Purification and Characterization of Membrane-Bound Prostaglandin E Synthase from Bovine Hearts

  • Kikuko Watanabe
  • Kayoko Kurihara
  • Toshiko Suzuki
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 507)


E series of prostaglandin (PG)s were first discovered in sheep seminal vesicles. PGE2is widely distributed in various organs, and exhibits various biological activities such as smooth muscle dilatation/contraction, Na+ excretion, body temperature regulation, inhibition of gastric acid secretion, and inhibition of immune responses. PGE synthase (EC. 5. 3. 99. 3.) catalyzes the conversion of PGH2to PGE2. Although several groups have attempted to purify this enzyme for the last 20 years, the membrane-bound PGE synthase has not yet been purified to homogeneity from microsomes of any tissues. In 1997, we reported that PGE synthase activity is widely distributed in the microsomal fractions of rat organs (1). Most of the PGE synthase activities in these organs absolutely required glutathione (GSH). In contrast, the enzyme activity in the heart, spleen, and uterine microsomes required SH-reducing reagents including dithiothreitol (DTT), GSH, or ß-mercaptoethanol (β-Mer), but the requirement for its catalytic activity was not specific for GSH. We purified the GSH-independent PGE synthase from bovine heart to apparent homogeneity, and examined its molecular and catalytic properties (2).


Gastric Acid Secretion Genital Organ Sodium Cholate Bovine Heart Apparent Homogeneity 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    K. Watanabe, K. Kurihara, O. Hayaishi, Two types of microsomal prostaglandin E synthase:glutathionedependent and -independent prostaglandin E synthasesBiochem. Biophys. Res. Commun.235: 148 (1997).PubMedCrossRefGoogle Scholar
  2. 2.
    K. Watanabe, K. Kurihara, and T. Suzuki, Purification and Characterization of Membrane-bound Prostaglandin E Synthase from Bovine Heart. Biochim. Biophys. Acta 1439: 406 (1999).Google Scholar
  3. 3.
    L-A. Klein and JS. Stoff, Prostaglandin synthesis is independent of androgen levels in rat male genitaliaJ. Lab. Clin. Med.109: 402 (1987).PubMedGoogle Scholar
  4. 4.
    P-J. Jakobsson, T. Staffan, R. Morgenstern, and B. Samuelsson, Identification of human prostaglandin E synthase: A microsomal, glutathione-dependent, inducible enzyme, constituting a potential novel drug targetProc. Natl. Acad. Sci. USA96: 7220 (1999)PubMedCentralPubMedCrossRefGoogle Scholar
  5. 5.
    T. Ogorochi, M. Ujihara, S. Narumiya, Purification and properties of prostaglandin H-E isomerase from the cytosol of human brain: Identification as anionic forms of glutathione S-transferaseJ. Neurochem.48: 900 (1987).PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 2002

Authors and Affiliations

  • Kikuko Watanabe
    • 1
  • Kayoko Kurihara
    • 2
  • Toshiko Suzuki
    • 3
  1. 1.Division of Applied Life SciencesGraduate School of Integrated Sciences and Arts, University of East AsiaShimonosekiJapan
  2. 2.Department of NeurovirologyResearch Institute for Microbial Diseases, Osaka UniversityYamadaoka SuitaJapan
  3. 3.Department of Anatomy and Cell Biology, School of MedicineThe University of TokushimaTokushimaJapan

Personalised recommendations