TY - JOUR
T1 - Tuftsin‐macrophage interaction
T2 - Specific binding and augmentation of phagocytosis
AU - Bar‐Shavit, Zvi
AU - Stabinsky, Yitzhak
AU - Fridkin, Mati
AU - Goldman, Rachel
PY - 1979/7
Y1 - 1979/7
N2 - The binding of [3H]tuftsin to normal and in vivo stimulated mouse peritoneal macrophage populations was studied at 22°C. The [3H]tuftsin binding to thioglycollate‐stimulated macrophages was shown to be rapid and saturable, with an equilibrium dissociation constant (KD) (calculated from a Scatchard plot) of 5.3 × 10−8 M. The calculated number of binding sites per macrophage amounts to approximately 72,000. Binding competition studies with unlabelled tuftsin yielded a KD of 5.0 × 10−8 M. [3H] [N‐Acetyl‐Thr1]tuftsin, an inactive analog of tuftsin, failed to bind specifically to thioglycollatestimulated 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 six different macrophage populations induced by stimulation with thioglycollate, concanavalin‐A, starch, mineral oil, glucan and Bacillus Calmette Guerrin (BCG), exhibited a similar degree of binding of [3H]tuftsin. Corynebacterium parvum (CP)‐stimulated macrophages, on the other hand, 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 both 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.
AB - The binding of [3H]tuftsin to normal and in vivo stimulated mouse peritoneal macrophage populations was studied at 22°C. The [3H]tuftsin binding to thioglycollate‐stimulated macrophages was shown to be rapid and saturable, with an equilibrium dissociation constant (KD) (calculated from a Scatchard plot) of 5.3 × 10−8 M. The calculated number of binding sites per macrophage amounts to approximately 72,000. Binding competition studies with unlabelled tuftsin yielded a KD of 5.0 × 10−8 M. [3H] [N‐Acetyl‐Thr1]tuftsin, an inactive analog of tuftsin, failed to bind specifically to thioglycollatestimulated 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 six different macrophage populations induced by stimulation with thioglycollate, concanavalin‐A, starch, mineral oil, glucan and Bacillus Calmette Guerrin (BCG), exhibited a similar degree of binding of [3H]tuftsin. Corynebacterium parvum (CP)‐stimulated macrophages, on the other hand, 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 both 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.
UR - http://www.scopus.com/inward/record.url?scp=0018760679&partnerID=8YFLogxK
U2 - 10.1002/jcp.1041000106
DO - 10.1002/jcp.1041000106
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C2 - 381320
AN - SCOPUS:0018760679
SN - 0021-9541
VL - 100
SP - 55
EP - 62
JO - Journal of Cellular Physiology
JF - Journal of Cellular Physiology
IS - 1
ER -