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| July 1998, Volume 6, Number 4, Pages 337-340 |
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| Original paper |
| Isolation of a novel human voltage-dependent anion channel gene |
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| Zohra Rahmani1,2,a, Catherine Maunoury2 and Aleem Siddiqui1 |
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1Department of Microbiology and Program in Molecular Biology, University of Colorado Health Sciences Center, Denver, Colorado, USA
2Hôpital Necker-Enfants Malades, CNRS URA 1335 Paris, France
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aCorrespondence: Hôpital Necker-Enfants Malades, Faculté de Médecine, CNRS URA 1335, 156 Rue de Vaugirard, 75730 Paris Cedex 15, France. Tel: 331 40 61 56 96; Fax: 331 40 61 56 90; E-mail: rahmani@ceylan.necker.fr. |
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| Abstract |
| The voltage-dependent anion channel of the mitochondrial outer membrane (VDAC) is a small, abundant pore-forming protein found in the outer membranes of all eukaryotic mitochondria. The VDAC protein is believed to control the movement of adenine nucleotides through the outer membrane and to be the mitochondrial binding site for hexokinase and glycerol kinase. Two human VDAC cDNAs (HVDAC1 and HVDAC2) have been previously isolated and mapped on chromosome X and 21, respectively. Here, we report the isolation of a novel third human VDAC cDNA, corresponding to the mouse MVDAC3 gene. The expression of this gene in various tissues and its chromosomal localization by polymerase chain reaction (PCR) using a human/rodent somatic cell mapping panel and by fluorescence in situ hybridization is also presented. |
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| Keywords |
| VDAC; fluorescence in situ hybridization; gene mapping; chromosome 8 |
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| Received 17 September 1997; revised 15 January 1998; accepted 26 January 1998 |
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| July 1998, Volume 6, Number 4, Pages 337-340 |
| Table of contents Previous Abstract Next Article PDF |
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