GPR172B antibody
- Known as:
- GPR172B (anti-)
- Catalog number:
- orb100328
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Biorbyt biorb
- Gene target:
- GPR172B antibody
Related genes to: GPR172B antibody
- Gene:
- SLC52A1 NIH gene
- Name:
- solute carrier family 52 member 1
- Previous symbol:
- GPR172B
- Synonyms:
- FLJ10060, GPCR42, PAR2, hRFT1, RFVT1
- Chromosome:
- 17p13.2
- Locus Type:
- gene with protein product
- Date approved:
- 2004-07-19
- Date modifiied:
- 2016-10-05
Related products to: GPR172B antibody
Related articles to: GPR172B antibody
- Serum urate levels are high in hominoids because of the evolutionary loss of uricase, an enzyme involved in purine metabolism during evolution. However, the mechanism underlying uricase loss remains unclear. We report the involvement of the neofunctionalized solute carrier family 52 member A1 (SLC52A1) in the evolutionary loss of uricase. Synteny analysis revealed that SLC52A1 was duplicated from SLC52A2, which encodes a riboflavin transporter and is conserved among primates. Functional studies demonstrated the ability of primate SLC52A1 to transport urate as well as riboflavin and the mediation of cellular uptake and efflux of urate by human SLC52A1 through facilitated diffusion. Transcellular transport studies demonstrated that SLC52A1, which is basolaterally localized in enterocytes, works synergistically with ABC subfamily G member 2, a luminally localized urate efflux transporter, to remove urate from the basolateral side. Before uricase loss, acquiring SLC52A1 may have provided primates with a novel intestinal urate transport system and allowed for evolutionary uricase loss in hominoids. - Source: PubMed
Publication date: 2026/02/26
Yamamoto SyunsukeInoue KatsuhisaYasujima TomoyaTakei HidekiYamashiro TakahiroAsai KeikoMatake IsamuUchiyama SoraOhta KinyaKishimoto HisanaoHiguchi KeiAnayama HisashiAsao YuukoHirabayashi HidekiAmano NobuyukiShimizu ToruTakada TappeiTamura TakashiWakai KenjiKawamura YusukeNakayama AkiyoshiToyoda YuMatsuo HirotakaYuasa Hiroaki - Riboflavin (vitamin B2) is an essential water-soluble vitamin that serves as a precursor for flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN), key cofactors in biological redox reactions. These reactions are crucial for energy metabolism and cellular homeostasis. Mammals cannot synthesize riboflavin and rely on specialized transport systems for its absorption and distribution. The discovery of the riboflavin transporter (RFVT) family, comprising RFVT1 (SLC52A1), RFVT2 (SLC52A2), and RFVT3 (SLC52A3) has provided critical insights into riboflavin homeostasis. These transporters show tissue-specific expression and play essential roles in riboflavin uptake. Mutations in SLC52A2 and SLC52A3 have been linked to Brown-Vialetto-Van Laere syndrome (BVVLS), a rare neurodegenerative disorder characterized by progressive sensorineural hearing loss and cranial nerve dysfunction. Functional studies using knockout mouse models have demonstrated that Rfvt deficiency results in embryonic lethality or severe neurological impairment due to impaired riboflavin transport. Patients with BVVLS and RFVT mutations showed symptomatic improvement with high-dose riboflavin supplementation. This review summarizes the molecular characteristics, physiological functions, and pathological implications of RFVTs and emphasizes their role in disease mechanisms and potential therapeutic strategies. Understanding the riboflavin transport mechanisms provides a foundation for developing targeted treatments for riboflavin-related disorders. - Source: PubMed
Yonezawa Atsushi - Endogenous retroviruses (ERVs) are remnants of ancestral viral infections in germ cells that constitute a substantial proportion of the mammalian genome and are assumed to provide molecular fossil records of ancient infections. Analysis of these sequences may reveal the mechanisms of virus-host co-evolution, viral endogenization, and extinction. Chimpanzee endogenous retrovirus 1 (CERV1), a gamma retrovirus, is estimated to have circulated within primates for ~10 million years, although it is now apparently extinct. In this study, we aimed to gain an understanding of how the extinct CERV1 was transmitted and endogenized. On the basis of the identification of CERV1 fossils in the primate genome and using the expression-cloning method with the human cDNA library, we found that riboflavin transporter human SLC52A2 served as a receptor for CERV1 entry. The ectopic expression of human and chimpanzee