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J. Biol. Chem., Vol. 262, Issue 8, 3510-3517, 03, 1987
PJ Marshall, RJ Kulmacz and WE Lands
The formation of prostaglandins by prostaglandin H synthase can be limited
by the availability of the fatty acid substrate or the hydroperoxide
activator and also by a self-catalyzed inactivation associated with the
oxygenation reaction. Each pmol of synthase appeared able to form only
about 1300 pmol of prostaglandin from arachidonate before it was
inactivated. This extent of synthesis was not diminished when substrate
fatty acid was complexed with cytosolic proteins even though the velocity
of the oxygenation reaction was greatly decreased by the lower availability
of substrate acid. When the availability of hydroperoxide activator was
decreased by added glutathione peroxidase, the extent of oxygenation per
mol of synthase was decreased irrespective of the amount of cytosolic
protein present. Approximately 65% of the total prostaglandin synthesis by
homogenates was suppressed with a glutathione peroxidase to prostaglandin H
synthase ratio of about 90. The remaining prostaglandin synthetic activity
was more resistant, being completely suppressed only when the ratio of
peroxidase to synthase exceeded 750. The overall ratio of glutathione
peroxidase (peroxide-removing) capacity to prostaglandin synthetic
(peroxide-forming) capacity in selected tissues ranged from over 1800 in
rat liver to less than 30 in leukocytes. A comparison between the daily
urinary output of prostaglandin metabolites and tissue prostaglandin
synthetic capacity suggested that prostaglandin H synthase inactivation
along with glutathione peroxidase suppression of the extent of
prostaglandin synthase may be important in limiting prostaglandin
biosynthesis within cells.
Constraints on prostaglandin biosynthesis in tissues
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