Brain-type prostaglandin D synthetase occurs in the rat cochlea.

Tachibana, Masayoshi; Fex, Jörgen; Urade, Yoshihiro; Hayaishi, Osamu

doi:10.1073/pnas.84.21.7677

Cited by 30 publications

(20 citation statements)

References 24 publications

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“…Inner ear hair cells play an essential role in the auditory pathway that converts sound stimulation into electrical signals and then into a neural code. In the adult rat cochleas, the L-PGDS immunoreactivity was found in inner and outer hair cells, their supporting cells (Claudius' cells and Deiters' cells), marginal cells, basal cells, and cells of Reissner's membrane (Tachibana et al 1987). However, it remains to be investigated whether L-PGDS is expressed in intermediate cells.…”

Section: Sound Melanocytes Are Required For Sound Sensingmentioning

confidence: 99%

Neuroendocrine Functions of Melanocytes: Beyond the Skin-Deep Melanin Maker

Takeda

Takahashi

Shibahara

2007

Tohoku J. Exp. Med.

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The skin is armored with "dead cells", the stratum corneum, and is continuously exposed to external stressful environments, such as atmospheric oxygen, solar radiations, and thermal and chemical insults. Melanocytes of neural crest origin are located in the skin, eye, inner ear, and leptomeninges. Melanin pigment in the skin is produced by melanocytes under the influence of various endogenous factors, derived from neighboring keratinocytes and underlying fibroblasts. The differentiation and functions of melanocytes are regulated at multiple processes, including transcription, RNA editing, melanin synthesis, and the transport of melanosomes to keratinocytes. Impairment at each step causes the pigmentary disorders in humans, with the historical example of oculocutaneous albinism. Moreover, heterozygous mutations in the gene coding for microphthalmia-associated transcription factor, a key regulator for melanocyte development, are associated with Waardenburg syndrome type 2, an auditory-pigmentary disorder. Sun tanning, melasma, aging spots (lentigo senilis), hair graying, and melanoma are well-known melanocyte-related pathologies. Melanocytes therefore have attracted much attention of many ladies, makeup artists and molecular biologists. More recently, we have shown that lipocalin-type prostaglandin D synthase (L-PGDS) is expressed in melanocytes but not in other skin cell types. L-PGDS generates prostaglandin D 2 and also functions as an inter-cellular carrier protein for lipophilic ligands, such as bilirubin and thyroid hormones. Thus, melanocytes may exert hitherto unknown functions through L-PGDS and prostaglandin D 2 . Here we update the neuroendocrine functions of melanocytes and discuss the possible involvement of melanocytes in the control of the central chemosensor that generates respiratory rhythm.heme; hypoxia; lipocalin-type prostaglandin D synthase; melanocyte; microphthalmia-associated transcription factor

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Section: Sound Melanocytes Are Required For Sound Sensingmentioning

confidence: 99%

Neuroendocrine Functions of Melanocytes: Beyond the Skin-Deep Melanin Maker

Takeda

Takahashi

Shibahara

2007

Tohoku J. Exp. Med.

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“…This enzyme is responsible for biosynthesis of PGD2 in the brain, while several other enzymes, such as GSH-requiring PGD synthase and GSH S-transferase, also catalyze the reaction to produce PGD2 and are present in various other rat tissues (4). The enzyme is localized in the central nervous system (4) and associated tissues, such as the retina (5) and cochlea (6). Furthermore, postnatal changes in the cellular localization of this enzyme have been observed in the brain (7) and cochlea (6).…”

mentioning

confidence: 99%

“…The enzyme is localized in the central nervous system (4) and associated tissues, such as the retina (5) and cochlea (6). Furthermore, postnatal changes in the cellular localization of this enzyme have been observed in the brain (7) and cochlea (6). For example, the enzyme is distributed in most neurons in the brain of 1-to 2-week-old rats, but the major localization site shifts to oligodendrocytes in adult animals (7).…”

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confidence: 99%

Human brain prostaglandin D synthase has been evolutionarily differentiated from lipophilic-ligand carrier proteins.

Nagata

Suzuki

Igarashi

et al. 1991

Proc. Natl. Acad. Sci. U.S.A.

