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J Biol Chem, Vol. 274, Issue 35, 24973-24979, August 27, 1999
From the Shionogi Research Laboratories, Shionogi and Co., Ltd.,
Sagisu 5-12-4, Fukushima-ku, Osaka 553-0002, Japan
Mammalian secretory phospholipase
A2s (sPLA2s) are classified into several
groups according to molecular structure and the localization of
intramolecular disulfide bridges. Among them, group IIA
sPLA2 has been thought to be one of the key enzymes in the
pathogenesis of inflammatory diseases owing to its augmented expression
under various inflammatory conditions. However, in a number of inbred
mouse strains, the group IIA sPLA2 gene is naturally
disrupted by a frameshift mutation. Here, we report the cloning of a
cDNA encoding a novel sPLA2 expressed in the spleen of
group IIA sPLA2-deficient mouse. We also cloned its human
homolog and mapped its gene location on chromosome 1p36.12 near the
loci of group IIA and V sPLA2 genes. The human mature sPLA2 protein consists of 125 amino acids
(Mr = 14,500) preceded by a 20-residue
prepeptide and is most similar to group IIA sPLA2 with
respect to the number and positions of cysteine residues as well as
overall identity (48%). Based on these structural properties, the
novel sPLA2 should be categorized into group II, called
group IID to follow the already identified IIA to IIC
sPLA2s. When the cDNA was expressed in COS-7 cells,
PLA2 activity preferentially accumulated in the culture
medium. It is maximally active at neutral to alkaline pH and with 2 mM Ca2+. In assays with individual substrates,
L-
-1-palmitoyl-2-linoleoyl phosphatidylethanolamine was
more efficiently hydrolyzed than the other phospholipids examined. An
RNA blot hybridized with the cDNA exhibited two transcripts (2.0 and 1.0 kb) in human spleen, thymus, and colon. The expression of a
novel sPLA2 mRNA was elevated in the thymus after
treatment with endotoxin in rats as well as in group IIA
sPLA2-deficient mice, suggesting its functional role in the
progression of the inflammatory process.
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