Luminol dependent chemiluminescence and thiol group oxidation provoked by neutrophils is attributable to different oxidizing species.
Luminol-dependent chemiluminescence and thiol group oxidation of glutathione and human serum albumin were measured in order to demonstrate whether the inhibition of polymorphonuclear leukocyte chemiluminescence by albumin was attributable to thiol group oxidation. We have shown that: 1. thiol groups on glutathione and albumin are oxidized by PMNL stimulated by soluble and phagocytic stimuli; 2. thiol group oxidation in albumin and glutathione did not correlate with the inhibitory effects of these substances on luminol-dependent chemiluminescence with respect to time course, magnitude, effects of known scavengers or extracellular activity. It was therefore concluded that thiol group oxidation was not the cause of albumin inhibition of luminol-dependent chemiluminescence; 3. a metastable oxidant was identified after PMNL activation which was capable of oxidizing thiol groups but unable to elicit chemiluminescence from luminol.
D001386:Azides / Q000494:pharmacology; D002474:Cell-Free System; D005978:Glutathione / Q000097:blood; D006801:Humans; D066298:In Vitro Techniques; D008163:Luminescent Measurements; D008165:Luminol / Q000378:metabolism*; D009504:Neutrophils / Q000187:drug effects / Q000378:metabolism*; D010084:Oxidation-Reduction; D011724:Pyridazines / Q000378:metabolism*; D012709:Serum Albumin / Q000378:metabolism; D019810:Sodium Azide; D013438:Sulfhydryl Compounds / Q000097:blood*; D013482:Superoxide Dismutase / Q000494:pharmacology
D001386:Azides; D011724:Pyridazines; D012709:Serum Albumin; D013438:Sulfhydryl Compounds; D008165:Luminol; D019810:Sodium Azide; D013482:Superoxide Dismutase; D005978:Glutathione