Prostaglandin H Synthase

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Heme coordination of prostaglandin H synthase.

The heme coordination of ovine prostaglandin H synthase (PGHS) has been characterized by EPR, magnetic circular dichroism, resonance Raman, and optical spectroscopies. The EPR spectrum of ferric PGHS is consistent with an equilibrium mixture of high-spin and low-spin heme species. Both species disappear on reaction of the synthase with hydroperoxides. The high-spin to low-spin interconversion i...

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Prostaglandin H synthase and vascular function.

Prostaglandin H synthase (PGHS) is a rate-limiting enzyme in the production of prostaglandins and thromboxane, which are important regulators of vascular function. Under normal physiological conditions, PGHS-dependent vasodilators (such as prostacyclin) modulate vascular tone. However, PGHS-dependent vasoconstriction (mediated by thromboxane and/or its immediate precursor, PGH(2)) predominates ...

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PTGS 2 ( prostaglandin - endoperoxide synthase 2 ( prostaglandin G / H synthase and cyclooxygenase ) )

COX2 is an enzyme that belongs to the prostaglandin G/H synthase family. It consists of 604 amino acids and has a molecular weight of 68996 Da. COX2 possesses two catalytic activities and respective active sites: a cyclooxygenase (COX) that converts arachidonic acid to a prostaglandin endoperoxide, prostaglandin G2 (PGG2), and; a peroxidase (POX) that reduces PGG2 to PGH2. COX2 functions as hom...

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Metabolism of aromatic amines by prostaglandin H synthase.

The metabolism of aromatic amines by the peroxidase activity of prostaglandin H synthase (PHS) has been studied in this laboratory by use of two model compounds, the carcinogenic primary amine 2-aminofluorene (2-AF) and the substituted amine aminopyrine (AP). 2-AF is oxidized by PHS to 2, 2-azobisfluorene, 2-aminodifluorenylamine, 2-nitrofluorene, polymeric material, and products covalently bou...

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Prostaglandin endoperoxide H synthase expression in human thyroid epithelial cells.

KAT-50, an established human thyrocyte cell line, expresses constitutively high levels of prostaglandin endoperoxide H synthase-2 (PGHS-2), the inflammatory cyclooxygenase. Here, we examine primary human thyrocytes. We find that they, too, express PGHS-2 mRNA and protein under control culture conditions. A substantial fraction of the basal prostaglandin E(2) (PGE(2)) produced by these cells can...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 2000

ISSN: 0021-9258

DOI: 10.1074/jbc.m003982200