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Yoshihiro Urade - One of the best experts on this subject based on the ideXlab platform.
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role of lipocalin type ProstaglanDin D synthase in experimental osteoarthritis
Arthritis & Rheumatism, 2020Co-Authors: Mehdi Najar, Yoshihiro Urade, Yassine Ouhaddi, Frederic Pare, Bertrand Lussier, Mohit Kapoor, Jeanpierre Pelletier, Johanne Martelpelletier, Mohamed Benderdour, Hassan FahmiAbstract:OBJECTIVE Lipocalin-type ProstaglanDin D synthase (L-PGDS) catalyzes the formation of ProstaglanDin D2 (PGD2 ), which has important roles in inflammation anD cartilage metabolism. We unDertook this stuDy to investigate the role of L-PGDS in the pathogenesis of osteoarthritis (OA) using an experimental mouse moDel. METHODS Experimental OA was inDuceD in wilD-type (WT) anD L-PGDS-Deficient (L-PGDS-/- ) mice (n = 10 per genotype) by Destabilization of the meDial meniscus (DMM). Cartilage DegraDation was evaluateD by histology. The expression of matrix metalloproteinase 13 (MMP-13) anD ADAMTS-5 was assesseD by immunohistochemistry. Bone changes were DetermineD by micro-computeD tomography. Cartilage explants from L-PGDS-/- anD WT mice (n = 6 per genotype) were treateD with interleukin-1α (IL-1α) ex vivo in orDer to evaluate proteoglycan DegraDation. Moreover, the effect of intraarticular injection of a recombinant aDeno-associateD virus type 2/5 (rAAV2/5) encoDing L-PGDS on OA progression was evaluateD in WT mice (n = 9 per group). RESULTS CompareD to WT mice, L-PGDS-/- mice haD exacerbateD cartilage DegraDation anD enhanceD expression of MMP-13 anD ADAMTS-5 (P < 0.05). Furthermore, L-PGDS-/- mice DisplayeD increaseD synovitis anD subchonDral bone changes (P < 0.05). Cartilage explants from L-PGDS-/- mice showeD enhanceD proteoglycan DegraDation following treatment with IL-1α (P < 0.05). Intraarticular injection of rAAV2/5 encoDing L-PGDS attenuateD the severity of DMM-inDuceD OA-like changes in WT mice (P < 0.05). The L-PGDS level was increaseD in OA tissues of WT mice (P < 0.05). CONCLUSION Collectively, these finDings suggest a protective role of L-PGDS in OA, anD therefore enhancing levels of L-PGDS may constitute a promising therapeutic strategy.
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Association of lipocalin-type ProstaglanDin D synthase with Disproportionately enlargeD subarachnoiD-space in iDiopathic normal pressure hyDrocephalus.
Fluids and barriers of the CNS, 2014Co-Authors: Namiko Nishida, Yoshihiro Urade, Mitsuhito Mase, Nanae Nagata, Hiroki Toda, Naoto Jingami, Kengo Uemura, Akihiko Ozaki, Sadayuki Matsumoto, Koichi IwasakiAbstract:BackgrounD IDiopathic normal pressure hyDrocephalus (iNPH) is a treatable cause of Dementia, gait Disturbance, anD urinary incontinence in elDerly patients with ventriculomegaly. Its unique morphological feature, calleD Disproportionately enlargeD subarachnoiD-space hyDrocephalus (DESH), may also be a Diagnostic feature. Lipocalin-type ProstaglanDin D synthase (L-PGDS) is a major cerebrospinal fluiD (CSF) protein proDuceD by arachnoiD cells, anD its concentration in the CSF is reporteDly DecreaseD in iNPH. L-PGDS acts as a ProstaglanDin D2-proDucing enzyme anD behaves as a chaperone to prevent the neurotoxic aggregation of amyloiD beta (Aβ) implicateD in Alzheimer’s Disease, a major comorbiDity of iNPH. The aim of this stuDy was to confirm the L-PGDS Decrease in DESH-type iNPH anD to clarify its relationship with clinico-raDiological features or other CSF biomarkers.
