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Second, rosetting still occurs with erythrocytes genetically deficient in CD44(127). CD44is associated with ankyrin in murine lymphocytes and maytherefore associate with the erythrocyte membraneskeleton (130). In one scenario, cross-linking CD44maydecrease the deformability oferythrocytes which could inhibit adhesion by limiting the area of contact between T lymphocyte and erythrocyte. Finally, mAbto a glycoprotein of 32 kd partially inhibit humanthymocyte rosetting with sheep or human erythrocytes by binding to thymocytes (131).

Hydrophilic, recombinant CD2binds LFA-3on B lymphoblastoidcells with a Ko---- 4 × 10- 7 M(114). Similarly, a water-soluble monomericform of LFA-3generated by enzymatic cleavage blocks adhesion with an IC(50) -- 10-6 M(115). In contrast to these hydrophilic forms, in the absence of detergent, purified LFA-3with an intact hydrophobic anchor aggregates to form octameric protein micelles (l 15). Purified intact CD2also probably aggregates in solution, although the form taken by CD2in solution has not been characterized (20, 28).

In contrast, ICAM-1÷ lymphocytes showsignificant adhesion to purified LFA-1in planar membranesat 4°C, as well as 37°C (5). Thus, there is evidence for sidedness of temperature requirements for the LFA1/ICAM mechanism. " Similarities between family membersinclude not only structural features, but functional characteristics and an understanding of these relationships form the basis for our subsequentdiscussion of adhesion receptors. CD2, LFA-3, and ICAMsin the Immunoglobulin Super family The primary structures of CD2, LFA-3, and both ICAMsresemble those of the immunoglobulinsuperfamily, a functionally diverse family of molecules manyof which are expressed on the cell surface.

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