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A Novel Type of Membrane-Associated Prostaglandin E Synthase

  • Kikuko Watanabe
  • Yoshihiro Ohmiya
  • Hiroaki Ohkubo
  • Naomi Tanikawa
  • Masami Kojima
  • Seiji Ito
Chapter
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 525)

Abstract

Prostaglandin (PG) E2 is widely distributed in various organs, and exhibits various biologically important activities such as smooth muscle dilatation/contraction, body temperature regulation, induction of pain, stimulation of bone resorption, and inhibition of immune responses. PGE synthase catalyzes the conversion of PGH2 to PGE2. About 25 years ago, Ogino et al [1] reported that glutathione (GSH) was required for the PGE synthase activity, and laid the groundwork for the study of membrane- associated PGE synthase (mPGE synthase). Tanaka et al [2] characterized PGE synthase in sheep vesicular gland microsomes by use of a monoclonal antibody. In 1999, using a clone of microsomal GSH S-transferase 1-like 1, Jakobsson et al [3] expressed human GSH-specific mPGE synthase (mPGE synthase-1) in E. coli. The mPGE synthase-1 had high GSH-dependent PGE synthase activity, and the protein expression was induced by IL-1β. Moreover, Ogorochi et al [4] and Meyer et al [5] independently purified the PGE synthase from the cytosol fraction of human brain and Ascaridia galli, respectively, and reported that the enzyme was GSH S-transferase (GST). Recently Tanioka et al [6] isolated the PGE synthase from the cytosol fraction of rat brain, and reported that the enzyme belonged to GST family.

Keywords

Cytosol Fraction Bovine Heart Apparent Homogeneity Consensus Region Body Temperature Regulation 
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.

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Copyright information

© Springer Science+Business Media New York 2003

Authors and Affiliations

  • Kikuko Watanabe
  • Yoshihiro Ohmiya
  • Hiroaki Ohkubo
  • Naomi Tanikawa
  • Masami Kojima
  • Seiji Ito

There are no affiliations available

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