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Hematopoietic ProstaglanDin D synthase (H-PgDs) is expresseD in the early embryonic gonaD anD participates to the initial nuclear translocation of the SOX9 protein
Developmental dynamics : an official publication of the American Association of Anatomists, 2011Co-Authors: Brigitte Moniot, Yoshihiro Urade, Kosuke Aritake, Naomi Eguchi, Andalib Farhat, Faustine Declosmenil, Serge Nef, Francis Poulat, Brigitte Boizet-bonhoureAbstract:In mammals, the ProstaglanDin D(2) (PGD(2) ) signaling pathway is involveD in male gonaDal Development, regulating Sox9 gene expression anD SOX9 protein subcellular localization through lipocalin ProstaglanDin D synthase (L-PgDs) activity. Nevertheless, because L-PgDs is Downstream of Sox9, its expression cannot explain the initial nuclear translocation of the SOX9 protein. Here, we show that another source of PGD(2) , hematopoietic-PgDs (H-PgDs) enzyme is expresseD in somatic anD germ cells of the embryonic gonaD of both sexes, as early as embryonic Day (E) 10.5, before the onset of L-PgDs expression. Inhibition of H-PgDs activity by the specific HQL-79 inhibitor leaDs to impaireD nuclear translocation of SOX9 protein in E11.5 Sertoli cells. Furthermore, analysis of H-PgDs(-/-) male embryonic gonaDs confirms abnormal subcellular localization of SOX9 protein at the E11.5 early stage of mouse testicular Differentiation suggesting a role for H-PgDs-proDuceD PGD(2) in the initial nuclear translocation of SOX9.
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InDuction of lipocalin-type ProstaglanDin D synthase in mouse heart unDer hypoxemia.
Biochemical and biophysical research communications, 2009Co-Authors: Feng Han, Yoshihiro Urade, Kazuhisa Takeda, Kazunobu Ishikawa, Masao Ono, Fumiko Date, Satoru Yokoyama, Kazumichi Furuyama, Yotaro Shinozawa, Shigeki ShibaharaAbstract:Hypoxemia is a common manifestation of various DisorDers anD generates pressure overloaD to the heart. Here we analyzeD the expression of lipocalin-type ProstaglanDin D synthase (L-PGDS) in the heart of C57BL/6 mice kept unDer normobaric hypoxia (10% O2) that generates hemoDynamic stress. Northern anD Western blot analyses revealeD that the expression levels of L-PGDS mRNA anD protein were significantly increaseD (>twofolD) after 14 Days of hypoxia, compareD to the mice kept unDer normoxia. Immunohistochemical analysis inDicateD that L-PGDS was increaseD in the myocarDium of auricles anD ventricles anD the pulmonary venous myocarDium at 28 Days of hypoxia. Moreover, using C57BL/6 mice lacking heme oxygenase-2 (HO-2−/−), a moDel of chronic hypoxemia, we showeD that the expression level of L-PGDS protein was twofolD higher in the heart than that of wilD-type mouse. L-PGDS expression is inDuceD in the myocarDium unDer hypoxemia, which may reflect the aDaptation to the hemoDynamic stress.
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lipocalin ProstaglanDin D synthase is a critical beneficial factor in transient anD permanent focal cerebral ischemia
Neuroscience, 2009Co-Authors: Sofiyan Saleem, Yoshihiro Urade, Zahoor A. Shah, Sylvain DoréAbstract:ProstaglanDin D(2) (PGD(2)) is the most abunDant ProstaglanDin proDuceD in the brain. It is a metabolite of arachiDonic aciD anD synthesizeD by ProstaglanDin D(2) synthases (PGDS) via the cyclooxygenase pathway. Two Distinct types of PGDS have been iDentifieD: hematopoietic ProstaglanDin D synthase (H-PGDS) anD lipocalin-type ProstaglanDin D synthase (L-PGDS). Because relatively little is known about the role of L-PGDS in the CNS, here we examineD the outcomes in L-PGDS knockout anD wilD-type (WT) mice after two Different cerebral ischemia moDels, transient miDDle cerebral artery (MCA) occlusion (tMCAO) anD permanent Distal miDDle cerebral artery occlusion (pMCAO). In the tMCAO moDel, the MCA was occluDeD with a monofilament for 90 min anD then reperfuseD for 4 Days. In the pMCAO moDel, the Distal part of the MCA was permanently occluDeD anD the mice were sacrificeD after 7 Days. Percent correcteD infarct volume anD neurological score were DetermineD after 4 anD 7 Days, respectively. L-PGDS knockout mice haD significantly greater infarct volume anD brain eDema than DiD WT mice after tMCAO (P<0.01). Similarly, L-PGDS knockout mice showeD greater infarct volume anD neurological Deficits as compareD to their WT counterparts after pMCAO (P<0.01). Using the two moDels enableD us to stuDy the role of L-PGDS in both early (tMCAO) anD DelayeD (pMCAO) ischemic processes. Our finDings suggest that L-PGDS is beneficial for protecting the brain against transient anD permanent cerebral ischemia. These results proviDe a better unDerstanDing of the role playeD by the enzymes that control eicosanoiD synthesis anD how they can be utilizeD as potential targets to prevent Damage following either acute or potentially chronic neurological DisorDers.
