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J Biol Chem, Vol. 273, Issue 7, 4096-4105, February 13, 1998
From the Medical Research Council Immunochemistry Unit, Department
of Biochemistry, Oxford University, South Parks Road,
Oxford OX1 3QU, United Kingdom
Sequence analysis of cDNA clones
corresponding to a number of genes located in the class III region of
the human major histocompatibility complex (MHC), in the chromosome
band 6p21.3, has shown that the G15 gene encodes a
283-amino acid polypeptide with significant homology over the entire
polypeptide with the enzyme lysophosphatidic acid acyltransferase
(LPAAT) from different yeast, plant, and bacterial species. The amino
acid sequence of the MHC-encoded human LPAAT (hLPAAT
) is 48%
identical to the recently described hLPAAT (Eberhardt, C., Gray,
P. W., and Tjoelker, L. W. (1997) J. Biol. Chem.
272, 20299-20305), which is encoded by a gene located on
chromosome 9p34.3. LPAAT is the enzyme that in lipid metabolism converts lysophosphatidic acid (LPA) into phosphatidic acid (PA). The
expression of the hLPAAT polypeptide in the baculovirus system and
in mammalian cells has shown that it is an intracellular protein that
contains LPAAT activity. Cell extracts from insect cells overexpressing
hLPAAT were analyzed in different LPAAT enzymatic assays using, as
substrates, different acyl acceptors and acyl donors. These cell
extracts were found to contain up to 5-fold more LPAAT activity
compared with control cell extracts, indicating that the hLPAAT
specifically converts LPA into PA, incorporating different acyl-CoAs
with different affinities. The hLPAAT polypeptide expressed in the
mammalian Chinese hamster ovary cell line was found, by confocal
immunofluorescence, to be localized in the endoplasmic reticulum. Due
to the known role of LPA and PA in intracellular signaling and
inflammation, the hLPAAT gene represents a candidate gene for some
MHC-associated diseases.
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