[Human serum albumin modified under oxidative/halogenative stress enhances luminol-dependent chemiluminescence of human neutrophils].
It is shown that human serum albumin, previously treated with HOCl (HSA-Cl), enhances luminol-dependent chemiluminescence of neutrophils activated by phorbol-12-myristate-13-acetate (PMA). The enzyme-linked immunosorbent assay revealed that addition of HSA-Cl to neutrophils promotes exocytosis of myeloperoxidase. Inhibitor of myeloperoxidase--4-aminobenzoic acid hydrazide, without any effect on lucigenin-dependent chemiluminescence of neutrophils stimulated with PMA, effectively suppressed luminol-dependent chemiluminescence (IC50 = 20 microM) under the same conditions. The transfer of the cells from medium with HSA-Cl and myeloperoxidase to fresh medium abolished an increase in PMA-induced luminol-dependent chemiluminescence, but not the ability of neutrophils to respond to re-addition of HSA-Cl. A direct and significant (r = 0.75, p) correlation was observed between the intensity of PMA stimulated neutrophil chemiluminescence response and myeloperoxidase activity in the cell-free media after chemiluminescence measurements. These results suggest the involvement of myeloperoxidase in the increase of neutrophil PMA-stimulated chemiluminescence response in the presence of HSA-Cl. A significant positive correlation was found between myeloperoxidase activity in blood plasma of children with severe burns and the enhancing effects of albumin fraction of the same plasma on luminol-dependent chemiluminescence of PMA-stimulated donor neutrophils. These results support a hypothesis that proteins modified in reactions involving myeloperoxidase under oxidative/halogenative stress, stimulate neutrophils, leading to exocytosis of myeloperoxidase, a key element of halogenative stress, and to closing a "vicious circle" of neutrophil activation at the inflammatory site.
E V
EV
Mikhal'chik
N V
NV
Smolina
T C
TC
Astamirova
I V
IV
Gorudko
D V
DV
Grigor'eva
V A
VA
Ivanov
A V
AV
Sokolov
V A
VA
Kostevich
S N
SN
Cherenkevich
O M
OM
Panasenko
D000814:Aniline Compounds / Q000494:pharmacology; D002056:Burns / Q000201:enzymology* / Q000473:pathology; D002648:Child; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004797:Enzyme-Linked Immunosorbent Assay; D006801:Humans; D006997:Hypochlorous Acid / Q000737:chemistry; D049449:Luminescence; D008163:Luminescent Measurements; D008165:Luminol / Q000737:chemistry*; D018375:Neutrophil Activation / Q000187:drug effects; D009504:Neutrophils / Q000187:drug effects* / Q000201:enzymology / Q000378:metabolism / Q000473:pathology; D018384:Oxidative Stress; D009195:Peroxidase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D010703:Phorbol Esters / Q000494:pharmacology; D012709:Serum Albumin / Q000737:chemistry / Q000494:pharmacology*
D000814:Aniline Compounds; D004791:Enzyme Inhibitors; D010703:Phorbol Esters; D012709:Serum Albumin; C119222:phorbol-12-myristate; C034343:4-aminobenzhydrazide; D008165:Luminol; D006997:Hypochlorous Acid; D009195:Peroxidase