Osamu Hayaishi - One of the best experts on this subject based on the ideXlab platform.
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Cloning, Expression, Crystallization, anD Preliminary X-Ray Analysis of Recombinant Mouse Lipocalin-type ProstaglanDin D Synthase, a Somnogen-ProDucing Enzyme
Journal of biochemistry, 2003Co-Authors: Daisuke Irikura, Osamu Hayaishi, Takashi Kumasaka, Masaki Yamamoto, Hideo Ago, Masashi Miyano, Kilunga Bruno Kubata, Hiroaki Sakai, Yoshihiro UradeAbstract:Lipocalin-type ProstaglanDin D synthase is the key enzyme for the proDuction of ProstaglanDin D 2 , a potent enDogenous somnogen, in the brain. We cloneD, proDuceD, anD crystallizeD the native enzyme anD selenomethionyl Cys 6 5 Ala mutants of the recombinant mouse protein by the hanging Drop vapor-Diffusion methoD with both malonate anD citrate as precipitants. The native crystals obtaineD with malonate belong to orthorhombic space group P2 1 2 1 2 1 with lattice constants a = 46.2, b = 66.8, anD c = 105.3 A. The selenomethionyl crystals obtaineD with citrate belong to orthorhombic space group C222 1 with lattice constants a = 45.5, b = 66.8, anD c = 104.5 A. The native crystals DiffracteD beyonD 2.1 A resolution.
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Cellular localization of lipocalin-type ProstaglanDin D synthase (?-trace) in the central nervous system of the aDult rat
The Journal of comparative neurology, 2000Co-Authors: Carsten T. Beuckmann, Michael Lazarus, Dmitry Gerashchenko, Akira Mizoguchi, Sakashi Nomura, Ikuko Mohri, Akira Uesugi, Takeshi Kaneko, Noboru Mizuno, Osamu HayaishiAbstract:We applieD high-resolution laser-scanning microscopy, electron microscopy, anD non-raDioactive in situ hybriDization histochemistry to Determine the cellular anD intracellular localization of lipocalin-type ProstaglanDin D synthase, the major brain-DeriveD protein component of cerebrospinal fluiD, anD its mRNA in leptomeninges, choroiD plexus, anD parenchyma of the aDult rat brain. Both immunoreactivity anD mRNA for ProstaglanDin D synthase were locateD in arachnoiD barrier cells, arachnoiD trabecular cells, anD arachnoiD pia mater cells. Furthermore, meningeal macrophages anD perivascular microglial cells, iDentifieD by use of ED2 antiboDy, were immunopositive for ProstaglanDin D synthase. In the arachnoiD trabecular cells, the immunoreactivity for ProstaglanDin D synthase was locateD in the nuclear envelope, Golgi apparatus, anD secretory vesicles, inDicating the active proDuction anD secretion of ProstaglanDin D synthase. In the meningeal macrophages, ProstaglanDin D synthase was not founD arounD the nucleus but in lysosomes in the cytoplasm, pointing to an uptake of the protein from the cerebrospinal fluiD. Furthermore, the existence of meningeal cyclooxygenase (COX) -1 anD COX-2 was investigateD by Western blot, Northern blot, anD reverse transcriptase—polymerase chain reaction (RT-PCR), anD the colocalization of COX-2 anD ProstaglanDin D synthase was DemonstrateD in virtually all cells of the leptomeninges, choroiD plexus epithelial cells, anD perivascular microglial cells, suggesting that these cells synthesize ProstaglanDin D2 actively. Alternatively, oligoDenDrocytes showeD ProstaglanDin D synthase immunoreactivity without Detectable COX-2. The localization of lipocalin-type ProstaglanDin D synthase in meningeal cells anD its colocalization with COX-2 proviDe eviDence for its function as a ProstaglanDin D2-proDucing enzyme. J. Comp. Neurol. 428:62–78, 2000. © 2000 Wiley-Liss, Inc.
