Topic
Prostaglandin-D synthase
About: Prostaglandin-D synthase is a research topic. Over the lifetime, 227 publications have been published within this topic receiving 8372 citations. The topic is also known as: (5,13)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate D-isomerase & PGD2 synthase.
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TL;DR: X-ray crystallographic analyses revealed that PGDS possesses a beta-barrel structure with a hydrophobic pocket in which an active thiol, Cys(65), the active center for the catalytic reaction, was located facing to the inside of the pocket.
329 citations
TL;DR: Two distinct types of PGD synthase are purified; one is the lipocalin-type enzyme and the other is the hematopoietic enzyme, which acts as a PGD2-producing enzyme and also as a lipophilic ligand-binding protein, with high affinities.
Abstract: Prostaglandin (PG) D synthase catalyzes the isomerization of PGH2, a common precursor of various prostanoids, to produce PGD2 in the presence of sulfhydryl compounds PGD2 induces sleep, regulates nociception, inhibits platelet aggregation, acts as an allergic mediator, and is further converted to 9 alpha, 11 beta-PGF2 or the J series of prostanoids, such as PGJ2, delta 12-PGJ2, and 15-deoxy-delta 12,14-PGJ2 We have purified two distinct types of PGD synthase; one is the lipocalin-type enzyme and the other is the hematopoietic enzyme We isolated the cDNA and the gene for each enzyme and determined the tissue distribution profile and the cellular localization in several animal species Lipocalin-type PGD synthase is localized in the central nervous system and male genital organs of various mammals and the human heart and is secreted into cerebrospinal fluid, seminal plasma, and plasma, respectively The human enzyme was identified as beta-trace, which is a major protein in human cerebrospinal fluid This enzyme is considered to be a dual-function protein; it acts as a PGD2-producing enzyme and also as a lipophilic ligand-binding protein, because the enzyme binds retinoids, thyroids, and bile pigments, with high affinities Hematopoietic PGD synthase is widely distributed in the peripheral tissues and localized in the antigen-presenting cells, mast cells, and megakaryocytes The hematopoietic enzyme is the first recognized vertebrate homolog of the sigma class of glutathione S-transferase X-ray crystallographic analyses and generation of gene-knockout and transgenic mice for each enzyme have been performed
289 citations
TL;DR: When the amounts of primary prostaglandins formed from endogenous arachidonic acid were determined in homogenates of various tissues of adult rats, prostaglandin D2 was the major prostaglandsin found in most tissues.
261 citations
TL;DR: Prostaglandin D synthetase was purified 2,600-fold from rat brain to apparent homogeneity, as judged by polyacrylamide gel electrophoresis and ultracentrifugation, indicating that the preparation is a major component of the enzyme responsible for the biosynthesis of prostaglandsin D2 in the brain.
235 citations
TL;DR: Prostaglandin D synthase is mainly synthesized and located in the leptomeninges, choroid plexus, and oligodendrocytes in the brain, and the findings agree with those obtained by immunohistochemical staining with antibodies against the enzyme.
Abstract: Glutathione-independent prostaglandin D synthase [prostaglandin-H2 D-isomerase; (5Z,13E)-(15S)-9 alpha,11 alpha-epidioxy-15-hydroxyprosta-5,13-dienoate D-isomerase, EC 5.3.99.2] is an enzyme responsible for biosynthesis of prostaglandin D2 in the central nervous system. In situ hybridization with antisense RNA for the enzyme indicated that mRNA for the enzyme was predominantly expressed in the leptomeninges, choroid plexus, and oligodendrocytes of the adult rat brain. The findings agree with those obtained by immunohistochemical staining with antibodies against the enzyme. It was further revealed that prostaglandin D synthase activity was considerably greater in the isolated leptomeninges (14.2 nmol per min per mg of protein) and choroid plexus (7.0 nmol per min per mg of protein) than the activity in the whole brain (2.0 nmol per min per mg of protein). These results, taken together, indicate that the enzyme is mainly synthesized and located in the leptomeninges, choroid plexus, and oligodendrocytes in the brain.
231 citations