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J Biol Chem, Vol. 273, Issue 16, 9886-9893, April 17, 1998
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From the Department of Biochemistry, Michigan State University,
East Lansing, Michigan 48824 and the Prostaglandin endoperoxide H synthases-1 and -2 (PGHS-1 and -2) are the major targets of nonsteroidal anti-inflammatory
drugs like aspirin and ibuprofen. These enzymes catalyze the committed step in the formation of prostanoids from arachidonic acid. Although PGHS-1 and -2 are similar biochemically, a number of studies suggest that PGHS-1 and PGHS-2 function independently to form prostanoids that
subserve different cellular functions. We have hypothesized that these
isozymes may reside, at least in part, in different subcellular
compartments and that their compartmentation may affect their access to
arachidonic acid and serve to separate the functions of the enzymes. To
obtain high resolution data on the subcellular locations of PGHS-1 and
-2, we employed immunoelectron microscopy with multiple antibodies
specific to each isozyme. Both PGHS-1 and -2 were found on the lumenal
surfaces of the endoplasmic reticulum (ER) and nuclear envelope of
human monocytes, murine NIH 3T3 cells, and human umbilical vein
endothelial cells. Within the nuclear envelope, PGHS-1 and -2 were
present on both the inner and outer nuclear membranes and in similar
proportions. Western blotting data showed a similar distribution of
PGHS-1 and -2 in subcellular fractions, and product analysis using
isozyme-specific inhibitors suggested that both enzymes generate the
same products in NIH 3T3 cells. Thus, we are unable to attribute the
independent functioning of PGHS-1 and PGHS-2 to differences in their
subcellular locations. Instead, the independent operation of these
isozymes may be attributable to subtle kinetic differences
(e.g. negative allosteric regulation of PGHS-1 at low
concentrations of arachidonate (500-1000 nM)). A further
conclusion of importance from a cell biological perspective is that
membrane proteins such as PGHS-1 and -2, which are located on the
lumenal surface of the ER, are able to diffuse freely among the ER and
the inner and outer membranes of the nuclear envelope.
Department of
Biochemical and Molecular Pathology, Merck Research Laboratories,
Rahway, New Jersey 07065
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