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cellular localization of lipocalin type ProstaglanDin D synthase trace in the central nervous system of the aDult rat
The Journal of Comparative Neurology, 2000Co-Authors: Carsten T. Beuckmann, Michael Lazarus, Dmitry Gerashchenko, Akira Mizoguchi, Sakashi Nomura, Ikuko Mohri, Akira Uesugi, Takeshi Kaneko, Noboru Mizuno, Osamu HayaishiAbstract:We applieD high-resolution laser-scanning microscopy, electron microscopy, anD non-raDioactive in situ hybriDization histochemistry to Determine the cellular anD intracellular localization of lipocalin-type ProstaglanDin D synthase, the major brain-DeriveD protein component of cerebrospinal fluiD, anD its mRNA in leptomeninges, choroiD plexus, anD parenchyma of the aDult rat brain. Both immunoreactivity anD mRNA for ProstaglanDin D synthase were locateD in arachnoiD barrier cells, arachnoiD trabecular cells, anD arachnoiD pia mater cells. Furthermore, meningeal macrophages anD perivascular microglial cells, iDentifieD by use of ED2 antiboDy, were immunopositive for ProstaglanDin D synthase. In the arachnoiD trabecular cells, the immunoreactivity for ProstaglanDin D synthase was locateD in the nuclear envelope, Golgi apparatus, anD secretory vesicles, inDicating the active proDuction anD secretion of ProstaglanDin D synthase. In the meningeal macrophages, ProstaglanDin D synthase was not founD arounD the nucleus but in lysosomes in the cytoplasm, pointing to an uptake of the protein from the cerebrospinal fluiD. Furthermore, the existence of meningeal cyclooxygenase (COX) -1 anD COX-2 was investigateD by Western blot, Northern blot, anD reverse transcriptase—polymerase chain reaction (RT-PCR), anD the colocalization of COX-2 anD ProstaglanDin D synthase was DemonstrateD in virtually all cells of the leptomeninges, choroiD plexus epithelial cells, anD perivascular microglial cells, suggesting that these cells synthesize ProstaglanDin D2 actively. Alternatively, oligoDenDrocytes showeD ProstaglanDin D synthase immunoreactivity without Detectable COX-2. The localization of lipocalin-type ProstaglanDin D synthase in meningeal cells anD its colocalization with COX-2 proviDe eviDence for its function as a ProstaglanDin D2-proDucing enzyme. J. Comp. Neurol. 428:62–78, 2000. © 2000 Wiley-Liss, Inc.
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BinDing of BiliverDin, Bilirubin, anD ThyroiD Hormones to Lipocalin-Type ProstaglanDin D Synthase†
Biochemistry, 1999Co-Authors: Carsten T. Beuckmann, Osamu Hayaishi, Masaaki Aoyagi, Issay Okazaki, Takaaki Hiroike, Hiroyuki Toh, Yoshihiro UradeAbstract:Lipocalin-type ProstaglanDin D synthase is a major protein of the cerebrospinal fluiD anD was originally known as β-trace. We investigateD the binDing ability of ProstaglanDin D synthase towarD bile pigments, thyroiD hormones, steroiD hormones, anD fatty aciDs in this present stuDy. We founD that the recombinant enzyme binDs bile pigments anD thyroiD hormones, resulting in quenching of the intrinsic tryptophan fluorescence, the appearance of inDuceD circular Dichroism of the lipophilic liganDs, anD a reD shift of the absorption spectra of bilirubin anD biliverDin. The binDing of ProstaglanDin D synthase to lipophilic liganDs was also DemonstrateD by the resonant mirror technique anD surface plasmon resonance Detection. The Dissociation constants were calculateD to be 33 nM, 37 nM, 660 nM, 820 nM, anD 2.08 μM for biliverDin, bilirubin, l-thyroxine, 3,3‘,5‘-triioDo-l-thyronine, anD 3,3‘,5-triioDo-l-thyronine, respectively. BiliverDin anD bilirubin unDerwent a shift in their absorption peaks from 375 to 380 ...
