E. Blachlydyson et al., HUMAN GENES ENCODING THE VOLTAGE-DEPENDENT ANION CHANNEL (VDAC) OF THE OUTER MITOCHONDRIAL-MEMBRANE - MAPPING AND IDENTIFICATION OF 2 NEW ISOFORMS, Genomics, 20(1), 1994, pp. 62-67
The voltage-dependent anion channel of the mitochondrial outer membran
e (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 hexok
inase and glycerol kinase. Previous studies have indicated that at lea
st two human VDAC isoforms are expressed. Here, we report the mapping
of VDAC 1 to the X chromosome in the interval Xq13-q21 and VDAC2 to ch
romosome 21 by polymerase chain reaction and restriction analysis of a
human/rodent somatic cell mapping panel. In the process of mapping th
ese genes, we identified and mapped two additional sequences highly ho
mologous to VDAC1. VDAC3 maps to chromosome 12 and VDAC4 maps to chrom
osome 1. The locations of VDAC1 and VDAC4 have been confirmed by fluor
escence in situ hybridization analysis. Future studies will be aimed a
t defining the specific physiological role of each member of this fami
ly of channel proteins. (C) 1994 Academic Press, Inc.