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


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          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.

          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.
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            Molecular cloning, expression and characterization of an endogenous human cytochrome P450 arachidonic acid epoxygenase isoform.

            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


                Author and article information

                S. Karger AG
                July 1999
                21 June 1999
                : 82
                : 3
                : 254-260
                Division of Toxicology, University of Arkansas for Medical Sciences, Little Rock, Ark., USA
                45410 Nephron 1999;82:254–260@5L}@4A}
                © 1999 S. Karger AG, Basel

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                Page count
                Figures: 6, References: 16, Pages: 7
                Self URI (application/pdf): https://www.karger.com/Article/Pdf/45410
                Self URI (text/html): https://www.karger.com/Article/FullText/45410
                Self URI (journal page): https://www.karger.com/SubjectArea/Nephrology
                Original Paper

                Cardiovascular Medicine,Nephrology
                Renal proximal tubule,Neuronal glycine receptor β-subunit


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