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      Call for Papers: Green Renal Replacement Therapy: Caring for the Environment

      Submit here before September 30, 2024

      About Blood Purification: 3.0 Impact Factor I 5.6 CiteScore I 0.83 Scimago Journal & Country Rank (SJR)

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      Expression and Localization of the Neuronal Glycine Receptor Beta-Subunit in Human, Rabbit and Rat Kidneys

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          Abstract

          The glycine receptor (GlyR) is a ligand-gated Cl<sup>–</sup> channel composed of two transmembrane subunits, α and β, and gephyrin. The goal of this study was to determine whether the α- and/or β-subunits of the GlyR are expressed in human, rabbit and/or rat kidneys. Screening of human and rat kidney cortex cDNA libraries identified polymerase chain reaction products that were identical to the neuronal GlyR β-subunit. Sequencing revealed that rat kidney cortex and neuronal GlyR β-subunits were identical. RNA isolated from the S<sub>2</sub> segment of rabbit renal proximal tubules (RPT) and rat and rabbit kidney cortex was amplified following reverse transcription and gave similar results to that of human and rat kidney cDNA libraries. Degenerate primers against all GlyR α-subunits did not yield a product from rat and rabbit kidney cortex RNA, or from human and rat kidney cortex cDNA libraries. Immunofluorescence studies localized the β-subunit and gephyrin to the basolateral membrane of rabbit RPT. These results provide compelling evidence for the GlyR β-subunit, but not the α-subunit, in human, rabbit and rat kidney cortex.

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          The strychnine-binding subunit of the glycine receptor shows homology with nicotinic acetylcholine receptors.

          G Grenningloh, A Rienitz, B. Schmitt … (2015)
          We have cloned and sequenced cDNAs of the strychnine-binding subunit of the rat glycine receptor, a neurotransmitter-gated chloride channel protein of the CNS. The deduced polypeptide shows significant structural and amino-acid sequence homology with nicotinic acetylcholine receptor proteins, indicating that there is a family of genes encoding neurotransmitter-gated ion channels.
          Article 0 comments Cited 55 times – based on 0 reviews     Review now
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            Molecular cloning, expression and characterization of an endogenous human cytochrome P450 arachidonic acid epoxygenase isoform.

            Darryl C. Zeldin, J Russel Falck, J. Capdevila … (1995)
            A cDNA containing an open reading frame coding for a human cytochrome P450 arachidonic acid epoxygenase was isolated from a male human kidney cDNA library. Sequence analysis showed that, with few exceptions, this cDNA was nearly identical to the published sequence for human liver Cyp 2C8 (S. T. Okino et al., 1987, J. Biol. Chem. 262, 16072-16079) and encoded a polypeptide of 490 amino acids. Nucleic acid hybridization indicated that: (a) Cyp 2C8 and 2C10 were expressed at comparable levels in the human liver and (b) compared to Cyp 2C10, the steady state concentrations of Cyp 2C8 transcripts in the human kidney were substantially lower. The kidney 2C8 cDNA was cloned into a pBlue BacIII vector, expressed using a baculovirus/Sf9 insect cell system, and the recombinant Cyp 2C8 protein was purified by a combination of hydrophobic and hydroxylapatite chromatography. Purified recombinant Cyp 2C8 and 2C10 were reconstituted in the presence of NADPH and NADPH-cytochrome P450 reductase and shown to metabolize arachidonic via olefin epoxidation with both proteins generating, almost exclusively, epoxygenase-derived products (94 and 90% of total products, respectively). Catalytic turnover (1.05 and 0.75 nmol of product/nmol of hemoprotein/min at 30 degrees C for Cyp 2C8 and 2C10, respectively) was inhibited by the addition of purified cytochrome b5. Metabolism by recombinant 2C8 was both regio- and enantioselective for 11(R), 12(S)- and 14(R), 15(S)-epoxyeicosatrienoic acids (82% optical purity, each). Compared to Cyp 2C8, arachidonic acid epoxidation by Cyp 2C10 was less regio- and stereo-selective and generated mixtures of 8(S), 9(R)-, 11(S), 12(R)-, and 14(R), 15(S)-epoxyeicosatrienoic acids (with optical purities of 66, 69, 63%, respectively). Importantly, recombinant Cyp 2C8 and 2C10 epoxidized the arachidonic acid 11, 12-olefin with opposite enantiofacial selectivities. Only for Cyp 2C8 did the chirality of the products match that of the enantiomers present, in vivo, in human kidney cortex (A. Karara et al., 1990, FEBS Lett. 268, 227-230). Hence, we propose that Cyp 2C8 is one of the human cytochrome P450 isoforms responsible for the metabolism of endogenous arachidonic acid pools.
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              Alternative splicing generates two isoforms of the α2 subunit of the inhibitory glycine receptor

              A Kuryatov, Y Maulet, M.L. Malosio … (1991)
              Article 0 comments Cited 15 times – based on 0 reviews     Review now
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                Author and article information

                Journal
                Journal ID (publisher-id): NEF
                Journal ID (nlm-ta): Nephron
                Journal ID (doi): 10.1159/issn.1660-8151
                Title: Nephron
                Publisher: S. Karger AG
                ISSN (Print): 1660-8151
                ISSN (Electronic): 2235-3186
                Publication date Subscription-year: 1999
                Publication date (Print): July 1999
                Publication date (Electronic): 21 June 1999
                Volume: 82
                Issue: 3
                Pages: 254-260
                Affiliations
                Division of Toxicology, University of Arkansas for Medical Sciences, Little Rock, Ark., USA
                Article
                Publisher ID: 45410 Other ID: Nephron 1999;82:254–260@5L}@4A}
                DOI: 10.1159/000045410
                PubMed ID: 10395998
                SO-VID: 3455dee8-a9a6-48c7-97c9-1c00dc11c9f0
                Copyright © © 1999 S. Karger AG, Basel
                License:

                Copyright: All rights reserved. No part of this publication may be translated into other languages, reproduced or utilized in any form or by any means, electronic or mechanical, including photocopying, recording, microcopying, or by any information storage and retrieval system, without permission in writing from the publisher. Drug Dosage: The authors and the publisher have exerted every effort to ensure that drug selection and dosage set forth in this text are in accord with current recommendations and practice at the time of publication. However, in view of ongoing research, changes in government regulations, and the constant flow of information relating to drug therapy and drug reactions, the reader is urged to check the package insert for each drug for any changes in indications and dosage and for added warnings and precautions. This is particularly important when the recommended agent is a new and/or infrequently employed drug. Disclaimer: The statements, opinions and data contained in this publication are solely those of the individual authors and contributors and not of the publishers and the editor(s). The appearance of advertisements or/and product references in the publication is not a warranty, endorsement, or approval of the products or services advertised or of their effectiveness, quality or safety. The publisher and the editor(s) disclaim responsibility for any injury to persons or property resulting from any ideas, methods, instructions or products referred to in the content or advertisements.

                History
                Page count
                Figures: 6, References: 16, Pages: 7
                Categories
                Subject: Original Paper

                ScienceOpen disciplines: Cardiovascular Medicine,Nephrology
                Keywords: Renal proximal tubule,Neuronal glycine receptor β-subunit
                Data availability:
                ScienceOpen disciplines: Cardiovascular Medicine, Nephrology
                Keywords: Renal proximal tubule, Neuronal glycine receptor β-subunit

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