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J Biol Chem, Vol. 274, Issue 17, 11881-11888, April 23, 1999
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From the Group V phospholipase A2 is a
recently discovered secretory phospholipase A2
(PLA2) that has been shown to be involved in eicosanoid
formation in inflammatory cells, such as macrophages and mast cells. We
have demonstrated that human group V PLA2
(hsPLA2-V) can bind phosphatidylcholine (PC) membranes and
hydrolyze PC substrates much more efficiently than human group IIa
PLA2, which makes it better suited for acting on the outer
plasma membrane (Han, S.-K., Yoon, E. T., and Cho, W. (1998)
Biochem. J. 331, 353-357). In this study, we demonstrate
that exogenous hsPLA2-V has much greater activity than does
group IIa PLA2 to release fatty acids from various
mammalian cells and to elicit leukotriene B4 formation from
human neutrophils. To understand the molecular basis of these activities, we mutated two surface tryptophans of hsPLA2-V
to alanine (W31A and W79A) and measured the effects of these mutations on the kinetic activity toward various substrates, on the binding affinity for vesicles and phospholipid-coated beads, on the penetration into phospholipid monolayers, and on the activity to release fatty acids and elicit eicosanoid formation from various mammalian cells. These studies show that the relatively high ability of
hsPLA2-V to induce cellular eicosanoid formation derives
from its high affinity for PC membranes and that Trp31 on
its putative interfacial binding surface plays an important role in its
binding to PC vesicles and to the outer plasma membrane.
Department of Chemistry, University of
Illinois, Chicago, Illinois 60607, the ¶ Departments of
Chemistry and Biochemistry, University of Washington,
Seattle, Washington 98195, the Department of Medicine,
University of Chicago, Chicago, Illinois 60307, and the ** Department
of Biochemistry, University of Southampton, Bassett Crescent East,
Southampton S09 3TU, United Kingdom
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W. Cho Membrane Targeting by C1 and C2 Domains J. Biol. Chem., August 24, 2001; 276(35): 32407 - 32410. [Full Text] [PDF]
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