sq-23377 and 1-2-didecanoylglycerol

sq-23377 has been researched along with 1-2-didecanoylglycerol* in 2 studies

Other Studies

2 other study(ies) available for sq-23377 and 1-2-didecanoylglycerol

Article	Year
Altered O2-/H2O2 production ratio by in vitro and in vivo primed human neutrophils. Biochemical and biophysical research communications, 1990, Mar-30, Volume: 167, Issue:3 Human neutrophils were primed by exudation or pretreatment with a synthetic diacylglycerol (diC10), the Ca2+ ionophore ionomycin or lipopolysaccharide (LPS). Compared to control cells, these primed cells showed a significantly decreased O2-/H2O2 ratio when stimulated with formylmethionyl-leucyl-phenylalanine (FMLP). This shift indicates a comparative (and net) increased H2O2 detection in the extracellular medium and can not be explained by a dose-dependent impairment in either O2- or H2O2 detecting capacity. An altered H2O2 degenerating capacity was not observed in the primed cells. We propose that priming enhances the capacity to divalently reduce oxygen and thereby directly produce H2O2. Topics: Diglycerides; Humans; Hydrogen Peroxide; In Vitro Techniques; Ionomycin; Kinetics; Lipopolysaccharides; N-Formylmethionine Leucyl-Phenylalanine; Neutrophils; Skin Physiological Phenomena; Superoxides	1990
Degranulation in human neutrophils primes the cells for subsequent responsiveness to the chemoattractant N-formylmethionylleucylphenylalanine but does not increase the sensitivity of the NADPH-oxidase to an intracellular calcium rise. Biochimica et biophysica acta, 1990, Apr-09, Volume: 1052, Issue:1 Both the chemotactic peptide formylmethionylleucylphenylalanine (FMLP) and the calcium-specific ionophore ionomycin can activate the NADPH-oxidase in human neutrophils. However, since ionomycin and FMLP activity differ in their requirement for azide, a potent inhibitor of the hydrogen peroxide consuming enzymes catalase and myeloperoxidase, we propose that the two stimuli can activate different pools of the oxidase. Degranulation, induced in vitro by sn-1,2-dedecaoylglycerol or in vivo by an exudation process, resulted in a priming of the cells using FMLP as stimulating agent as well as in a reduced capacity to generate H2O2 in response to ionomycin. The sensitivity of the plasma membrane-bound NADPH-oxidase to an intracellular [Ca2+] rise, induced by the ionophore was, however, not changed by the degranulation. From these results we propose that FMLP activates the plasma membrane-bound oxidase, whereas the ionophore is capable of activating a granule-bound pool of the oxidase. Topics: Adult; Azides; Calcium; Chemotaxis, Leukocyte; Cytoplasmic Granules; Diglycerides; Humans; Hydrogen Peroxide; In Vitro Techniques; Ionomycin; Kinetics; N-Formylmethionine Leucyl-Phenylalanine; NADH, NADPH Oxidoreductases; NADPH Oxidases; Neutrophils; Superoxides	1990

Article

Year

Altered O2-/H2O2 production ratio by in vitro and in vivo primed human neutrophils.

Biochemical and biophysical research communications, 1990, Mar-30, Volume: 167, Issue:3

Human neutrophils were primed by exudation or pretreatment with a synthetic diacylglycerol (diC10), the Ca2+ ionophore ionomycin or lipopolysaccharide (LPS). Compared to control cells, these primed cells showed a significantly decreased O2-/H2O2 ratio when stimulated with formylmethionyl-leucyl-phenylalanine (FMLP). This shift indicates a comparative (and net) increased H2O2 detection in the extracellular medium and can not be explained by a dose-dependent impairment in either O2- or H2O2 detecting capacity. An altered H2O2 degenerating capacity was not observed in the primed cells. We propose that priming enhances the capacity to divalently reduce oxygen and thereby directly produce H2O2.

Topics: Diglycerides; Humans; Hydrogen Peroxide; In Vitro Techniques; Ionomycin; Kinetics; Lipopolysaccharides; N-Formylmethionine Leucyl-Phenylalanine; Neutrophils; Skin Physiological Phenomena; Superoxides

1990

Degranulation in human neutrophils primes the cells for subsequent responsiveness to the chemoattractant N-formylmethionylleucylphenylalanine but does not increase the sensitivity of the NADPH-oxidase to an intracellular calcium rise.

Biochimica et biophysica acta, 1990, Apr-09, Volume: 1052, Issue:1

Both the chemotactic peptide formylmethionylleucylphenylalanine (FMLP) and the calcium-specific ionophore ionomycin can activate the NADPH-oxidase in human neutrophils. However, since ionomycin and FMLP activity differ in their requirement for azide, a potent inhibitor of the hydrogen peroxide consuming enzymes catalase and myeloperoxidase, we propose that the two stimuli can activate different pools of the oxidase. Degranulation, induced in vitro by sn-1,2-dedecaoylglycerol or in vivo by an exudation process, resulted in a priming of the cells using FMLP as stimulating agent as well as in a reduced capacity to generate H2O2 in response to ionomycin. The sensitivity of the plasma membrane-bound NADPH-oxidase to an intracellular [Ca2+] rise, induced by the ionophore was, however, not changed by the degranulation. From these results we propose that FMLP activates the plasma membrane-bound oxidase, whereas the ionophore is capable of activating a granule-bound pool of the oxidase.

Topics: Adult; Azides; Calcium; Chemotaxis, Leukocyte; Cytoplasmic Granules; Diglycerides; Humans; Hydrogen Peroxide; In Vitro Techniques; Ionomycin; Kinetics; N-Formylmethionine Leucyl-Phenylalanine; NADH, NADPH Oxidoreductases; NADPH Oxidases; Neutrophils; Superoxides

1990