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Blood, 1 February 2002, Vol. 99, No. 3, pp. 1044-1052
PHAGOCYTES
Activation of 5-lipoxygenase by cell stress is calcium
independent in human polymorphonuclear leukocytes
Oliver Werz,
Eva Bürkert,
Bengt Samuelsson,
Olof Rådmark, and
Dieter Steinhilber
From the Institute of Pharmaceutical Chemistry,
University of Frankfurt, Germany, and the Department of Medical
Biochemistry and Biophysics, Division of Physiological Chemistry II,
Karolinska Institute, Stockholm, Sweden.
5-Lipoxygenase (5-LO) is the key enzyme in the biosynthesis of
proinflammatory leukotrienes. This study showed that various forms of
cell stress, such as chemical stress (sodium arsenite), osmotic stress,
or heat shock lead to substantial formation of 5-LO products in freshly
isolated human polymorphonuclear leukocytes (PMNLs), when exogenous
arachidonic acid (10 µM) was present. In parallel, cell
stress led to activation of p38 MAPK (mitogen-activated protein kinase)
and mitogen-activated protein kinase-activated protein
kinases (MAPKAPKs) kinases, which can phosphorylate 5-LO in
vitro. Interestingly, arsenite also caused redistribution of 5-LO
from the cytosol to the nuclear membrane. Only minor activation of
extracellular signal-regulated kinases and c-jun
NH2-terminal kinases was observed, implying that these
MAPKs are less important for 5-LO product formation in
stress-stimulated PMNLs. Stimulation of 5-LO product formation by
Ca++-ionophore A23187 or thapsigargin depended on
Ca++; almost no 5-LO product formation was observed in
freshly isolated PMNLs when Ca++ was depleted by
chelating agents. Also the response to
N-formylmethionyl-leucyl-phenylalanine (fMLP) was clearly diminished, but some 5-LO product formation remained. In contrast, stress-induced product formation and
translocation of 5-LO, as well as activation of p38 MAPK, occurred also
after Ca++ depletion. Moreover, the p38 MAPK
inhibitor SB203580 blocked stress-induced 5-LO product formation
efficiently, whereas ionophore- or thapsigargin-induced formation of
5-LO products was less sensitive. These data show that cell stress can
activate 5-LO in isolated PMNLs by a mechanism that does not involve
Ca++ mobilization. This mechanism could function
independently of Ca++-mediated 5-LO activation for
stimulation of leukotriene biosynthesis under physiologic conditions as
well as in inflammatory diseases.
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