title: Domains of receptor mobility and endocytosis in the membranes of neonatal human erythrocytes and reticulocytes are deficient in spectrin.
abstract: It has previously shown (Schekman, R., and S.J. Singer, Proc. Natl. Acad. Sci. U.S.A. 73:4075-4079) that receptors in the membranes of neonatal human erythrocytes show a restricted degree of lateral mobility, whereas in adult human erythrocytes the receptors are essentially immobile. This restricted mobility is exhibited, for example, when concanavalin A (Con A) induces a limited clustering of its receptors in the neonatal erythrocyte membrane, resulting in the formation of invaginations and endocytic vesicles. This does not happen with adult cells. By the use of indirect immunoferritin labeling of ultrathin frozen sections of Con A-treated neonatal blood cells, we now show that the invaginations and endocytotic vesicles do not stain for spectrin, whereas the adjacent unperturbed membrane is heavily stained. The reticulocytes in the neonatal cell population undergo substantially more Con A-induced invagination and endocytosis than do the erythrocytes. These results lend strong support to the hypothesis that specialized discrete domains exist, or are induced, in the membranes of these neonatal cells, in which receptors are laterally mobile, whereas in the remaining (and predominant) part of the membrane the receptors are immobile. Such mobile domains are characterized by an absence of spectrin. During the maturation of the neonatal reticulocyte to erythrocyte, it is proposed that these domains are in large part, but not completely, eliminated.
mesh_terms: D003208:Concanavalin A / Q000494:pharmacology; D004705:Endocytosis / Q000187:drug effects; D004910:Erythrocyte Membrane / Q000187:drug effects / Q000648:ultrastructure*; D004912:Erythrocytes / Q000648:ultrastructure*; D005312:Fetal Blood / Q000166:cytology*; D006801:Humans; D007231:Infant, Newborn; D008565:Membrane Proteins / Q000032:analysis*; D011952:Receptors, Concanavalin A / Q000032:analysis* / Q000187:drug effects; D011955:Receptors, Drug / Q000032:analysis*; D012156:Reticulocytes / Q000648:ultrastructure*; D013049:Spectrin / Q000032:analysis*
chemical_list: D008565:Membrane Proteins; D011952:Receptors, Concanavalin A; D011955:Receptors, Drug; D003208:Concanavalin A; D013049:Spectrin