caa a22 4500 39755561X CHVBK 20180308164801.0 cr unu---uuuuu 161202e199612 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021548 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021548 Requirement of Calcium Influx for Hydrolytic Action of Membrane Phospholipids by Cytosolic Phospholipase A2 Rather than Mitogen-Activated Protein Kinase Activation in FcεRI-Stimulated Rat Peritoneal Mast Cells [Elektronische Daten] [Tsuyoshi Ishimoto, Kyoichi Arisato, Takashi Sato] The mechanism by which cytosolic phospholipase A2 (cPLA2 is not responsible for eicosanoid production in rat peritoneal mast cells upon antigen stimulation [Ishimoto et al (1996) J. Biochem. 120, 616-623] was investigated in the mast cells stimulated by crosslinking of the IgE receptor or with thapsigargin. Stimulation with thapsigargin, but not with antigen, resulted in apparent lysophosphatidyicholine (lysoPC) formation. Antigen stimulation significantly increased the activities of mitogen-activated protein (MAP) kinase and cPLA2 These activities were further potentiated by phorbol ester. The antigen elicited a rapid and transient increase in intracellular Ca2+ concentration, while thapsigargin produced a slow and sustained increase. Furthermore, a combination of antigen and thapsigargin rapidly increased and prolonged the intracellular Ca2+ concentration. Under these conditions, lysoPC was apparently generated, whereas it was not in response to antigen alone. These results suggest that a prolonged increase in the intracellular Ca2+ concentration is required for cPLA2 to associate with membranes, thus leading to hydrolysis of membrane phospholipids by the enzyme. © 1996 BY THE JOURNAL OF BIOCHEMISTRY Regular Papers nationallicence cytosolic phospholipase A2 nationallicence intracellular calcium concentration nationallicence lysophosphatidylcholine nationallicence mast cell nationallicence mitogen-activated protein kinase nationallicence Ishimoto Tsuyoshi Department of Pathological Biochemistry, Kyoto Pharmaceutical University, Misasagi, Yamashina-hu, Kyoto, Kyoto 607 aut Arisato Kyoichi Department of Pathological Biochemistry, Kyoto Pharmaceutical University, Misasagi, Yamashina-hu, Kyoto, Kyoto 607 aut Sato Takashi Department of Pathological Biochemistry, Kyoto Pharmaceutical University, Misasagi, Yamashina-hu, Kyoto, Kyoto 607 aut The Journal of Biochemistry Oxford University Press 120/6(1996-12), 1247-1252 0021-924X 120:6<1247 1996 120 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021548 text/html Onlinezugriff via DOI 1 other jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021548 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Ishimoto Tsuyoshi Department of Pathological Biochemistry, Kyoto Pharmaceutical University, Misasagi, Yamashina-hu, Kyoto, Kyoto 607 aut NATIONALLICENCE 700 1- Arisato Kyoichi Department of Pathological Biochemistry, Kyoto Pharmaceutical University, Misasagi, Yamashina-hu, Kyoto, Kyoto 607 aut NATIONALLICENCE 700 1- Sato Takashi Department of Pathological Biochemistry, Kyoto Pharmaceutical University, Misasagi, Yamashina-hu, Kyoto, Kyoto 607 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 120/6(1996-12), 1247-1252 0021-924X 120:6<1247 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