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Lipocalin-type ProstaglanDin D Synthase (β-Trace) Is a Newly RecognizeD Type of RetinoiD Transporter
The Journal of biological chemistry, 1997Co-Authors: Toshiki Tanaka, Yoshihiro Urade, Naomi Eguchi, Hiromi Kimura, Akemi Nishikawa, Osamu HayaishiAbstract:Abstract Lipocalin-type ProstaglanDin D synthase is responsible for the biosynthesis of ProstaglanDin D2in the central nervous system anD the genital organs anD is secreteD into the cerebrospinal fluiD anD the seminal plasma as β-trace. Here we analyzeD retinoiDs binDing of the enzyme by monitoring the fluorescence quenching of an intrinsic tryptophan resiDue, anD appearance of circular Dichroism arounD 330 nm, anD a reD shift of the UV absorption spectra of retinoiDs. We founD that the enzyme binDs all-trans- or 9-cis-retinoic aciD anD all-trans- or 13-cis-retinal, but not all-trans-retinol, with affinities (K Dof 70–80 nm) sufficient for function as a retinoiD transporter. All-trans-retinoic aciD inhibiteD the enzyme activity in a noncompetitive manner, suggesting that it binDs to the same hyDrophobic pocket as ProstaglanDin H2, the substrate for ProstaglanDin D synthase, but at a Different site in this pocket. It is likely that this enzyme is a bifunctional protein that acts as both retinoiD transporter anD ProstaglanDin D2-proDucing enzyme.
Naomi Eguchi - One of the best experts on this subject based on the ideXlab platform.
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Hematopoietic ProstaglanDin D synthase (H-PgDs) is expresseD in the early embryonic gonaD anD participates to the initial nuclear translocation of the SOX9 protein
Developmental dynamics : an official publication of the American Association of Anatomists, 2011Co-Authors: Brigitte Moniot, Yoshihiro Urade, Kosuke Aritake, Naomi Eguchi, Andalib Farhat, Faustine Declosmenil, Serge Nef, Francis Poulat, Brigitte Boizet-bonhoureAbstract:In mammals, the ProstaglanDin D(2) (PGD(2) ) signaling pathway is involveD in male gonaDal Development, regulating Sox9 gene expression anD SOX9 protein subcellular localization through lipocalin ProstaglanDin D synthase (L-PgDs) activity. Nevertheless, because L-PgDs is Downstream of Sox9, its expression cannot explain the initial nuclear translocation of the SOX9 protein. Here, we show that another source of PGD(2) , hematopoietic-PgDs (H-PgDs) enzyme is expresseD in somatic anD germ cells of the embryonic gonaD of both sexes, as early as embryonic Day (E) 10.5, before the onset of L-PgDs expression. Inhibition of H-PgDs activity by the specific HQL-79 inhibitor leaDs to impaireD nuclear translocation of SOX9 protein in E11.5 Sertoli cells. Furthermore, analysis of H-PgDs(-/-) male embryonic gonaDs confirms abnormal subcellular localization of SOX9 protein at the E11.5 early stage of mouse testicular Differentiation suggesting a role for H-PgDs-proDuceD PGD(2) in the initial nuclear translocation of SOX9.
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Association of Serum Lipocalin-Type ProstaglanDin D Synthase Levels with Subclinical Atherosclerosis in UntreateD Asymptomatic Subjects
Hypertension research : official journal of the Japanese Society of Hypertension, 2008Co-Authors: Yoshikazu Miwa, Hiroshi Oda, Naomi Eguchi, Yasuhiko Shiina, Kentaro Shikata, Motoo Tsushima, Satomi Nakano, Taro Maruyama, Shingo Kyotani, Yoshihiro UradeAbstract:Association of Serum Lipocalin-Type ProstaglanDin D Synthase Levels with Subclinical Atherosclerosis in UntreateD Asymptomatic Subjects
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Lipocalin-type ProstaglanDin D synthase as a melanocyte marker regulateD by MITF.
Biochemical and biophysical research communications, 2005Co-Authors: Kazuhisa Takeda, Naomi Eguchi, Miki Yoshizawa, Feng Han, Satoru Yokoyama, Hiroyuki Aburatani, Takayuki Masuda, Naomi Yamaki, Hiroaki Yamamoto, Yoshihiro UradeAbstract:Abstract Microphthalmia-associateD transcription factor (MITF) is responsible for Differentiation of melanocytes. A recessive MITF mutant, black-eyeD white Mitfmi-bw mouse, is characterizeD by white coat color anD Deafness, Due to the lack of melanocytes in the skin anD inner ears. By cDNA microarray analysis, we have iDentifieD lipocalin-type ProstaglanDin D synthase (L-PGDS), whose mRNA is unDetectable in the homozygous Mitfmi-bw skin. Immunohistochemical analysis of wilD-type mice iDentifieD the specific expression of L-PGDS in follicular melanocytes. L-PGDS mRNA is expresseD in B16 mouse melanoma cells, but unDetectable in human melanoma cell lines. RNA interference analysis against MITF suggests that L-PGDS expression is DepenDent on MITF in B16 melanoma cells. Furthermore, we have proviDeD eviDence that MITF is involveD in the melanocyte lineage-specific transcription of the mouse L-PGDS gene. Thus, L-PGDS represents a newly iDentifieD melanocyte marker. MITF may moDulate the proDuction of ProstaglanDin D2 by activating the L-PGDS gene in melanocytes.
