After removal of very late antigen (VLA) 2 material from a radiolabeled detergent lysate of platelets, another VLA heterodimer was precipitated using antibody to the common VLA beta subunit. This structure was identified as VLA-5 because it contained VLA beta plus an alpha subunit that was (i) recognized by anti-alpha 5 antibodies and (ii) cleaved by V8 protease to yield a characteristic alpha 5-like pattern of peptide fragments. Besides VLA-2 and VLA-5, a third heterodimer, here named VLA-6, was also present on platelets. VLA-6 (an alpha 6 beta complex) was defined using the monoclonal antibody GoH3 (Sonnenberg, A., Janssen, H., Hogervorst, F., Calafat, J., and Hilgers, J. (1987) J. Biol. Chem. 262, 10376-10383). Although it resembled VLA-5 in size, VLA-6 was different from VLA-5 because (i) removal of the alpha 5 subunit did not remove alpha 6, (ii) removal of alpha 6 by the GoH3 antibody did not remove alpha 5, (iii) the alpha 5 and alpha 6 subunits had very distinct one-dimensional V8 peptide maps, and (iv) the alpha 6 and alpha 5 subunits had distinct migration patterns on two-dimensional O'Farrell gels. The beta subunit of VLA-6 was identified as the common VLA beta subunit because (i) it was recognized by anti-VLA beta antibody and (ii) it yielded a V8 protease cleavage map characteristic of beta. VLA-6 was not readily seen in anti-VLA beta immunoprecipitations, apparently because the alpha 6 subunit is only loosely or partially associated with the VLA beta subunit. Because VLA-5 and VLA-6 both closely resemble the previously defined Ic-IIa platelet protein complex, it is likely that there is more than one platelet "Ic" protein complexed with IIa.
|Original language||English (US)|
|Number of pages||6|
|Journal||Journal of Biological Chemistry|
|State||Published - Jun 5 1988|
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