Effects of cytochalasin B on glycogen metabolism in phagocytizing human polymorphonuclear leukocytes
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چکیده
منابع مشابه
Microtubule dynamics and glutathione metabolism in phagocytizing human polymorphonuclear leukocytes
Glutathione oxidants such as tertiary butyl hydroperoxide were shown previously to prevent microtubule assembly and cause breakdown of preassembled cytoplasmic microtubules in human polymorphonuclear leukocytes. The objectives of the present study were to determine the temporal relationship between the attachment and ingestion of phagocytic particles and the assembly of microtubules, and simult...
متن کاملEffect of Cytochalasin B on Response of Human Polymorphonuclear Leukocytes to Zymosan
Phagocytosis of zymosan particles by human peripheral blood polymorphonuclear leukocytes (PMN) results in the release of lysosomal enzymes into the extracellular medium (1) and enhanced glucose oxidation and lactate production (2) . The antibiotic, cytochalasin B (CB), inhibits phagocytosis by PMN (3, 4), presumably by interfering with the membrane-associated network of microfilaments (5) . CB ...
متن کاملModification of Zymosan-induced Release of Lysosomal Enzymes from Human Polymorphonuclear Leukocytes by Cytochalasin B
During the process of phagocytosis, polymorphonuclear leukocytes (PMN) release lysosomal enzymes into the extracellular medium. When the antibiotic cytochalasin B (CB) is present in the incubation medium along with phagocytable particles, enhanced recovery of enzyme activities from the incubation medium has been observed. These findings have led to the interpretation that CB enhances lysosomal ...
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Release of arachidonic acid by the membrane phospholipase and metabolism by the 5-lipoxygenase pathway was examined in human polymorphonuclear leukocytes (PMNs). The 5-lipoxygenase pathway is activated when PMNs are given arachidonic acid in ethanol and there is extensive metabolism to 5-hydroxyicosatetraenoic acid (5-HETE) and leukotriene B4 (LTB4). This activation event was shown to be altere...
متن کاملKinetic mechanism of glycogen synthase D from human polymorphonuclear leukocytes.
catalyzed by glycogen synthase D (UDP-glucose:glycogen o-4-glucosyltransferase, EC 2.4.1.11) was studied, using r4C isotope transfer rates. The reaction rates were determined at varying concentrations of either substrate at constant amounts of the other substrate. The inhibition patterns of UDP as well as the activation patterns of the activator glucose 6-phosphate toward either substrate were ...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1979
ISSN: 0014-5793
DOI: 10.1016/0014-5793(79)80267-7