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J. Biol. Chem., Vol. 262, Issue 24, 11478-11485, Aug, 1987
ME Hemler, C Huang, Y Takada, L Schwarz, JL Strominger and ML Clabby
A monoclonal antibody (B-5G10) was produced which specifically recognizes
the Mr 150,000/130,000 VLA-4 complex on the surface of human cells.
Cross-linking studies indicated that the Mr 150,000 alpha 4 subunit of
VLA-4 is in noncovalent 1:1 association with the Mr 130,000 VLA beta
subunit. In the absence of cross-linking, the VLA-4 alpha 4 beta subunit
complex was easily dissociated, especially in Nonidet P-40 detergent, or at
elevated pH (above 8.0). Studies of dissociated subunits showed that B-5G10
recognizes an epitope on the Mr 150,000 alpha 4 subunit of VLA-4, whereas
the beta subunit is immunologically identical to the Mr 130,000 beta
subunit common to all VLA heterodimers. VLA-4 is widely distributed on
hematopoietic cells, including thymocytes, peripheral blood lymphocytes,
monocytes, activated T cells, T and B lymphoblastoid cell lines, and
myeloid cell lines. However, VLA-4 is only weakly expressed on most
adherent cell lines tested. Immunoprecipitates of VLA-4 often contain
additional proteins of Mr 80,000 and Mr 70,000. These are probably derived
from the Mr 150,000 alpha 4 subunit because: 1) they are both recognized by
anti-alpha 4 sera, but not anti-beta sera; 2) the sum of their sizes is
equal to the size of alpha 4; 3) they are selectively coexpressed with
alpha 4 and not other VLA alpha subunits; 4) the Mr 80,000 protein has an
identical NH2-terminal sequence to alpha 4; 5) like alpha 4, the Mr 70,000
and 80,000 peptides can variably associate with the VLA beta subunit; and
6) trypsin appears to cleave the Mr 150,000 alpha 4 subunit into products
of Mr 70,000 and 80,000.
Characterization of the cell surface heterodimer VLA-4 and related peptides
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