PGD2 formation in the vasculature: characteristics of rat tail vein prostaglandin endoperoxide-D isomerase.
Rat tail vein homogenates, microsome and high speed supernatant fractions were incubated with [1-(14) C]prostaglandin endoperoxide (PGH2) and products separated and identified by radio-thinlayer chromatography. PGI2 synthase was localized to the microsomal fraction, but exhibited low activity compared to rat tail arteries prepared in the same manner. PGH-D isomerase was identified in the cytosolic fraction of tail veins. The isomerase was maximally active in the presence of reduced glutathione at pH 7.5-8.0, exhibited a Km for PGH2 of 33 microM, and was inhibited sulfhydryl-directed reagents. The similarities of this enzyme to PGD synthase of the rat cerebral microvasculature are discussed.
D000818:Animals; D005982:Glutathione Transferase / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D019746:Intramolecular Oxidoreductases; D007535:Isomerases / Q000378:metabolism*; D054834:Lipocalins; D008297:Male; D009131:Muscle, Smooth, Vascular / Q000201:enzymology*; D015230:Prostaglandin D2; D011453:Prostaglandins / Q000096:biosynthesis*; D011457:Prostaglandins D / Q000096:biosynthesis*; D011506:Proteins / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains; D012039:Regional Blood Flow; D013623:Tail / Q000098:blood supply
D054834:Lipocalins; D011453:Prostaglandins; D011457:Prostaglandins D; D011506:Proteins; D005982:Glutathione Transferase; D007535:Isomerases; D019746:Intramolecular Oxidoreductases; C022466:prostaglandin R2 D-isomerase; D015230:Prostaglandin D2