For Publishers
DiscoveryMetadataPeer reviewHostingPublishing
For Researchers
JoinPublishReviewCollect
Register
Blog
About
Search
Advanced search
My ScienceOpen
Search
For Publishers
For Researchers
Blog
About
11
views
97
references
 Top references
cited by
5
    
0 reviews
 Review
0
comments
 Comment
0
recommends
+1 Recommend
0 collections
    0
    shares
      368
      similar
       All similar
      • Record: found
      • Abstract: found
      • Article: not found

      Brilliant Blue Dyes in Daily Food: How Could Purinergic System Be Affected?

      review-article

      Read this article at

      ScienceOpenPublisherPMC
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Dyes were first obtained from the extraction of plant sources in the Neolithic period to produce dyed clothes. At the beginning of the 19th century, synthetic dyes were produced to color clothes on a large scale. Other applications for synthetic dyes include the pharmaceutical and food industries, which are important interference factors in our lives and health. Herein, we analyzed the possible implications of some dyes that are already described as antagonists of purinergic receptors, including special Brilliant Blue G and its derivative FD&C Blue No. 1. Purinergic receptor family is widely expressed in the body and is critical to relate to much cellular homeostasis maintenance as well as inflammation and cell death. In this review, we discuss previous studies and show purinergic signaling as an important issue to be aware of in food additives development and their correlations with the physiological functions.

          Related collections

          Most cited references97

          • Record: found
          • Abstract: found
          • Article: not found

          Pannexins, a family of gap junction proteins expressed in brain.

          R Bruzzone, S Hormuzdi, M. T. Barbe … (2011)
          Database search has led to the identification of a family of proteins, the pannexins, which share some structural features with the gap junction forming proteins of invertebrates and vertebrates. The function of these proteins has remained unclear so far. To test the possibility that pannexins underlie electrical communication in the brain, we have investigated their tissue distribution and functional properties. Here, we show that two of these genes, pannexin 1 (Px1) and Px2, are abundantly expressed in the CNS. In many neuronal cell populations, including hippocampus, olfactory bulb, cortex and cerebellum, there is coexpression of both pannexins, whereas in other brain regions, e.g., white matter, only Px1-positive cells were found. On expression in Xenopus oocytes, Px1, but not Px2 forms functional hemichannels. Coinjection of both pannexin RNAs results in hemichannels with functional properties that are different from those formed by Px1 only. In paired oocytes, Px1, alone and in combination with Px2, induces the formation of intercellular channels. The functional characteristics of homomeric Px1 versus heteromeric Px1/Px2 channels and the different expression patterns of Px1 and Px2 in the brain indicate that pannexins form cell type-specific gap junctions with distinct properties that may subserve different functions.
          Article 0 comments Cited 207 times – based on 0 reviews     Review now
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Purine and pyrimidine receptors.

            G Burnstock (2007)
            Adenosine 5'-triphosphate (ATP), in addition to its intracellular roles, acts as an extracellular signalling molecule via a rich array of receptors, which have been cloned and characterised. P1 receptors are selective for adenosine, a breakdown product of ATP, produced after degradation by ectonucleotidases. Four subtypes have been identified, A(1), A(2A), A(2B) and A(3) receptors. P2 receptors are activated by purines and some subtypes also by pyrimidines. P2X receptors are ligand-gated ion channel receptors and seven subunits have been identified, which form both homomultimers and heteromultimers. P2Y receptors are G protein-coupled receptors, and eight subtypes have been cloned and characterised to date.
            Article 0 comments Cited 187 times – based on 0 reviews     Review now
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              Activation and regulation of purinergic P2X receptor channels.

              Claudio Coddou, Zonghe Yan, Tomas Obsil … (2011)
              Mammalian ATP-gated nonselective cation channels (P2XRs) can be composed of seven possible subunits, denoted P2X1 to P2X7. Each subunit contains a large ectodomain, two transmembrane domains, and intracellular N and C termini. Functional P2XRs are organized as homomeric and heteromeric trimers. This review focuses on the binding sites involved in the activation (orthosteric) and regulation (allosteric) of P2XRs. The ectodomains contain three ATP binding sites, presumably located between neighboring subunits and formed by highly conserved residues. The detection and coordination of three ATP phosphate residues by positively charged amino acids are likely to play a dominant role in determining agonist potency, whereas an AsnPheArg motif may contribute to binding by coordinating the adenine ring. Nonconserved ectodomain histidines provide the binding sites for trace metals, divalent cations, and protons. The transmembrane domains account not only for the formation of the channel pore but also for the binding of ivermectin (a specific P2X4R allosteric regulator) and alcohols. The N- and C- domains provide the structures that determine the kinetics of receptor desensitization and/or pore dilation and are critical for the regulation of receptor functions by intracellular messengers, kinases, reactive oxygen species and mercury. The recent publication of the crystal structure of the zebrafish P2X4.1R in a closed state provides a major advance in the understanding of this family of receptor channels. We will discuss data obtained from numerous site-directed mutagenesis experiments accumulated during the last 15 years with reference to the crystal structure, allowing a structural interpretation of the molecular basis of orthosteric and allosteric ligand actions.
              Article 0 comments Cited 166 times – based on 0 reviews     Review now
                Bookmark
                All references

                Author and article information

                Journal
                Journal ID (nlm-ta): Int J Food Sci
                Journal ID (iso-abbrev): Int J Food Sci
                Journal ID (publisher-id): IJFS
                Title: International Journal of Food Science
                Publisher: Hindawi Publishing Corporation
                ISSN (Electronic): 2314-5765
                Publication date (Print): 2016
                Publication date (Electronic): 19 October 2016
                Volume: 2016
                Electronic Location Identifier: 7548498
                Affiliations
                1Laboratory of Inflammation, Oswaldo Cruz Foundation, Av. Brazil, 4365 Rio de Janeiro, RJ, Brazil
                2Laboratory of Toxoplasmosis, Oswaldo Cruz Foundation, Av. Brazil, 4365 Rio de Janeiro, RJ, Brazil
                3Laboratory of Cellular Communication, Oswaldo Cruz Foundation, Av. Brazil, 4365 Rio de Janeiro, RJ, Brazil
                Author notes
                *Robson Xavier Faria: robson.xavier@ 123456gmail.com

                Academic Editor: Rosana G. Moreira

                Author information
                http://orcid.org/0000-0001-8218-834X
                Article
                DOI: 10.1155/2016/7548498
                PMC ID: 5090090
                SO-VID: 09773b79-6cd8-4077-910f-8afa70494105
                Copyright © Copyright © 2016 Leonardo Gomes Braga Ferreira et al.
                License:

                This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                Date received : 31 May 2016
                Date accepted : 28 August 2016
                Categories
                Subject: Review Article

                Data availability:

                Comments

                Comment on this article

                scite_

                Similar content368

                See all similar

                Cited by5

                See all cited by

                Most referenced authors1,287

                See all reference authors