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Journal articles on the topic 'GPR109a'

Author: Grafiati

Published: 4 June 2021

Last updated: 2 February 2022

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1

Docampo, Melissa D., Christoph K. Stein-Thoeringer, Amina Lazrak, Marina D. Burgos da Silva, Justin Cross, and Marcel R. M. van den Brink. "Expression of the Butyrate/Niacin Receptor, GPR109a on T Cells Plays an Important Role in a Mouse Model of Graft Versus Host Disease." Blood 132, Supplement 1 (2018): 61. http://dx.doi.org/10.1182/blood-2018-99-118783.

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Abstract INTRODUCTION: The intestinal microbiota is essential for the fermentation of fibers into the short-chain fatty acids (SCFA) butyrate, acetate and propionate. SCFA can bind to G-protein-coupled receptors GPR41, GPR43 and GPR109a to activate downstream anti-inflammatory signaling pathways. In colitis or graft versus host disease (GVHD), GPR43 signaling has been reported as an important regulator of intestinal homeostasis by increasing the pool of regulatory T cells. In contrast to GPR43, which binds preferentially propionate and acetate, GPR109a is the major receptor for butyrate. We an

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2

Geisler, Caroline E., Kendra E. Miller, Susma Ghimire, and Benjamin J. Renquist. "The Role of GPR109a Signaling in Niacin Induced Effects on Fed and Fasted Hepatic Metabolism." International Journal of Molecular Sciences 22, no. 8 (2021): 4001. http://dx.doi.org/10.3390/ijms22084001.

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Signaling through GPR109a, the putative receptor for the endogenous ligand β-OH butyrate, inhibits adipose tissue lipolysis. Niacin, an anti-atherosclerotic drug that can induce insulin resistance, activates GPR109a at nM concentrations. GPR109a is not essential for niacin to improve serum lipid profiles. To better understand the involvement of GPR109a signaling in regulating glucose and lipid metabolism, we treated GPR109a wild-type (+/+) and knockout (−/−) mice with repeated overnight injections of saline or niacin in physiological states characterized by low (ad libitum fed) or high (16 h f

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3

Zellner, Christian, Clive R. Pullinger, Bradley E. Aouizerat, et al. "Variations in human HM74 (GPR109B) and HM74A (GPR109A) niacin receptors." Human Mutation 25, no. 1 (2004): 18–21. http://dx.doi.org/10.1002/humu.20121.

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4

Snelson, Matthew, Sih Min Tan, Gavin C. Higgins, Runa S. J. Lindblom, and Melinda T. Coughlan. "Exploring the role of the metabolite-sensing receptor GPR109a in diabetic nephropathy." American Journal of Physiology-Renal Physiology 318, no. 3 (2020): F835—F842. http://dx.doi.org/10.1152/ajprenal.00505.2019.

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Alterations in gut homeostasis may contribute to the progression of diabetic nephropathy. There has been recent attention on the renoprotective effects of metabolite-sensing receptors in chronic renal injury, including the G protein-coupled receptor (GPR)109a, which ligates the short-chain fatty acid butyrate. However, the role of GPR109a in the development of diabetic nephropathy, a milieu of diminished microbiome-derived metabolites, has not yet been determined. The present study aimed to assess the effects of insufficient GPR109a signaling, via genetic deletion of GPR109a, on the developmen

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Ahmed, Kashan, Sorin Tunaru, and Stefan Offermanns. "GPR109A, GPR109B and GPR81, a family of hydroxy-carboxylic acid receptors." Trends in Pharmacological Sciences 30, no. 11 (2009): 557–62. http://dx.doi.org/10.1016/j.tips.2009.09.001.

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6

Plaisance, Eric P., Martina Lukasova, Stefan Offermanns, Youyan Zhang, Guoqing Cao, and Robert L. Judd. "Niacin stimulates adiponectin secretion through the GPR109A receptor." American Journal of Physiology-Endocrinology and Metabolism 296, no. 3 (2009): E549—E558. http://dx.doi.org/10.1152/ajpendo.91004.2008.

