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J. Biol. Chem., Vol. 266, Issue 16, 10241-10245, Jun, 1991
R Pulido, MJ Elices, MR Campanero, L Osborn, S Schiffer, A Garcia-Pardo, R Lobb, ME Hemler and F Sanchez-Madrid
The human integrin VLA (very late activation antigens)-4 (CD49d/CD29), the
leukocyte receptor for both the CS-1 region of plasma fibronectin (Fn) and
the vascular cell surface adhesion molecule-1 (VCAM-1), also mediates
homotypic aggregation upon triggering with specific anti-VLA-4 monoclonal
antibody (mAb). Epitope mapping of this integrin on the human B-cell line
Ramos, performed with a wide panel of anti-VLA-4 mAb by both
cross-competitive cell binding and protease sensitivity assays, revealed
the existence of three topographically distinct epitopes on the alpha 4
chain, referred to as epitopes A-C. By testing this panel of anti-VLA-4 mAb
for inhibition of cell binding to both a 38-kDa Fn fragment containing CS-1
and to VCAM-1, as well as for induction and inhibition of VLA-4 mediated
homotypic cell adhesion, we have found overlapping but different functional
properties associated with each epitope. Anti-alpha 4 mAb recognizing
epitope B inhibited cell attachment to both Fn and VCAM-1, whereas mAb
against epitope A did not block VCAM-1 binding and only partially inhibited
binding to Fn. In contrast, mAb directed to epitope C did not affect cell
adhesion to either of the two VLA-4 ligands. All mAb directed to site A, as
well as a subgroup of mAb recognizing epitope B (called B2), were able to
induce cell aggregation, but this effect was not exerted by mAb specific to
site C and by a subgroup against epitope B (called B1). Moreover, although
anti-epitope C and anti-epitope B1 mAb did not trigger aggregation, those
mAb blocked aggregation induced by anti- epitope A or B2 mAb. In addition,
anti-epitope A mAb blocked B2-induced aggregation, and conversely,
anti-epitope B2 mAb blocked A-induced aggregation. Further evidence for
multiple VLA-4 functions is that anti- Fn and anti-VCAM-1 antibodies
inhibited binding to Fn or to VCAM-1, respectively, but did not affect
VLA-4-mediated aggregation. In summary, we have demonstrated that there are
at least three different VLA-4-mediated adhesion functions, we have defined
three distinct VLA-4 epitopes, and we have correlated these epitopes with
the different functions of VLA-4.
Functional evidence for three distinct and independently inhibitable adhesion activities mediated by the human integrin VLA-4. Correlation with distinct alpha 4 epitopes
Seccion de Inmunologia, Hospital de la Princesa, Universidad Autonoma de Madrid, Spain.
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