ADP‐ribosylation of tuftsin suppresses its receptor‐binding capacity and phagocytosis‐stimulating activity to murine peritoneal macrophages

FEBS Letters

Shimoyama, Makoto¹  Hara, Nobumasa¹  Terashima, Masaharu¹  Tsuchiya, Mikako¹  Badruzzaman, Muhammad¹ 

[1] Department of Biochemistry, Shimane Medical University, Izumo 693, Japan

关键词: ADP-ribosyltransferase (EC 2.4.2.31);    ADP-ribosylation;    Tuftsin;    Phagocytosis;    Macrophage;    GPI;    glycosyl-phosphatidylinositol;    EDTA;    ethylenediaminetetraacetic acid;    PMSF;    phenylmethanesulfonyl fluoride;    FITC;    fluorescein isothiocyanate;    PCA;    perchloric acid;    TFA;    trifluoroacetic acid;    TKPR;    tuftsin;   

DOI  :  10.1016/S0014-5793(97)00784-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 phagocytosis-stimulating tetrapeptide derived from leukokinin, as a preferential substrate of the enzyme in chicken plasma. Specific binding of FITC-tuftsin to murine peritoneal macrophages, observed under a fluorescent microscope, was impaired by ADP-ribosylation of the labelled peptide. Phagocytic assay analyzed by flow cytometry revealed that ADP-ribosylation of tuftsin decreased its phagocytosis-stimulating activity towards the macrophages. Thus, the ADP-ribosylation of tuftsin apparently decreases its biological activity and ADP-ribosylation may possibly be involved in inflammatory processes through alterations in tuftsin activity.

【 授权许可】

Unknown