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Niacin (nicotinic acid) has recently been shown to increase serum adiponectin concentrations in men with the metabolic syndrome. However, little is known about the mechanism(s) by which niacin regulates the intracellular trafficking and secretion of adiponectin. Since niacin appears to exert its effects on lipolysis through receptor (GPR109A)-dependent and -independent pathways, the purpose of this investigation was to examine the role of the recently identified GPR109A receptor in adiponectin secretion. Initial in vivo studies in rats demonstrated that niacin (30 mg/kg po) acutely increases s

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7

Giri, Banabihari, Kasey Belanger, Marissa Seamon, et al. "Niacin Ameliorates Neuro-Inflammation in Parkinson’s Disease via GPR109A." International Journal of Molecular Sciences 20, no. 18 (2019): 4559. http://dx.doi.org/10.3390/ijms20184559.

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In this study, we used macrophage RAW264.7 cells to elucidate the molecular mechanism underlying the anti-inflammatory actions of niacin. Anti-inflammatory actions of niacin and a possible role of its receptor GPR109A have been studied previously. However, the precise molecular mechanism of niacin’s action in reducing inflammation through GPR109A is unknown. Here we observed that niacin reduced the translocation of phosphorylated nuclear kappa B (p-NF-κB) induced by lipopolysaccharide (LPS) in the nucleus of RAW264.7 cells. The reduction in the nuclear translocation in turn decreased the expre

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8

Horimatsu, Tetsuo, Andra L. Blomkalns, Mourad Ogbi, et al. "Niacin protects against abdominal aortic aneurysm formation via GPR109A independent mechanisms: role of NAD+/nicotinamide." Cardiovascular Research 116, no. 14 (2019): 2226–38. http://dx.doi.org/10.1093/cvr/cvz303.

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Abstract Aims Chronic adventitial and medial infiltration of immune cells play an important role in the pathogenesis of abdominal aortic aneurysms (AAAs). Nicotinic acid (niacin) was shown to inhibit atherosclerosis by activating the anti-inflammatory G protein-coupled receptor GPR109A [also known as hydroxycarboxylic acid receptor 2 (HCA2)] expressed on immune cells, blunting immune activation and adventitial inflammatory cell infiltration. Here, we investigated the role of niacin and GPR109A in regulating AAA formation. Methods and results Mice were supplemented with niacin or nicotinamide,

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9

Karunaratne, Tennekoon B., Chijioke Okereke, Marissa Seamon, Sharad Purohit, Chandramohan Wakade, and Amol Sharma. "Niacin and Butyrate: Nutraceuticals Targeting Dysbiosis and Intestinal Permeability in Parkinson’s Disease." Nutrients 13, no. 1 (2020): 28. http://dx.doi.org/10.3390/nu13010028.

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Dysbiosis is implicated by many studies in the pathogenesis of Parkinson’s disease (PD). Advances in sequencing technology and computing have resulted in confounding data regarding pathogenic bacterial profiles in conditions such as PD. Changes in the microbiome with reductions in short-chain fatty acid (SCFA)-producing bacteria and increases in endotoxin-producing bacteria likely contribute to the pathogenesis of PD. GPR109A, a G-protein coupled receptor found on the surface of the intestinal epithelium and immune cells, plays a key role in controlling intestinal permeability and the inflamma

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10

Ye, Lingyan, Zheng Cao, Xiangru Lai, Ying Shi, and Naiming Zhou. "Niacin Ameliorates Hepatic Steatosis by Inhibiting De Novo Lipogenesis Via a GPR109A-Mediated PKC–ERK1/2–AMPK Signaling Pathway in C57BL/6 Mice Fed a High-Fat Diet." Journal of Nutrition 150, no. 4 (2019): 672–84. http://dx.doi.org/10.1093/jn/nxz303.

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ABSTRACT Background Nonalcoholic fatty liver disease (NAFLD) is the most common liver disease in the world. Hepatic de novo lipogenesis (DNL) has been suggested to contribute to the pathogenesis of NAFLD. Recent studies have demonstrated that niacin (NA) modulates hepatic DNL through GPR109A. However, the underlying mechanism remains largely unknown. Objectives This study aims to elucidate the potential molecular mechanism by which GPR109A inhibits hepatic DNL. Methods C57BL/6 wild-type (WT) and Gpr109a knockout (KO) mice (male, 5 wk old) were fed a high-fat diet (60% energy from fat) firstly

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11

Feng, Wenqian, Yancheng Wu, Guangxin Chen, et al. "Sodium Butyrate Attenuates Diarrhea in Weaned Piglets and Promotes Tight Junction Protein Expression in Colon in a GPR109A-Dependent Manner." Cellular Physiology and Biochemistry 47, no. 4 (2018): 1617–29. http://dx.doi.org/10.1159/000490981.

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Background/Aims: Butyric acid plays an important role in maintaining intestinal health. Butyric acid has received special attention as a short-chain fatty acid, but its role in protecting the intestinal barrier is poorly characterized. Butyric acid not only provides energy for epithelial cells but also acts as a histone deacetylase inhibitor; it is also a natural ligand for G protein-coupled receptor 109A (GPR109A). A GPR109A analog was expressed in Sus scrofa and mediated the anti-inflammatory effects of beta-hydroxybutyric acid. This study investigated the effects of butyrate on growth perfo

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12

Jadeja, Ravirajsinh N., and Pamela M. Martin. "GPR109A activation and aging liver." Aging 11, no. 19 (2019): 8044–45. http://dx.doi.org/10.18632/aging.102343.

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13

Jung, Jae-Kyu, Benjamin R. Johnson, Tracy Duong, et al. "Analogues of Acifran: Agonists of the High and Low Affinity Niacin Receptors, GPR109a and GPR109b." Journal of Medicinal Chemistry 50, no. 7 (2007): 1445–48. http://dx.doi.org/10.1021/jm070022x.

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14

Wakade, Chandramohan, Raymond Chong, Eric Bradley, Bobby Thomas, and John Morgan. "Upregulation of GPR109A in Parkinson’s Disease." PLoS ONE 9, no. 10 (2014): e109818. http://dx.doi.org/10.1371/journal.pone.0109818.

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15

Guo, Wenjin, Juxiong Liu, Wen Li, et al. "Niacin Alleviates Dairy Cow Mastitis by Regulating the GPR109A/AMPK/NRF2 Signaling Pathway." International Journal of Molecular Sciences 21, no. 9 (2020): 3321. http://dx.doi.org/10.3390/ijms21093321.

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Mastitis is one of three bovine diseases recognized as a cause of substantial economic losses every year throughout the world. Niacin is an important feed additive that is used extensively for dairy cow nutrition. However, the mechanism by which niacin acts on mastitis is not clear. The aim of this study is to investigate the mechanism of niacin in alleviating the inflammatory response of mammary epithelial cells and in anti-mastitis. Mammary glands, milk, and blood samples were collected from mastitis cows not treated with niacin (n = 3) and treated with niacin (30 g/d, n = 3) and healthy cow

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16

Imbriglio, Jason E., Sookhee Chang, Rui Liang, et al. "GPR109a agonists. Part 2: Pyrazole-acids as agonists of the human orphan G-protein coupled receptor GPR109a." Bioorganic & Medicinal Chemistry Letters 20, no. 15 (2010): 4472–74. http://dx.doi.org/10.1016/j.bmcl.2010.06.041.

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17

Borthakur, Alip, Shubha Priyamvada, Anoop Kumar, et al. "A novel nutrient sensing mechanism underlies substrate-induced regulation of monocarboxylate transporter-1." American Journal of Physiology-Gastrointestinal and Liver Physiology 303, no. 10 (2012): G1126—G1133. http://dx.doi.org/10.1152/ajpgi.00308.2012.

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Monocarboxylate transporter isoform-1 (MCT1) plays an important role in the absorption of short-chain fatty acids (SCFAs) in the colon. Butyrate, a major SCFA, serves as the primary energy source for the colonic mucosa, maintains epithelial integrity, and ameliorates intestinal inflammation. Previous studies have shown substrate (butyrate)-induced upregulation of MCT1 expression and function via transcriptional mechanisms. The present studies provide evidence that short-term MCT1 regulation by substrates could be mediated via a novel nutrient sensing mechanism. Short-term regulation of MCT1 by

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18

Sun, Jingxuan, Boyu Yuan, Yancheng Wu та ін. "Sodium Butyrate Protects N2a Cells against Aβ Toxicity In Vitro". Mediators of Inflammation 2020 (15 квітня 2020): 1–9. http://dx.doi.org/10.1155/2020/7605160.

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Alzheimer’s disease (AD) is a common neurodegenerative disease. Aβ plays an important role in the pathogenesis of AD. Sodium butyrate (NaB) is a short-chain fatty acid salt that exerts neuroprotective effects such as anti-inflammatory, antioxidant, antiapoptotic, and cognitive improvement in central nervous system diseases. The aim of this study is to research the protective effects of NaB on neurons against Aβ toxicity and to uncover the underlying mechanisms. The results showed that 2 mM NaB had a significant improvement effect on Aβ-induced N2a cell injury, by increasing cell viability and

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19

Hepler, Chelsea, Caroline E. Foy, Mark R. Higgins та Benjamin J. Renquist. "The hypophagic response to heat stress is not mediated by GPR109A or peripheral β-OH butyrate". American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 310, № 10 (2016): R992—R998. http://dx.doi.org/10.1152/ajpregu.00513.2015.

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Rising temperatures resulting from climate change will increase the incidence of heat stress, negatively impacting the labor force and food animal production. Heat stress elevates circulating β-OH butyrate, which induces vasodilation through GPR109a. Interestingly, both heat stress and intraperitoneal β-OH butyrate administration induce hypophagia. Thus, we aimed to investigate the role of β-OH butyrate in heat stress hypophagia in mice. We found that niacin, a β-OH butyrate mimetic that cannot be oxidized to generate ATP, also reduces food intake. Interestingly, the depression in food intake

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20

Kostylina, G., D. Simon, M. F. Fey, S. Yousefi, and H. U. Simon. "Neutrophil apoptosis mediated by nicotinic acid receptors (GPR109A)." Cell Death & Differentiation 15, no. 1 (2007): 134–42. http://dx.doi.org/10.1038/sj.cdd.4402238.

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21

Kiepura, Anna, Kamila Stachyra, and Rafał Olszanecki. "Anti-Atherosclerotic Potential of Free Fatty Acid Receptor 4 (FFAR4)." Biomedicines 9, no. 5 (2021): 467. http://dx.doi.org/10.3390/biomedicines9050467.

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Fatty acids (FAs) are considered not only as a basic nutrient, but are also recognized as signaling molecules acting on various types of receptors. The receptors activated by FAs include the family of rhodopsin-like receptors: GPR40 (FFAR1), GPR41 (FFAR3), GPR43 (FFAR2), GPR120 (FFAR4), and several other, less characterized G-protein coupled receptors (GPR84, GPR109A, GPR170, GPR31, GPR132, GPR119, and Olfr78). The ubiquitously distributed FFAR4 can be activated by saturated and unsaturated medium- and long-chain fatty acids (MCFAs and LCFAs), as well as by several synthetic agonists (e.g., TU

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22

Li, Yan Jun, Xiaochen Chen, Tony K. Kwan, et al. "Dietary Fiber Protects against Diabetic Nephropathy through Short-Chain Fatty Acid–Mediated Activation of G Protein–Coupled Receptors GPR43 and GPR109A." Journal of the American Society of Nephrology 31, no. 6 (2020): 1267–81. http://dx.doi.org/10.1681/asn.2019101029.

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BackgroundStudies have reported “dysbiotic” changes to gut microbiota, such as depletion of gut bacteria that produce short-chain fatty acids (SCFAs) through gut fermentation of fiber, in CKD and diabetes. Dietary fiber is associated with decreased inflammation and mortality in CKD, and SCFAs have been proposed to mediate this effect.MethodsTo explore dietary fiber’s effect on development of experimental diabetic nephropathy, we used streptozotocin to induce diabetes in wild-type C57BL/6 and knockout mice lacking the genes encoding G protein–coupled receptors GPR43 or GPR109A. Diabetic mice we

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23

Fu, Shou-Peng, Su-Nan Li, Jian-Fa Wang та ін. "BHBA Suppresses LPS-Induced Inflammation in BV-2 Cells by Inhibiting NF-κB Activation". Mediators of Inflammation 2014 (2014): 1–12. http://dx.doi.org/10.1155/2014/983401.

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β-Hydroxybutyric acid (BHBA) has neuroprotective effects, but the underlying molecular mechanisms are unclear. Microglial activation plays an important role in neurodegenerative diseases by producing several proinflammatory enzymes and proinflammatory cytokines. The current study investigates the potential mechanisms whereby BHBA affects the expression of potentially proinflammatory proteins by cultured murine microglial BV-2 cells stimulated with lipopolysaccharide (LPS). The results showed that BHBA significantly reduced LPS-induced protein and mRNA expression levels of iNOS, COX-2, TNF-α, I

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Zandi‐Nejad, Kambiz, Ayumi Takakura, Mollie Jurewicz, et al. "The role of HCA2 (GPR109A) in regulating macrophage function." FASEB Journal 27, no. 11 (2013): 4366–74. http://dx.doi.org/10.1096/fj.12-223933.

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Benyó, Zoltán, Andreas Gille, Jukka Kero, et al. "GPR109A (PUMA-G/HM74A) mediates nicotinic acid–induced flushing." Journal of Clinical Investigation 115, no. 12 (2005): 3634–40. http://dx.doi.org/10.1172/jci23626.

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Wanders, D., and R. L. Judd. "Future of GPR109A agonists in the treatment of dyslipidaemia." Diabetes, Obesity and Metabolism 13, no. 8 (2011): 685–91. http://dx.doi.org/10.1111/j.1463-1326.2011.01400.x.

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Jadeja, Ravirajsinh N., Malita A. Jones, Ollya Fromal, et al. "Loss of GPR109A/HCAR2 induces aging-associated hepatic steatosis." Aging 11, no. 2 (2019): 386–400. http://dx.doi.org/10.18632/aging.101743.

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Ye, Lingyan, Zheng Cao, Xiangru Lai, et al. "Niacin fine‐tunes energy homeostasis through canonical GPR109A signaling." FASEB Journal 33, no. 4 (2018): 4765–79. http://dx.doi.org/10.1096/fj.201801951r.

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Jobin, Christian. "GPR109a: The Missing Link between Microbiome and Good Health?" Immunity 40, no. 1 (2014): 8–10. http://dx.doi.org/10.1016/j.immuni.2013.12.009.

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Imbriglio, Jason E., Sookhee Chang, Rui Liang, et al. "GPR109a agonists. Part 1: 5-Alkyl and 5-aryl-pyrazole–tetrazoles as agonists of the human orphan G-protein coupled receptor GPR109a." Bioorganic & Medicinal Chemistry Letters 19, no. 8 (2009): 2121–24. http://dx.doi.org/10.1016/j.bmcl.2009.03.014.

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31

Offermanns, Stefan, Steven L. Colletti, Timothy W. Lovenberg, Graeme Semple, Alan Wise, and Adriaan P. IJzerman. "International Union of Basic and Clinical Pharmacology. LXXXII: Nomenclature and Classification of Hydroxy-carboxylic Acid Receptors (GPR81, GPR109A, and GPR109B)." Pharmacological Reviews 63, no. 2 (2011): 269–90. http://dx.doi.org/10.1124/pr.110.003301.

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32

Deng, Qiaolin, Jessica L. Frie, Daria M. Marley, et al. "Molecular modeling aided design of nicotinic acid receptor GPR109A agonists." Bioorganic & Medicinal Chemistry Letters 18, no. 18 (2008): 4963–67. http://dx.doi.org/10.1016/j.bmcl.2008.08.030.

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33

Gharbaoui, Tawfik, Philip J. Skinner, Young-Jun Shin, et al. "Agonist lead identification for the high affinity niacin receptor GPR109a." Bioorganic & Medicinal Chemistry Letters 17, no. 17 (2007): 4914–19. http://dx.doi.org/10.1016/j.bmcl.2007.06.028.

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34

Zou, Huawei, Rui Hu, Xianwen Dong та ін. "Lipid Catabolism in Starved Yak Is Inhibited by Intravenous Infusion of β-Hydroxybutyrate". Animals 10, № 1 (2020): 136. http://dx.doi.org/10.3390/ani10010136.

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Lipid is the chief energy source for starved animals. β-hydroxybutyrate (BHBA) is the main ketone body produced by lipid decomposition. In Chinese hamster ovary (CHO) cell experiment, it was found that BHBA could be used not only as an energy substance, but also as a ligand of GPR109A for regulating lipid metabolism. However, whether BHBA can regulate lipid metabolism of yaks, and its effective concentration and signal pathway are not clear. This study investigated the effects and mechanism of starvation and BHBA on the lipid metabolism of yak. Eighteen male Jiulong yaks were selected and then

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35

Rezq, S., and A. A. Abdel-Rahman. "Central GPR109A Activation Mediates Glutamate-Dependent Pressor Response in Conscious Rats." Journal of Pharmacology and Experimental Therapeutics 356, no. 2 (2015): 457–66. http://dx.doi.org/10.1124/jpet.115.229146.

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36

Boatman, P. Douglas, Thomas O. Schrader, Michelle Kasem, et al. "Potent tricyclic pyrazole tetrazole agonists of the nicotinic acid receptor (GPR109a)." Bioorganic & Medicinal Chemistry Letters 20, no. 9 (2010): 2797–800. http://dx.doi.org/10.1016/j.bmcl.2010.03.062.

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37

Wanders, Desiree, Emily C. Graff, and Robert L. Judd. "Effects of high fat diet on GPR109A and GPR81 gene expression." Biochemical and Biophysical Research Communications 425, no. 2 (2012): 278–83. http://dx.doi.org/10.1016/j.bbrc.2012.07.082.

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38

Geyer, Marcel, Johannes A. Baus, Ola Fjellström, Eric Wellner, Linda Gustafsson, and Reinhold Tacke. "Synthesis and Pharmacological Properties of Silicon-Containing GPR81 and GPR109A Agonists." ChemMedChem 10, no. 12 (2015): 2063–70. http://dx.doi.org/10.1002/cmdc.201500343.

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Li, Xiaoyu, John S. Millar, Nicholas Brownell, François Briand, and Daniel J. Rader. "Modulation of HDL metabolism by the niacin receptor GPR109A in mouse hepatocytes." Biochemical Pharmacology 80, no. 9 (2010): 1450–57. http://dx.doi.org/10.1016/j.bcp.2010.07.023.

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Elangovan, Selvakumar, Rajneesh Pathania, Sabarish Ramachandran, et al. "The Niacin/Butyrate Receptor GPR109A Suppresses Mammary Tumorigenesis by Inhibiting Cell Survival." Cancer Research 74, no. 4 (2013): 1166–78. http://dx.doi.org/10.1158/0008-5472.can-13-1451.

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41

Feingold, Kenneth R., Arthur Moser, Judy K. Shigenaga, and Carl Grunfeld. "Inflammation stimulates niacin receptor (GPR109A/HCA2) expression in adipose tissue and macrophages." Journal of Lipid Research 55, no. 12 (2014): 2501–8. http://dx.doi.org/10.1194/jlr.m050955.

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Lee, A. Kyoung, Dae Hyun Kim, EunJin Bang, Yeon Ja Choi та Hae Young Chung. "β-Hydroxybutyrate Suppresses Lipid Accumulation in Aged Liver through GPR109A-mediated Signaling". Aging and disease 11, № 4 (2020): 777. http://dx.doi.org/10.14336/ad.2019.0926.

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Skinner, Philip J., Martin C. Cherrier, Peter J. Webb, et al. "Fluorinated pyrazole acids are agonists of the high affinity niacin receptor GPR109a." Bioorganic & Medicinal Chemistry Letters 17, no. 20 (2007): 5620–23. http://dx.doi.org/10.1016/j.bmcl.2007.07.101.

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44

Zhang, Shu‐jie, Zi‐hua Li, Yu‐dian Zhang, et al. "Ketone Body 3‐Hydroxybutyrate Ameliorates Atherosclerosis via Receptor Gpr109a‐Mediated Calcium Influx." Advanced Science 8, no. 9 (2021): 2003410. http://dx.doi.org/10.1002/advs.202003410.

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45

Chen, Guangxin, Shoupeng Fu, Wenqian Feng, et al. "AMP010014A09 in Sus Scrofa Encodes an Analog of G Protein-Coupled Receptor 109A, Which Mediates the Anti-Inflammatory Effects of Beta-Hydroxybutyric Acid." Cellular Physiology and Biochemistry 42, no. 4 (2017): 1420–30. http://dx.doi.org/10.1159/000479206.

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Background: Hydroxy-carboxylic acid receptor 2 (HCA2, also called GPR109A) belongs to the G protein-coupled receptor (GPCR) family and is found in humans, rats, mice, hamsters and guinea pigs, but there are almost no reports of this protein in other species. In this investigation, we speculated that AMP010014A09 (AMP+) is a homologue of GPR109A in swine. Methods: To test this hypothesis, the following experiments were designed: monocytes isolated from the peripheral blood of swine were treated with LPS after pretreating with or without β-hydroxybutyric acid (BHBA), and the levels of pro-inflam

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46

Bhatt, Brinda, Peng Zeng, Huabin Zhu, et al. "Gpr109a Limits Microbiota-Induced IL-23 Production To Constrain ILC3-Mediated Colonic Inflammation." Journal of Immunology 200, no. 8 (2018): 2905–14. http://dx.doi.org/10.4049/jimmunol.1701625.

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47

Kashiwagi, Saori, Kazuhiko Uchiyama, Kazuyuki Ogita, et al. "Tu1280 - GPR109A is Involved in Butyrate-Induced Hsp25 Expression in Colonic Epithelial Cells." Gastroenterology 154, no. 6 (2018): S—923. http://dx.doi.org/10.1016/s0016-5085(18)33106-8.

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Chen, Lihua, Wing Yan So, Stephen Y. T. Li, Qianni Cheng, Barbara J. Boucher, and Po Sing Leung. "Niacin-induced hyperglycemia is partially mediated via niacin receptor GPR109a in pancreatic islets." Molecular and Cellular Endocrinology 404 (March 2015): 56–66. http://dx.doi.org/10.1016/j.mce.2015.01.029.

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49

Chai, Joshua T., Janet E. Digby, Neil Ruparelia, Andrew Jefferson, Ashok Handa, and Robin P. Choudhury. "Nicotinic Acid Receptor GPR109A Is Down-Regulated in Human Macrophage-Derived Foam Cells." PLoS ONE 8, no. 5 (2013): e62934. http://dx.doi.org/10.1371/journal.pone.0062934.

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Shen, Hong C. "Acyl hydroxypyrazoles as novel agonists for high-affinity nicotinic acid receptor GPR109A: WO2008051403." Expert Opinion on Therapeutic Patents 19, no. 8 (2009): 1149–55. http://dx.doi.org/10.1517/13543770902798061.

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