SLC52A2 and its related SLC52A1 in heterogenic cells confers susceptibility to infection by CERV1 and porcine endogenous retrovirus (PERV). Virus interference experiments have shown that CERV1 inhibits infection by PERV and . This finding indicates that CERV1 and PERV belong to the same virus interference group. CERV1 shows infection in a wide range of human and primate cells. Notably, CERV1 infection is observed in human cell lines that express human SLC52A2 abundantly but hardly express human SLC52A1. Although CERV1 has been established to be present at high copy numbers in the great apes (, , and ) and 15 Old World monkey species of the Cercopithecinae and Colobinae subfamilies, it is absent in humans and orangutans. CERV1 gene expression is observed in primates, including chimpanzees, suggesting that CERV1 has co-evolved with its hosts. Our results suggest that ERVs may have conferred resistance to viral infections in a convergent evolutionary manner. These findings are significant not only for advancing the field of paleovirology but also in terms of gaining an understanding of the potential risks of viral infection with respect to xenotransplantation, such as that from pigs to humans. - Source: PubMed
Publication date: 2025/05/07
AbuEed LoaiMiyake ArikoWanjala NashonPramono DidikAbdillah DimasImamura MasanoriShimojima MasayukiDenner JoachimKawasaki JunnaNishigaki Kazuo - Cellular senescence is defined as a permanent proliferation arrest caused by various stresses, including DNA damage. We have recently identified the riboflavin transporter SLC52A1, whose expression is increased in response to senescence-inducing stimuli. Interestingly, increased expression of SLC52A1 suppresses cellular senescence through the uptake of riboflavin and an increase in intracellular flavin adenine dinucleotide (FAD), an enzyme cofactor synthesized from riboflavin. However, how FAD suppresses cellular senescence has not been fully elucidated. Therefore, in this study, we focused on lysine-specific demethylase 1 (LSD1), which uses FAD as a cofactor. First, we found that LSD1 inhibition promoted DNA damage-induced cellular senescence, whereas ectopic expression of LSD1 suppressed cellular senescence, suggesting that LSD1 suppresses senescence. In addition, the demethylation activity of LSD1 against histone H3 and p53 was increased by senescence-inducing stress in a riboflavin uptake-dependent manner. Furthermore, it was revealed that the LSD1 demethylation activity was required for suppression of pro-senescence genes Sirtuin-4 and p21 whose expression is modified by methylation status of histone H3 and possibly p53, respectively. Collectively, these results suggest that the FAD increase by senescence-inducing stress leads to LSD1-mediated demethylation of histone H3 and p53, which results in the suppression of pro-senescence genes to inhibit senescence induction. - Source: PubMed
Publication date: 2025/02/23
Osumi TaiichiNagano TaikiIwasaki TetsushiNakanishi JotaroMiyazawa KazuyukiKamada Shinji - Riboflavin, the FMN and FAD precursor, is a crucial vitamin in cell metabolism. Its adsorption and tissue distribution are mediated by tree membrane transporters namely RFVT1-3. Mutations of their genes are associated with Riboflavin Transporter Deficiency. Moreover, derangements of the level of these transporters have been found in several human cancers. To obtain a suitable experimental tool for studying the function of the single proteins, for testing the effect of pathological mutations and for validating predicted ligands as candidate drugs, we have set up a proteoliposome system harbouring the functional RFVT1 or RFVT3. RFVT proteins have been produced in E. coli and purified to the homogeneity by affinity chromatography. The purified proteins show an apparent molecular mass of 45.6 or 48.4 kDa, which are very close to the theoretical mass of RFVT1 or RFVT3, respectively. The purified transporters have been reconstituted into proteoliposomes using a methodology previously pointed out for RFVT2. The transport of riboflavin shows cooperative kinetics with K values of 0.86 or 1.13 μM and Hill coefficients of 1.19 or 1.3 for RFVT1 or RFVT3, respectively. The K data of both the transporters are similar the Km reported in intact cell studies. The transporters are inhibited by the riboflavin analogues FMN and lumiflavin in agreement with the molecular docking simulations. - Source: PubMed
Publication date: 2025/02/05
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