caa a22 4500 397555474 CHVBK 20180308164800.0 cr unu---uuuuu 161202e199612 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021543 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021543 Exocytosis of Arginine-Specific ADP-Ribosyltransferase and p33 Induced by A23187 and Calcium or Serum-Opsonized Zymosan in Chicken Polymorphonuclear Leukocytes [Elektronische Daten] [Masaharu Tarashima, Muhammad Badruzzaman, Mikako Tsuchiya, Makoto Shimoyama] Exocytosis is a common phenomenon in neutrophil functions. We earlier reported the co-localization of arginine-specific ADP-ribosyltransferase [EC 2.4.2.31] and its target protein p33 (mim-1 protein) in cytoplasmic granules in chicken polymorphonuclear leukocytes (so-called heterophils) [Mishima, K., Terashima, M., Obara, S., Yamada K., Imai, K., and Shimoyama, M. (1991) J. Biochem. 110, 388-394]. In the present study, we obtained evidence that the transferase and p33 were released Into the extracellular space by the stimulus of calcium ionophore A23187 or serum-opsonized zymosan, but scarcely by phorbol myristate acetate (PMA) or N-formyl-Met-Leu-Phe (fMLP), thereby indicating the co-localization of the transferase and p33 in the azurophilic granules, and not in specific granules. [32P] ADP-ribosylation of p33 occurred in the extracellular space, induced by the stimulus of A23187 or opsonized zymosan in the presence of [32P]NAD Our findings are interpreted to mean that heterophil transferase and p33 may be involved in neutrophil functions during processes of inflammation. © 1996 BY THE JOURNAL OF BIOCHEMISTRY Regular Papers nationallicence ADP-ribosyltransferase nationallicence calcium nationallicence exocytosis nationallicence polymorphonuclear leukocytes nationallicence zymosan nationallicence Tarashima Masaharu Department of Biochemistry, Shimane Medical University, Izumo 693 aut Badruzzaman Muhammad Department of Biochemistry, Shimane Medical University, Izumo 693 aut Tsuchiya Mikako Department of Biochemistry, Shimane Medical University, Izumo 693 aut Shimoyama Makoto Department of Biochemistry, Shimane Medical University, Izumo 693 aut The Journal of Biochemistry Oxford University Press 120/6(1996-12), 1209-1215 0021-924X 120:6<1209 1996 120 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021543 text/html Onlinezugriff via DOI 1 other jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021543 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Tarashima Masaharu Department of Biochemistry, Shimane Medical University, Izumo 693 aut NATIONALLICENCE 700 1- Badruzzaman Muhammad Department of Biochemistry, Shimane Medical University, Izumo 693 aut NATIONALLICENCE 700 1- Tsuchiya Mikako Department of Biochemistry, Shimane Medical University, Izumo 693 aut NATIONALLICENCE 700 1- Shimoyama Makoto Department of Biochemistry, Shimane Medical University, Izumo 693 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 120/6(1996-12), 1209-1215 0021-924X 120:6<1209 1996 120 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford