Expression and regulation of a vesicular monoamine transporter in rat stomach: a putative histamine transporter.

Dimaline, R.; Struthers, John E.

doi:10.1113/jphysiol.1996.sp021140

Cited by 73 publications

(55 citation statements)

References 28 publications

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“…In the fasting rat, ECL cells showed a decrease in both their L-histidine substrate uptake transporter SN2 and their VMAT-2 responsible for histamine uptake into the secretory vesicles (Dimaline et al 1993b, Dimaline & Struthers 1996, Lambrecht et al 2007. The reduction in histamine biosynthesis required under fasting conditions would thus be achieved by reducing substrate availability, as well as the histamine secretory pool, rather than inhibiting the biosynthetic enzyme histidine decarboxylase (Lambrecht et al 2007).…”

Section: Discussionmentioning

confidence: 99%

Selective expression of TLQP-21 and other VGF peptides in gastric neuroendocrine cells and modulation by feeding

Brancia¹,

Cocco²,

D'Amato³

et al. 2010

Journal of Endocrinology

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Although vgf gene knockout mice are hypermetabolic, administration of the VGF peptide TLQP-21 itself increased energy consumption. Agonist-antagonist roles are thus suggested for different VGF peptides, and the definition of their tissue heterogeneity is mandatory. We studied the rat stomach using antisera to C-or N-terminal sequences of known or predicted VGF peptides in immunohistochemistry and ELISA. TLQP (rat VGF 556-565 ) peptide/s were most abundant (162G11 pmol/g, meanGS.E.M.) and were brightly immunostained in enterochromaffin-like (ECL) cells and somatostatin cells. A peptide co-eluting with TLQP-21 was revealed in HPLC of gastric and hypothalamic extracts, while the extended TLQP-62 form was restricted to the hypothalamus. Novel PGH (rat VGF 422-430 ) peptide/s were revealed in ghrelin cells, mostly corresponding to low MW forms (0 . 8-1 . 5 kDa), while VGF C-terminus peptides were confined to neurons. VGF mRNA was present in the above gastric endocrine cell types, and was prominent in chief cells, in parallel with low-intensity staining for further cleaved products from the C-terminal region of VGF (HVLL peptides: VGF 605-614 ). In swine stomach, a comparable profile of VGF peptides was revealed by immunohistochemistry. When fed and fasted rats were studied, a clear-cut, selective decrease on fasting was observed for TLQP peptides only (162G11 vs 74G5 . 3 pmol/g, fed versus fasted rats, meanGS.E.M., P!0 . 00001). In conclusion, specific VGF peptides appear to be widely represented in different gastric endocrine and other mucosal cell populations. The selective modulation of TLQP peptides suggests their involvement in peripheral neuro-endocrine mechanisms related to feeding responses and/or ECL cell regulation.

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Section: Discussionmentioning

confidence: 99%

Selective expression of TLQP-21 and other VGF peptides in gastric neuroendocrine cells and modulation by feeding

Brancia¹,

Cocco²,

D'Amato³

et al. 2010

Journal of Endocrinology

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“…Physiological regulation of gastric acid secretion by the hormone gastrin is critically dependent upon the synthesis, storage, and release of histamine from the ECL cell (9,10,13,24). Expression of genes involved in these aspects of ECL cell function are tightly regulated by gastrin, including the gene encoding VMAT2, which is required for the sequestration of histamine into the secretory vesicles (4,13,25).…”

Section: Discussionmentioning

confidence: 99%

“…Histamine secreted by the ECL cell is the major stimulant of acid secretion from gastric parietal cells (9,10), and ECL cell function is tightly regulated by the hormone gastrin acting through the CCK 2 receptor (CCK 2 R) (9,11,12). Raised plasma gastrin concentrations increase expression of ECL cell genes that are key to histamine synthesis and secretion, including VMAT2 (13). Gastrin stimulates transcription of VMAT2 in gastric epithelial cells through protein kinase C and mitogen-activated protein kinase/extracellular signal-regulated kinase kinase signaling pathways via phosphorylation of CREB (14,15) and binding of uncharacterised nuclear factors to a GC-rich region of the promoter (15).…”

mentioning

confidence: 99%

Identification of a Gastrin Response Element in the Vesicular Monoamine Transporter Type 2 Promoter and Requirement of 20 S Proteasome Subunits for Transcriptional Activity