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Lipocalin-type ProstaglanDin D synthase in urine in aDriamycin-inDuceD nephropathy of mice.
Nephron. Physiology, 2004Co-Authors: Takamasa Tsuchida, Yoshihiro Urade, Yutaka Eguchi, Hiroshi Oda, Kousuke Seiki, Naomi Eguchi, Atsushi Numabe, Hiroshi Nakajima, Rie Hakamada-taguchi, Yoshio UeharaAbstract:BackgrounD/Aims: Lipocalin-type ProstaglanDin D synthase (L-PGDS), an enzyme converting ProstaglanDin H2 to ProstaglanDin D2, occurs particularly in the carDio
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Changes of lipocalin-type ProstaglanDin D synthase level During pregnancy.
The journal of obstetrics and gynaecology research, 2004Co-Authors: Yasuhiko Shiki, Hiroshi Oda, Naomi Eguchi, Koichiro Shimoya, Yoshihiro Tokugawa, Tadashi Kimura, Masayasu Koyama, Chihiro Azuma, Yuji Murata, Yoshihiro UradeAbstract:AIM: ProstaglanDin D (PGD), synthesizeD by lipocalin-type ProstaglanDin D synthase (L-PGDS), has markeD effects on a number of biological processes, incluDing the prevention of platelet aggregation anD the relaxation of vascular smooth muscle. The aim of the stuDy presenteD here was to examine the significance of L-PGDS in human pregnancy. METHODS: We measureD the concentration of plasma L-PGDS in pregnant anD non-pregnant women, anD the concentration of L-PGDS in the umbilical corD blooD, amniotic fluiD anD urine of newborns by enzyme-linkeD immunoabsorbent assay. To Determine the localization of L-PGDS, we performeD immunohistochemical analysis. To evaluate the usefulness of Diagnosis of rupture of membranes (ROM), we DetermineD the concentration of L-PGDS in cervicovaginal secretions. RESULTS: Pregnant women anD non-pregnant women haD similar L-PGDS concentrations (0.57 +/- 0.13 microg/mL vs 0.53 +/- 0.07 microg/mL). Umbilical corD blooD, amniotic fluiD anD newborn urine containeD higher L-PGDS concentrations (1.87 +/- 0.73 microg/mL, 2.62 +/- 0.86 microg/mL, 6.31 +/- 4.62 microg/mL, respectively) than maternal blooD. The concentration of L-PGDS in amniotic fluiD from 19 weeks onwarD was significantly greater than that at 15-18 weeks (3.201 +/- 0.384 microg/mL, n = 6 vs 1.735 +/- 0.477 microg/mL, n = 4; P < 0.05). Immunohistochemistry revealeD that the amniotic cells of the placenta expresseD L-PGDS. The sources of L-PGDS in amniotic fluiD are fetus urine anD amniotic cells. The concentration of L-PGDS in cervicovaginal secretions with rupture of membrane (ROM) were significantly higher than those without ROM. CONCLUSION: The measurement of L-PGDS in cervicovaginal fluiD was useful in the Detection of ROM During pregnancy.
Hidero Kitasato - One of the best experts on this subject based on the ideXlab platform.
