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两种小鼠线粒体电压依赖性阴离子通道亚型的分离、特性鉴定及定位

Isolation, characterization, and mapping of two mouse mitochondrial voltage-dependent anion channel isoforms.

作者信息

Sampson M J, Lovell R S, Craigen W J

机构信息

Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, Texas 77030, USA.

出版信息

Genomics. 1996 Apr 15;33(2):283-8. doi: 10.1006/geno.1996.0193.

DOI:10.1006/geno.1996.0193
PMID:8660977
Abstract

Voltage-dependent anion channels (VDACs) are small pore-forming channels found in the mitochondrial outer membrane of all eukaryotes. VDACs conduct adenine nucleotides and are the binding sites for several cytosolic enzymes, including the isoforms of hexokinase and glycerol kinase. VDAC binding is developmentally and metabolically regulated and allows the kinases preferential access to mitochondrial ATP. Two human VDAC cDNAs have recently been identified, and a total of four VDAC loci have been mapped. Here, the isolation of two mouse VDAC cDNAs (VDAC5 and VDAC6) is described. By Northern analysis the two mouse VDAC isoforms show nearly identical expression patterns, with high levels of expression detected in heart, kidney, brain, and skeletal muscle and lesser levels of expression in all other tissues examined. The only exception is the lack of expression of VDAC5 in testes, whereas VDAC6 expression is highest in this tissue. VDAC6 appears to be encoded by more than one transcript. The mouse VDAC5 gene was mapped using an interspecies DNA mapping panel to the proximal region of chromosome 11, and the mouse VDAC6 gene was mapped using a panel to the proximal region of chromosome 14.

摘要

电压依赖性阴离子通道(VDACs)是在所有真核生物线粒体外膜中发现的小孔形成通道。VDACs传导腺嘌呤核苷酸,并且是几种胞质酶的结合位点,包括己糖激酶和甘油激酶的同工型。VDAC的结合受到发育和代谢的调节,并使激酶能够优先获取线粒体ATP。最近已鉴定出两个人类VDAC cDNA,并且总共已定位了四个VDAC基因座。在此,描述了两种小鼠VDAC cDNA(VDAC5和VDAC6)的分离。通过Northern分析,两种小鼠VDAC同工型显示出几乎相同的表达模式,在心脏、肾脏、大脑和骨骼肌中检测到高水平的表达,而在所有其他检查的组织中表达水平较低。唯一的例外是VDAC5在睾丸中不表达,而VDAC6在该组织中的表达最高。VDAC6似乎由不止一种转录本编码。使用种间DNA作图板将小鼠VDAC5基因定位到11号染色体的近端区域,使用一个板将小鼠VDAC6基因定位到14号染色体的近端区域。

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