Receptor-mediated internalization of tuftsin by human polymorphonuclear leukocytes.
AuthorsAmoscato AA, Davies PJ, Babcock GF, Nishioka K
JournalJ Reticuloendothel Soc
PubMed ID6308252
'A high-performance liquid chromatography (HPLC) purified fluorescein-labeled analogue of tuftsin was prepared, which retains the full biological activity of the native molecule. Characterization of the derivatization site by amino acid analysis, N-terminal cleavage, and dansylation revealed a monofluorescinated derivative at the alpha-amino terminus. Binding of the fluorescent tuftsin to living ... More
Receptor-mediated internalization of tuftsin.
AuthorsAmoscato AA, Davies PJ, Babcock GF, Nishioka K
JournalAnn N Y Acad Sci
PubMed ID6324633
ADP-ribosylation of tuftsin suppresses its receptor-binding capacity and phagocytosis-stimulating activity to murine peritoneal macrophages.
AuthorsTerashima M, Hara N, Badruzzaman M, Shimoyama M, Tsuchiya M
JournalFEBS Lett
PubMed ID9257725
Arginine-specific ADP-ribosyltransferase present in granules of chicken polymorphonuclear leukocytes (so-called heterophils) is released into the extracellular space by stimulus of calcium ionophore A23187 or opsonized zymosan [Terashima et al. (1996) J. Biochem. 120, 1209-1215]. In the present work, we examined extracellular targets of the released transferase and identified tuftsin, a ... More
Stimulation of phagocytic activity of murine Kupffer cells by tuftsin.
AuthorsKubo S, Rodriguez T, Roh MS, Oyedeji C, Romsdahl MM, Nishioka K
JournalHepatology
PubMed ID8138244
Tuftsin (Thr-Lys-Pro-Arg) is a natural immunomodulating peptide. We have investigated for the presence of a specific tuftsin receptor on murine Kupffer cells using fluorescein-labeled tuftsin, which retains full biological activity. After incubation with fluorescein-labeled tuftsin, Kupffer cells displayed clear binding of this compound on the plasma membrane. Excess tuftsin inhibited ... More