Y. Lee et al., CLONING AND EXPRESSION OF HUMAN ADENYLATE KINASE-2 ISOZYMES - DIFFERENTIAL EXPRESSION OF ADENYLATE KINASE-1 AND KINASE-2 IN HUMAN MUSCLE TISSUES, Journal of Biochemistry, 123(1), 1998, pp. 47-54
A cDNA clone coding for adenylate kinase 2B was isolated from fetal li
ver, and the expression of AK2 was investigated in human tissues. The
ORF in the cDNA clone for human AK2B predicted a protein comprising 23
2 amino acids (25.6 kDa), The features of AK2A and AK2B sequences in h
uman were the same as those in the bovine system, Each of the recombin
ant proteins, AK2A and AK2B, was expressed in Escherichia coli cells,
and the purified recombinant proteins were enzymatically active, The d
istribution of AK2 transcripts in various human tissues was examined b
y Northern analysis, Unlike in the bovine system, it was found that th
e AK2A transcript was the major form of AK2 mRNA species in all human
tissues, The transcripts of AK2 isozymes were relatively abundant in h
eart, liver, and also in skeletal muscle, where the expression level o
f AK2 was known to be low, Western blot analysis of AK isozymes in hum
an heart and skeletal muscle revealed that AK2 protein was found only
in heart, whereas AK1 was detected in both tissues, These tissue-speci
fic expressions of the AK isozymes in human might suggest the presence
of organ-specific regulation of the AK2 gene including a post-transcr
iptional control in skeletal muscle.