STUDIES OF THE HUMAN LYMPHOCYTE MOUSE ERYTHROCYTE BOND

  • 1 January 1979
    • journal article
    • research article
    • Vol. 36  (3) , 536-546
Abstract
A subpopulation of human B[bone marrow-derived] lymphocytes formed rosettes with mouse erythrocytes through a glycoprotein-dependent bond. Further studies of this bond showed that the lymphocyte receptor was not immunoglobulin [Ig], although the binding of antisera or staphylococci to surface Ig inhibited the formation of mouse rosettes. Rosette formation could not be induced in thymocytes by enzymatic modification of the surface, or in T [thymus-derived] cells by lectin-induced transformation. The capacity to bind mouse erythrocytes was lost after incubation in a serum-free medium of lymphocytes from most patients with chronic lymphocytic leukemia (CLL) and normal subjects. This loss could be prevented by the addition of a variety of sera and glycoprotein-containing substances to the medium, including fetuin. Conditions conducive to the subsequent restoration of rosetting capacity could not be found, indicating that the loss of this capacity was not due to the shedding of a cell-surface receptor which could be re-synthesized. The functional receptors in B1 lymphocytes are apparently held in aggregates by cross-linking peripheral glycoprotein molecules. Disaggregation and consequent loss of the capacity to form rosettes with mouse erythrocytes occurred during incubation in serum-free media, and during maturation of lymphocytes to the B2 stage.