In this study we have used several complementary techniques to isolate and characterize a 72-kD polypeptide that is tightly associated with a major mouse T-lymphoma membrane glycoprotein, gp 85 (a wheat germ agglutinin-binding protein), in a 16 S complex. These two proteins do not separate in the presence of high salt but can be dissociated by treatment with 2 M urea. Further analysis indicates that the 72-kD protein has ankyrin-like properties based on the following criteria: (a) it cross-reacts with specific antibodies raised against erythrocyte and brain ankyrin; (b) it displays a peptide mapping pattern and a pI (between 6.5 and 6.8) similar to that of the 72-kD proteolytic fragment of erythrocyte ankyrin; (c) it competes with erythrocyte ghost membranes (spectrin-depleted preparations) for spectrin binding; and (d) it binds to purified spectrin and fodrin molecules. Most importantly, in intact lymphoma cells this ankyrin-like protein is localized directly underneath the plasma membrane and is found to be preferentially accumulated beneath receptor cap structures as well as associated with a membrane-cytoskeleton complex preparation. It is proposed that the ankyrin-like 72-kD protein may play an important role in linking certain surface glycoprotein(s) to fodrin which, in turn, binds to actin filaments required for lymphocyte cap formation.
Article| June 01 1986
A lymphoma plasma membrane-associated protein with ankyrin-like properties.
L Y Bourguignon,
L Y Bourguignon
S J Suchard
Online ISSN: 1540-8140
Print ISSN: 0021-9525
J Cell Biol (1986) 102 (6): 2115–2124.
L Y Bourguignon, G Walker, S J Suchard, K Balazovich; A lymphoma plasma membrane-associated protein with ankyrin-like properties.. J Cell Biol 1 June 1986; 102 (6): 2115–2124. doi: https://doi.org/10.1083/jcb.102.6.2115
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