Transport of prostaglandin D2 into brain

Suzuki, Fumio; Hayashi, Hideya; Hayaishi, Osamu

doi:10.1016/0006-8993(86)91079-6

Cited by 40 publications

(25 citation statements)

References 21 publications

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“…Although there is a substantial literature on carrier-mediated PG transport in other species (19)(20)(21)(22)(23)(24)(25)(26)(27)(28)(29)(30)(31)(32)(33)(34)(35)(36), there is surprisingly little information about this phenomenon in humans, perhaps because of difficulty in obtaining tissue for such studies. PGE 2 has been shown to be transported by the isolated perfused human placental cotyledon (52) and by the isolated human amnion (35).…”

Section: Discussionmentioning

confidence: 99%

“…Accordingly, PG transport is carrier-mediated in many diverse tissues, including the lung (19)(20)(21)(22), choroid plexus (23)(24)(25)(26)(27)(28), liver (29), anterior chamber of the eye (23)(24)(25)30), vagina and uterus (31)(32)(33), and placenta (34,35). Indeed, our laboratory recently identified rat prostaglandin transporter (PGT), 1 the first cloned carrier known to catalyze the transport of PGE and PGF 2 ␣ (36).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Cloning, in vitro expression, and tissue distribution of a human prostaglandin transporter cDNA(hPGT).

Lu¹,

Kanai²,

Bao³

et al. 1996

J. Clin. Invest.

212

138

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We recently identified a cDNA in the rat that encodes a broadly expressed PG transporter (PGT). Because PGs play diverse and important roles in human health and disease, we cloned human PGT (hPGT) from an adult human kidney cDNA library. A consensus sequence (4.0 kb) derived from several clones, plus 3 Ј polymerase chain reaction amplification, exhibited 74% nucleic acid identity and 82% amino acid identity compared to rat PGT. When transiently expressed in HeLa cells, a full-length clone catalyzed the transport of PGE 1 , PGE 2 , PGD 2 , PGF 2 ␣ and, to a lesser degree TXB 2 . Northern blotting revealed mRNA transcripts of many different sizes in adult human heart, placenta, brain, lung, liver, skeletal muscle, pancreas, kidney, spleen, prostate, ovary, small intestine, and colon. hPGT mRNAs are also strongly expressed in human fetal brain, lung, liver, and kidney. The broad tissue distribution and substrate profile of hPGT suggest a role in the transport and/or metabolic clearance of PGs in diverse human tissues. ( J. Clin. Invest.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Cloning, in vitro expression, and tissue distribution of a human prostaglandin transporter cDNA(hPGT).

Lu¹,

Kanai²,

Bao³

et al. 1996

J. Clin. Invest.

212

138

View full text Add to dashboard Cite

show abstract

“…Given that PGD 2 is produced in response to injurious stimuli and is quickly metabolized in vivo (half-life: $1.5 minutes; ref. 16), it is difficult to accurately measure its content in tissues. We previously showed that the urinary concentration of a PGD 2 metabolite, tetranor-PGDM, can be a stable index of PGD 2 production in tissues.…”

Section: Hematopoietic Prostaglandin D Synthase Deficiency Exacerbatementioning

confidence: 99%

Mast Cell–Derived Prostaglandin D2 Inhibits Colitis and Colitis-Associated Colon Cancer in Mice

et al. 2014

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Compared with prostaglandin E 2 , which has an established role in cancer, the role of the COX metabolite prostaglandin D 2 (PGD 2 ) in chronic inflammation leading to tumorigenesis is uncertain. In this study, we investigated the role of PGD 2 in colitis and colitis-associated colon cancer (CAC) using genetically modified mice and an established model of inflammatory colon carcinogenesis. Systemic genetic deficiency in hematopoietic PGD synthase (H-PGDS) aggravated colitis and accelerated tumor formation in a manner associated with increased TNFa expression. Treatment with a TNFa receptor antagonist attenuated colitis regardless of genotype. Histologic analysis revealed that infiltrated mast cells strongly expressed H-PGDS in inflamed colons. Mast cell-specific H-PGDS deficiency also aggravated colitis and accelerated CAC. In contrast, treatment with a PGD 2 receptor agonist inhibited colitis and CAC. Together, our results identified mast cell-derived PGD 2 as an inhibitor of colitis and CAC, with implications for its potential use in preventing or treating colon cancer. Cancer Res; 74(11); 3011-9. Ó2014 AACR.

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“…The apparent half-life of PGD 2 in the blood has been reported to be 1.5 min (11), and PGD 2 is rapidly metabolized in plasma to ⌬ 12 -PGJ 2 , which arises from catalytic conversion of PGJ 2 by albumin (12,13). The importance of ⌬ 12 -PGJ 2 as a systemic PGD 2 metabolite is also underlined by the fact that it can be detected in human urine in relevant amounts, which are increased after i.v.…”

Section: E Osinophils Are Important Effector Cells In Allergic Diseasesmentioning

confidence: 99%

Δ12-Prostaglandin J2, a Plasma Metabolite of Prostaglandin D2, Causes Eosinophil Mobilization from the Bone Marrow and Primes Eosinophils for Chemotaxis

Heinemann

Schuligoi

Sabroe

et al. 2003

The Journal of Immunology

101

138

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PGD2, a major mast cell mediator, is a potent eosinophil chemoattractant and is thought to be involved in eosinophil recruitment to sites of allergic inflammation. In plasma, PGD2 is rapidly transformed into its major metabolite Δ12-PGJ2, the effect of which on eosinophil migration has not yet been characterized. In this study we found that Δ12-PGJ2 was a highly effective chemoattractant and inducer of respiratory burst in human eosinophils, with the same efficacy as PGD2, PGJ2, or 15-deoxy-Δ12,14-PGJ2. Moreover, pretreatment of eosinophils with Δ12-PGJ2 markedly enhanced the chemotactic response to eotaxin, and in this respect Δ12-PGJ2 was more effective than PGD2. Δ12-PGJ2-induced facilitation of eosinophil migration toward eotaxin was not altered by specific inhibitors of intracellular signaling pathways relevant to the chemotactic response, phosphatidylinositol 3-kinase (LY-294002), mitogen-activated protein kinase/extracellular signal-regulated kinase kinase (U-0126), or p38 mitogen-activated protein kinase (SB-202190). Desensitization studies using calcium flux suggested that Δ12-PGJ2 signaled through the same receptor, CRTH2, as PGD2. Finally, Δ12-PGJ2 was able to mobilize mature eosinophils from the bone marrow of the guinea pig isolated perfused hind limb. Given that Δ12-PGJ2 is present in the systemic circulation at relevant levels, a role for this PGD2 metabolite in eosinophil release from the bone marrow and in driving eosinophil recruitment to sites of inflammation appears conceivable.

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Transport of prostaglandin D2 into brain

Cited by 40 publications

References 21 publications

Cloning, in vitro expression, and tissue distribution of a human prostaglandin transporter cDNA(hPGT).

Cloning, in vitro expression, and tissue distribution of a human prostaglandin transporter cDNA(hPGT).

Mast Cell–Derived Prostaglandin D2 Inhibits Colitis and Colitis-Associated Colon Cancer in Mice

Δ12-Prostaglandin J2, a Plasma Metabolite of Prostaglandin D2, Causes Eosinophil Mobilization from the Bone Marrow and Primes Eosinophils for Chemotaxis

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