cell surface molecules capable of transducing signals into the cell. We studied the role of the CD4 molecule in the binding of rat CD4+ T cells to the FN and LN components of the ECM. We now report that the CD4 molecule appears to play a major role in regulating T cell interactions with ECM. This conclusion is based on the following observations: (a) monoclonal antibodies directed against the CD4 molecule inhibited T cell adhesion to both FN and LN; (b) down‐regulation of the CD4 molecule resulted in partial loss of the ability of CD4+ T cells to adhere to FN and LN; (c) a CD4+ T cell clone adhered to both FN and LN while a CD4−CD8− clone expressing an identical T cell receptor bound weakly to both proteins and (d) treatment of the CD4+ T cells with an inhibitor of the CD4‐associated tyrosine protein kinase activity inhibited T cell adhesion to both ECM proteins.
UR - http://www.scopus.com/inward/record.url?scp=0026604760&partnerID=8YFLogxK
U2 - 10.1002/eji.1830220103
DO - 10.1002/eji.1830220103
M3 - ???researchoutput.researchoutputtypes.contributiontojournal.article???
C2 - 1730261
AN - SCOPUS:0026604760
SN - 0014-2980
VL - 22
SP - 7
EP - 13
JO - European Journal of Immunology
JF - European Journal of Immunology
IS - 1
ER -