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Inhibition of monosoDium urate monohyDrate crystal–inDuceD acute inflammation by retrovirally transfecteD ProstaglanDin D synthase
Arthritis and rheumatism, 2003Co-Authors: Yousuke Murakami, Tohru Akahoshi, Izumi Hayashi, Hirahito Endo, Atsushi Hashimoto, Shizuka Kono, Hirobumi Kondo, Shinichi Kawai, Matsuhisa Inoue, Hidero KitasatoAbstract:Objective Hematopoietic ProstaglanDin D synthase (H-PGDS) is a key enzyme in the proDuction of ProstaglanDin D anD its J series metabolites. We evaluateD the antiinflammatory effect of retrovirally transfecteD H-PGDS in orDer to investigate the role of H-PGDS in monosoDium urate monohyDrate (MSU) crystal–inDuceD acute inflammation. MethoDs Expression of enDogenous PGDS in a murine air-pouch moDel of MSU crystal–inDuceD acute inflammation was DetermineD by real-time polymerase chain reaction. H-PGDS complementary DNA (cDNA) was retrovirally transfecteD into C57BL/6J fibroblasts, anD the cells were DesignateD as C57-PGDS cells. ProDuction of ProstaglanDins by C57-PGDS cells was measureD by enzyme immunoassay. The effect of C57-PGDS cells on crystal-inDuceD inflammation was investigateD. Results Injection of the crystals causeD a rapiD Decrease in H-PGDS expression by infiltrating cells anD by the soft tissues arounD the air pouches. In contrast, expression of interleukin-1β (IL-1β) anD macrophage inflammatory protein 2 (MIP-2) as well as cellular infiltration were significantly increaseD During the early stage of inflammation. C57-PGDS cells, but not control cells, proDuceD an increaseD amount of PGD2 in vitro, but suppresseD proDuction of PGE2. Injection of C57-PGDS cells into air pouches inhibiteD cellular infiltration anD MIP-2 anD IL-1β expression. Conclusion In this murine air-pouch moDel of MSU crystal–inDuceD inflammation, retrovirally transfecteD H-PGDS cDNA coulD reDuce cellular infiltration, at least partly by inhibiting MIP-2 anD IL-1β. These finDings suggest that gene therapy with H-PGDS may be useful for treating inflammatory Diseases.
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inhibition of monosoDium urate monohyDrate crystal inDuceD acute inflammation by retrovirally transfecteD ProstaglanDin D synthase
Arthritis & Rheumatism, 2003Co-Authors: Yousuke Murakami, Tohru Akahoshi, Izumi Hayashi, Hirahito Endo, Atsushi Hashimoto, Shizuka Kono, Hirobumi Kondo, Shinichi Kawai, Matsuhisa Inoue, Hidero KitasatoAbstract:Objective Hematopoietic ProstaglanDin D synthase (H-PGDS) is a key enzyme in the proDuction of ProstaglanDin D anD its J series metabolites. We evaluateD the antiinflammatory effect of retrovirally transfecteD H-PGDS in orDer to investigate the role of H-PGDS in monosoDium urate monohyDrate (MSU) crystal–inDuceD acute inflammation. MethoDs Expression of enDogenous PGDS in a murine air-pouch moDel of MSU crystal–inDuceD acute inflammation was DetermineD by real-time polymerase chain reaction. H-PGDS complementary DNA (cDNA) was retrovirally transfecteD into C57BL/6J fibroblasts, anD the cells were DesignateD as C57-PGDS cells. ProDuction of ProstaglanDins by C57-PGDS cells was measureD by enzyme immunoassay. The effect of C57-PGDS cells on crystal-inDuceD inflammation was investigateD. Results Injection of the crystals causeD a rapiD Decrease in H-PGDS expression by infiltrating cells anD by the soft tissues arounD the air pouches. In contrast, expression of interleukin-1β (IL-1β) anD macrophage inflammatory protein 2 (MIP-2) as well as cellular infiltration were significantly increaseD During the early stage of inflammation. C57-PGDS cells, but not control cells, proDuceD an increaseD amount of PGD2 in vitro, but suppresseD proDuction of PGE2. Injection of C57-PGDS cells into air pouches inhibiteD cellular infiltration anD MIP-2 anD IL-1β expression. Conclusion In this murine air-pouch moDel of MSU crystal–inDuceD inflammation, retrovirally transfecteD H-PGDS cDNA coulD reDuce cellular infiltration, at least partly by inhibiting MIP-2 anD IL-1β. These finDings suggest that gene therapy with H-PGDS may be useful for treating inflammatory Diseases.
Hiroshi Oda - One of the best experts on this subject based on the ideXlab platform.
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Association of Serum Lipocalin-Type ProstaglanDin D Synthase Levels with Subclinical Atherosclerosis in UntreateD Asymptomatic Subjects
Hypertension research : official journal of the Japanese Society of Hypertension, 2008Co-Authors: Yoshikazu Miwa, Hiroshi Oda, Naomi Eguchi, Yasuhiko Shiina, Kentaro Shikata, Motoo Tsushima, Satomi Nakano, Taro Maruyama, Shingo Kyotani, Yoshihiro UradeAbstract:Association of Serum Lipocalin-Type ProstaglanDin D Synthase Levels with Subclinical Atherosclerosis in UntreateD Asymptomatic Subjects
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Lipocalin-type ProstaglanDin D synthase in urine in aDriamycin-inDuceD nephropathy of mice.
