Blachly-Dyson E, Baldini A, Litt M, McCabe E R, Forte M
Vollum Institute for Advanced Biomedical Research, Oregon Health Sciences University, Portland 97201.
Genomics. 1994 Mar 1;20(1):62-7. doi: 10.1006/geno.1994.1127.
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 form the major pathway for movement of adenine nucleotides through the outer membrane and to be the mitochondrial binding site for hexokinase and glycerol kinase. Previous studies have indicated that at least two human VDAC isoforms are expressed. Here, we report the mapping of VDAC1 to the X chromosome in the interval Xq13-q21 and VDAC2 to chromosome 21 by polymerase chain reaction and restriction analysis of a human/rodent somatic cell mapping panel. In the process of mapping these genes, we identified and mapped two additional sequences highly homologous to VDAC1. VDAC3 maps to chromosome 12 and VDAC4 maps to chromosome 1. The locations of VDAC1 and VDAC4 have been confirmed by fluorescence in situ hybridization analysis. Future studies will be aimed at defining the specific physiological role of each member of this family of channel proteins.
线粒体外膜电压依赖性阴离子通道(VDAC)是一种在所有真核生物线粒体的外膜中发现的小型、丰富的成孔蛋白。据信,VDAC蛋白形成了腺嘌呤核苷酸通过外膜移动的主要途径,并且是己糖激酶和甘油激酶的线粒体结合位点。先前的研究表明,至少有两种人类VDAC异构体表达。在此,我们通过聚合酶链反应和对人/啮齿动物体细胞定位板的限制性分析,报告了VDAC1定位于X染色体的Xq13-q21区间,VDAC2定位于21号染色体。在定位这些基因的过程中,我们鉴定并定位了另外两个与VDAC1高度同源的序列。VDAC3定位于12号染色体,VDAC4定位于1号染色体。VDAC1和VDAC4的位置已通过荧光原位杂交分析得到证实。未来的研究将旨在确定该通道蛋白家族每个成员的具体生理作用。