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J Biol Chem, Vol. 274, Issue 27, 19152-19160, July 2, 1999
From the Secreted phospholipases A2
(sPLA2s) form a class of structurally related enzymes that
are involved in a variety of physiological and pathological effects
including inflammation and associated diseases, cell proliferation,
cell adhesion, and cancer, and are now known to bind to specific
membrane receptors. Here, we report the cloning and expression of a
novel sPLA2 isolated from mouse thymus. Based on its
structural features, this sPLA2 is most similar to the
previously cloned mouse group IIA sPLA2 (mGIIA
sPLA2). As for mGIIA sPLA2, the novel
sPLA2 is made up of 125 amino acids with 14 cysteines, is
basic (pI = 8.71) and its gene has been mapped to mouse chromosome
4. However, the novel sPLA2 has only 48% identity with
mGIIA and displays similar levels of identity with the other mouse
group IIC and V sPLA2s, indicating that the novel
sPLA2 is not an isoform of mGIIA sPLA2. This
novel sPLA2 has thus been called mouse group IID (mGIID)
sPLA2. In further contrast with mGIIA, which is found
mainly in intestine, transcripts coding for mGIID sPLA2 are
found in several tissues including pancreas, spleen, thymus, skin,
lung, and ovary, suggesting distinct functions for the two enzymes.
Recombinant expression of mGIID sPLA2 in Escherichia
coli indicates that the cloned sPLA2 is an active
enzyme that has much lower specific activity than mGIIA and displays a
distinct specificity for binding to various phospholipid vesicles.
Finally, recombinant mGIID sPLA2 did not bind to the mouse
M-type sPLA2 receptor, while mGIIA was previously found to
bind to this receptor with high affinity.
Cloning and Recombinant Expression of a Novel Mouse-secreted
Phospholipase A2
,, and
Institut de Pharmacologie Moléculaire
et Cellulaire, CNRS, UPR 411, 660 route des Lucioles, Sophia Antipolis,
06560 Valbonne, France, the § Departments of Chemistry and
Biochemistry, University of Washington, Seattle, Washington 98195, and
the ¶ Laboratoire d'Etude du Génome Murin, IAG-CNRS, UMR
6549, Faculté de Médecine, Avenue de Valombrose,
06107 Nice, France
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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