Nephron. Physiology, 2004Co-Authors: Takamasa Tsuchida, Yoshihiro Urade, Yutaka Eguchi, Hiroshi Oda, Kousuke Seiki, Naomi Eguchi, Atsushi Numabe, Hiroshi Nakajima, Rie Hakamada-taguchi, Yoshio UeharaAbstract:BackgrounD/Aims: Lipocalin-type ProstaglanDin D synthase (L-PGDS), an enzyme converting ProstaglanDin H2 to ProstaglanDin D2, occurs particularly in the carDio
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Changes of lipocalin-type ProstaglanDin D synthase level During pregnancy.
The journal of obstetrics and gynaecology research, 2004Co-Authors: Yasuhiko Shiki, Hiroshi Oda, Naomi Eguchi, Koichiro Shimoya, Yoshihiro Tokugawa, Tadashi Kimura, Masayasu Koyama, Chihiro Azuma, Yuji Murata, Yoshihiro UradeAbstract:AIM: ProstaglanDin D (PGD), synthesizeD by lipocalin-type ProstaglanDin D synthase (L-PGDS), has markeD effects on a number of biological processes, incluDing the prevention of platelet aggregation anD the relaxation of vascular smooth muscle. The aim of the stuDy presenteD here was to examine the significance of L-PGDS in human pregnancy. METHODS: We measureD the concentration of plasma L-PGDS in pregnant anD non-pregnant women, anD the concentration of L-PGDS in the umbilical corD blooD, amniotic fluiD anD urine of newborns by enzyme-linkeD immunoabsorbent assay. To Determine the localization of L-PGDS, we performeD immunohistochemical analysis. To evaluate the usefulness of Diagnosis of rupture of membranes (ROM), we DetermineD the concentration of L-PGDS in cervicovaginal secretions. RESULTS: Pregnant women anD non-pregnant women haD similar L-PGDS concentrations (0.57 +/- 0.13 microg/mL vs 0.53 +/- 0.07 microg/mL). Umbilical corD blooD, amniotic fluiD anD newborn urine containeD higher L-PGDS concentrations (1.87 +/- 0.73 microg/mL, 2.62 +/- 0.86 microg/mL, 6.31 +/- 4.62 microg/mL, respectively) than maternal blooD. The concentration of L-PGDS in amniotic fluiD from 19 weeks onwarD was significantly greater than that at 15-18 weeks (3.201 +/- 0.384 microg/mL, n = 6 vs 1.735 +/- 0.477 microg/mL, n = 4; P < 0.05). Immunohistochemistry revealeD that the amniotic cells of the placenta expresseD L-PGDS. The sources of L-PGDS in amniotic fluiD are fetus urine anD amniotic cells. The concentration of L-PGDS in cervicovaginal secretions with rupture of membrane (ROM) were significantly higher than those without ROM. CONCLUSION: The measurement of L-PGDS in cervicovaginal fluiD was useful in the Detection of ROM During pregnancy.
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Lipocalin-type ProstaglanDin D synthase (beta-trace) in cerebrospinal fluiD: a useful marker for the Diagnosis of normal pressure hyDrocephalus.
Neuroscience research, 2003Co-Authors: Mitsuhito Mase, Hiroshi Oda, Naomi Eguchi, Takashi Inui, Kazuo Yamada, Naoki Shimazu, Kosuke Seiki, Hiroya Nakau, Yoshihiro UradeAbstract:Abstract Lipocalin-type ProstaglanDin D synthase (PGDS) is consiDereD to be mainly proDuceD in the leptomeninges anD secreteD into cerebrospinal fluiD (CSF). We founD PGDS levels in CSF of patients with normal pressure hyDrocephalus (NPH) (8.99±2.59 μg/ml, mean±S.D., n=14) to be significantly lower than levels in a control (15.29±5.17, n=14, P
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Lipocalin-Type ProstaglanDin D Synthase in Essential Hypertension
Hypertension, 2002Co-Authors: Nobuhito Hirawa, Yoshio Uehara, Minoru Yamakado, Yoshiyuki Toya, Tomoko Gomi, Toshio Ikeda, Yutaka Eguchi, Masao Takagi, Hiroshi Oda, Kousuke SeikiAbstract:Lipocalin-type ProstaglanDin D synthase (L-PGDS) reporteDly well preDicts carDiovascular injuries in humans. However, little is known about the implications of L-PGDS in hypertension. In the presen...
