TUFTSIN-MACROPHAGE INTERACTION - SPECIFIC BINDING AND AUGMENTATION OF PHAGOCYTOSIS
TUFTSIN-MACROPHAGE INTERACTION - SPECIFIC BINDING AND AUGMENTATION OF PHAGOCYTOSIS
复制标题
DOI:
10.1002/jcp.1041000106
复制
发表时间:
1979-01-01
影响因子:
5.6
通讯作者:
FRIDKIN, M
中科院分区:
文献类型:
--
作者:
BARSHAVIT, Z;GOLDMAN, R;FRIDKIN, M
The binding of [3H]tuftsin to normal and in vivo stimulated mouse peritoneal macrophage populations was studied at 22.degree. C. The [3H]tuftsin binding to thioglycollate-stimulated macrophages was rapid and saturable, with an equilibrium Kd (calculated from a Scatchard plot) of 5.3 .times. 10-8 M. The calculated number of binding sites per macrophage amounts to approximately 72,000. Binding competition studies with unlabeled tuftsin yielded a Kd of 5.0 .times. 10-8 M. [3H] [N-Acetyl-Thr1] tuftsin, an inactive analog of tuftsin, failed to bind specifically to thioglycollate-stimulated macrophages. [N-Acetyl-Thr1]tuftsin and the tripeptide [Des-Arg4]tuftsin failed to compete for tuftsin binding sites, while [D-Arg4]tuftsin, an analog with small tuftsin-like activity, exhibited a low degree of inhibition of [3H]tuftsin binding. Thus a rather high degree of specificity is involved in the binding of the tetrapeptide. Normal as well as 6 different macrophage populations induced by stimulation with thioglycollate, concanavalin A, starch, mineral oil, glucan and BCG, exhibited a similar degree of binding of [3H]tuftsin. Corynebacterium parvum [Propionibacterium acnes] (CP)-stimulated macrophages showed a 6- to 10-fold-lower capacity for tuftsin binding. Under similar experimental conditions, mouse fibroblast and lymphocyte preparations revealed no detectable specific binding. Tuftsin augmented the phagocytic response of normal and stimulated macrophages assessed for phagocytosis mediated via the Fc-receptor and via non-specific receptors. CP-stimulated macrophages did not exhibit an increased phagocytic response upon treatment with tuftsin.