Catlow

Ashurst

Varró

et al. 2007

Journal of Biological Chemistry

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Vesicular monoamine transporter type 2 (VMAT2) is crucial for accumulation of monoamine neurotranmitters into neuronal secretory vesicles and histamine into secretory granules of the enterochromaffin-like cell in the acid-secreting gastric mucosa. Gastric VMAT2 expression is regulated by the antral hormone gastrin acting at the CCK 2 receptor. We demonstrate a gastrin response element ؊56 ccgccccctc ؊47 in the proximal VMAT2 promoter that binds in a gastrin-sensitive manner to nuclear proteins from gastric epithelial cell lines. Mutations within this sequence prevented nuclear protein binding and significantly reduced gastrin-stimulated expression of VMAT2 promoter-reporter constructs in gastric epithelial cells. In a yeast one-hybrid screen of an AR42J cell cDNA library, using the gastrin response element as bait, we identified a beta subunit of the 20 S proteasome, PSMB1, as a potential binding partner. In supershift assays, antibodies to PSMB1 and other proteasome beta subunits disrupted gastrin sensitive nuclear protein binding to the VMAT2 promoter. Moreover, RNA interference of PSMB1 significantly inhibited gastrin-mediated VMAT2 transcription. These data suggest that elements of the 20 S proteasome interact with the VMAT2 promoter to enhance G-proteincoupled receptor-mediated transcription.The vesicular monoamine transporters (VMATs) 2 are responsible for the energy-dependent accumulation of biogenic amines into secretory vesicles of amine producing cells and thus play central roles in cellular physiology. The two members of this family, VMATs 1 and 2, have similar structures and mechanisms of action, but differ in their cellular localization and substrate specificity (1-4). VMAT2 (SLC18A2) is expressed in all monoaminergic neurones of the central nervous system, notably e.g. in dopaminergic neurones of the substantia nigra and histaminergic posterior hypothalamic neurones. Support for the idea that VMAT2 is important for neuronal function comes from studies in VMAT2 knock-out mice. Homozygotes have seriously disrupted patterns of feeding and locomotion and are poorly viable. Heterozygotes are grossly normal but have reduced central monoamine levels and are hypersensitive to the locomotor effects of cocaine and amphetamine and are more sensitive to the neurotoxin 1-methyl-(4-phenyl-1,2,3,6-tetrahydropyridine) (MPTP) and to 3,4-dihydroxyphenylalanine (L-DOPA) (5-7). VMAT2 is able to sequester from cytoplasm, toxins, and transmitters that cause Parkinson-like syndromes, and gain of function haplotypes have been reported to confer protection against Parkinson's disease (8). Transporter affinities for serotonin and the catecholamines are in the low micromolar range and are broadly similar for both VMATs. However, only VMAT2 has micromolar affinity for histamine (3). The ability of VMAT2 to accumulate histamine in secretory vesicles is consistent with its localization in central histaminergic neurones and in enterochromaffin-like (ECL) cells of the gastric epithelium, its only non-neuronal location (4). Hist...

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“…For this reason, we used two additional measures to more specifically characterize OCT-mediated transport in acutely dissected brain tissues. First, uptake of [ 3 H]-histamine by 3V-MH minces: of the above-mentioned transporters, only OCT2, OCT3, and VMAT2 are known to transport histamine (Merickel and Edwards, 1995;Dimaline and Struthers, 1996;Grundemann et al, 1999). Second, efflux of [ 3 H]-MPP ϩ from preloaded hypothalamic minces: although SERT, DAT, and NET are capable of transporting MPP ϩ , they are all predominantly unidirectional uptake transporters under physiological conditions (Levi and Raiteri, 1993;Scholze et al, 2002;Reed et al, 2003), whereas the OCTs are truly bidirectional transporters (Jonker and Schinkel, 2004).…”

Section: And [ 3 H]-histamine and Efflux Of [ 3 H]-mppmentioning

confidence: 99%

Corticosterone-Sensitive Monoamine Transport in the Rat Dorsomedial Hypothalamus: Potential Role for Organic Cation Transporter 3 in Stress-Induced Modulation of Monoaminergic Neurotransmission

Gasser¹,

Lowry²,

Orchinik³

2006

J. Neurosci.

127

104

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Expression and regulation of a vesicular monoamine transporter in rat stomach: a putative histamine transporter.

Cited by 73 publications

References 28 publications

Selective expression of TLQP-21 and other VGF peptides in gastric neuroendocrine cells and modulation by feeding

Selective expression of TLQP-21 and other VGF peptides in gastric neuroendocrine cells and modulation by feeding

Identification of a Gastrin Response Element in the Vesicular Monoamine Transporter Type 2 Promoter and Requirement of 20 S Proteasome Subunits for Transcriptional Activity

Corticosterone-Sensitive Monoamine Transport in the Rat Dorsomedial Hypothalamus: Potential Role for Organic Cation Transporter 3 in Stress-Induced Modulation of Monoaminergic Neurotransmission

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