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(Received for publication, November 18, 1996, and in revised form, December 23, 1996)
From the Division of Pulmonary and Critical Care Medicine,
Department of Internal Medicine, University of Michigan, Ann Arbor,
Michigan 48109-0652
5-Lipoxygenase catalyzes the synthesis of
leukotrienes from arachidonic acid. The subcellular distribution
of 5-lipoxygenase is known to be cell type-dependent and is
cytosolic in blood neutrophils. In this study, we asked whether
neutrophil recruitment into sites of inflammation can alter the
subcellular compartmentation of 5-lipoxygenase. In peripheral blood
neutrophils from rats, 5-lipoxygenase was exclusively cytosolic, as
expected. However, in glycogen-elicited peritoneal neutrophils,
abundant soluble 5-lipoxygenase was in the nucleus. Upon activation
with calcium ionophore A23187, intranuclear 5-lipoxygenase translocated
to the nuclear envelope. Elicited neutrophils required a greater
concentration of A23187 for activation than did blood neutrophils
(half-maximal response, 160 versus 52 nM,
respectively) but generated greater amounts of leukotriene B4 upon maximal stimulation (26.6 versus 7.68 ng/106 cells, respectively). Intranuclear 5-lipoxygenase
was also evident in human blood neutrophils after adherence to a
variety of surfaces, suggesting that adherence alone is sufficient to
drive 5-lipoxygenase redistribution. These results demonstrate a
physiologically relevant circumstance in which the subcellular
distribution of 5-lipoxygenase can be rapidly altered in resting cells,
independent of 5-lipoxygenase activation. Nuclear import of
5-lipoxygenase may be a universal accompaniment of neutrophil
recruitment into sites of inflammation, and this may be associated with
alterations in enzymatic function.
Volume 272, Number 13,
Issue of March 28, 1997
pp. 8276-8280
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
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