PMID: 6976988Mar 1, 1982Paper

Ligand-induced association of surface immunoglobulin with the detergent-insoluble cytoskeletal matrix of the B lymphocyte

The Journal of Immunology : Official Journal of the American Association of Immunologists
J BraunE R Unanue

Abstract

Ligand binding is believed to induce surface immunoglobulin (Ig) to form a physical association with the underlying cell cytoskeleton. We investigated this interaction by use of nonionic detergents, which are known to dissolve membrane proteins but preserve a detergent-insoluble cytoskeletal residue. In the absence of ligand treatment, surface Ig in the B cell plasma membrane was fully dissolved by nonionic detergent; however, interaction with a ligand converted the receptor to a novel, detergent-insoluble state. The conversion of surface Ig to a detergent-insoluble form required receptor cross-linking but occurred independently of capping. Several types of experiments demonstrated that this form of Ig was not due to the size insolubility of immune complexes and involved a stable, noncovalent association of the receptor with the detergent-insoluble, cytoskeletal residue. Incubation of ligand-bound cells at 37 degrees C promoted the degradation of surface Ig and the appearance of new, lower m.w. species, including a major soluble protein (50,000 daltons) that was antigenically related to surface Ig. These events corresponded to receptor endocytosis by several criteria (time course, temperature sensitivity, and energy dependence)...Continue Reading

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