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168

121

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ABSTRACTcDNAs for glutathione-independent prostaglandin D synthase were isolated from cDNA libraries of human brain. The longest cDNA insert was 837 base pairs long and contained a coding region of 570 base pairs corresponding to 190 amino acid residues with a calculated Mr of 21,016. Between two cDNA inserts isolated from the two different libraries, nucleotide substitutions were observed at 16 positions, including conservative amino acid substitutions at 2 positions and nonconservative substitutions at 5 positions, indicating genetic heterogeneity of this enzyme in humans. The computer-assisted homology search revealed that the enzyme is a member of the lipocalin superfamily, comprising secretory hydrophobic molecule transporters, showing the greatest homology (28.8-29.4% identity; 51.3-53.1% similarity) to a1-microglobulin among the members of this superfamily. In a phylogenetic tree of the superfamily, this enzyme, a,-microglobulin, and the y chain of the complement component C8 form a cluster separate from the other 14 members. The two distinctive characteristics of glutathione-independent prostaglandin D synthase, as compared to the other members ofthis superfamily, are its enzymatic properties and its association with membranes that were probably acquired after evolutionary divergence of the two lipocalins. Based on the observed sequence homology, the tertiary structure of the enzyme was deduced to consist of an eight-stranded anti-parallel ,B-barrel forming a hydrophobic pocket. Furthermore, the Cys-65 residue in the pocket, which is conserved only in the human and rat enzymes but not in other lipocalins, was considered to be a putative active site of the enzyme.Prostaglandin (PG) D2 is a major PG in rat brain and shows several central actions in vivo such as sleep induction, regulation of body temperature, anticonvulsion, suppression of luteinizing hormone release, nociception, and modulation of odor responses. In vitro it also regulates the growth and differentiation of rat glioma C6BU-1 cells and induces Ca2+ influx and cGMP formation in mouse neuroblastoma-rat glioma hybrid NG108-15 cells (for reviews, see refs. 1 and 2). In brief, PGD2 functions as a neuromodulator and/or trophic factor in the central nervous system. Glutathione (GSH)-independent PGD synthase [prostaglandin-H2 D-isomerase; (5Z,13E)-(15S)-9a,11a-epidioxy-15-hydroxyprosta-5,13-dienoate D-isomerase, EC 5.3.99.2] catalyzes the conversion of PGH2 to PGD2 in the presence of various sulfhydryl compounds (3). This enzyme is responsible for biosynthesis of PGD2 in the brain, while several other enzymes, such as GSH-requiring PGD synthase and GSH S-transferase, also catalyze the reaction to produce PGD2 and are present in various other rat tissues (4). The enzyme is localized in the central nervous system (4) and associated tissues, such as the retina (5) and cochlea (6). Furthermore, postnatal changes in the cellular localization of this enzyme have been observed in the brain (7) and cochlea (6). For example, the enzyme is distributed in m...

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“…1). Among several enzymes catalyzing the conversion of PGH2 to PGD2, glutathioneindependent PGD synthase [prostaglandin-H2 D-isomerase; (5Z,13E)-(15S)-9a,lla-epidioxy-15-hydroxyprosta-5,13-dienoate D-isomerase, EC 5.3.99.2] (2) is responsible for biosynthesis of PGD2 in the central nervous system (3), retina (4), and cochlea (5). Immunocytochemical studies with a polyclonal and two monoclonal anti-rat brain PGD synthase antibodies revealed that the major cellular location of the enzyme in the brain shifts postnatally from neurons of 1-to 2-week-old rats to oligodendrocytes in adult animals (6), suggesting that the enzyme may have distinct functions in those cells at each specific developmental stage and thus plays important roles in both maturation and maintenance of the central nervous system.…”

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confidence: 99%

Dominant expression of mRNA for prostaglandin D synthase in leptomeninges, choroid plexus, and oligodendrocytes of the adult rat brain.

Urade

Kitahama

Ohishi

et al. 1993

Proc. Natl. Acad. Sci. U.S.A.

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228

147

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Glutathione-independent prostaglandin D synthase [prostaglandin-H2 D-isomerase; (5Z,13E)-(15S)-9a,lla-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. (2) is responsible for biosynthesis of PGD2 in the central nervous system (3), retina (4), and cochlea (5). Immunocytochemical studies with a polyclonal and two monoclonal anti-rat brain PGD synthase antibodies revealed that the major cellular location of the enzyme in the brain shifts postnatally from neurons of 1-to 2-week-old rats to oligodendrocytes in adult animals (6), suggesting that the enzyme may have distinct functions in those cells at each specific developmental stage and thus plays important roles in both maturation and maintenance of the central nervous system.We previously isolated cDNAs encoding this enzyme in the brain of rats (7) and humans (8). The homology search in data bases of protein primary structure (8-10) indicated that the enzyme is a member ofthe lipocalin superfamily consisting of a variety of secretory proteins involved in the transport of small hydrophobic molecules (11). PGD synthase is the only lipocalin known to be associated with enzyme activity. The gene structure of rat brain PGD synthase (12) is also remarkably conserved among the members of this protein family inThe publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.terms of the numbers and sizes of exons and phases and sites of exon/intron splicing.Inorganic quadrivalent selenocompounds, such as SeCL4 and Na2SeO3, have recently been found to inhibit rat brain PGD synthase activity without affecting the activities ofother enzymes in the arachidonate cascade (13). Those selenocompounds were subsequently shown to inhibit sleep in unrestrained rats, promoting physiological wakefulness, in a timeand dose-dependent manner, when administered into the third ventricle via a microdialysis probe (14). These results further support our hypothesis that PGD2 is involved in the promotion of sleep under physiological conditions and imply that the PGD synthase may be a key enzyme in regulation of sleep-wake activities.We report here, by using in situ hybridization with antisense RNA for the enzyme, that mRNA for glutathioneindependent PGD synthase is dominantly expressed in the leptomeninges and choroid plexus, as well as in oligodendrocytes, of the adult rat brain. These tissues and cells were also found to be enriched in both the immunoreactivity and the enzyme activity of PGD synthase, indicating that the major site of synthesis of the enzyme, and also of PGD2, is predominantly, if not exclusively, located in the leptomen...

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Brain-type prostaglandin D synthetase occurs in the rat cochlea.

Abstract: Prostaglandin D synthetase [(5Z,13E

Cited by 30 publications

References 24 publications

Neuroendocrine Functions of Melanocytes: Beyond the Skin-Deep Melanin Maker

Neuroendocrine Functions of Melanocytes: Beyond the Skin-Deep Melanin Maker

Human brain prostaglandin D synthase has been evolutionarily differentiated from lipophilic-ligand carrier proteins.

Dominant expression of mRNA for prostaglandin D synthase in leptomeninges, choroid plexus, and oligodendrocytes of the adult rat brain.

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