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Identification of the cDNA for human red blood cell-specific hexokinase
isozyme
K Murakami and S Piomelli
Division of Pediatric Hematology, College of Physicians & Surgeons of
Columbia University, New York 10032, USA.
A unique cDNA for hexokinase (HK) was identified from poly(A)+ RNA of human
reticulocytes by anchored polymerase chain reaction. This appeared to
represent the cDNA for the red blood cell (RBC)-specific HK isozyme (HKR)
described in our previous study (Murakami et al: Blood 75:770, 1990). Its
nucleotide sequence was identical to HKI cDNA except for the 5' extreme
end. It lacked the first 62 nucleotides of the HKI coding region: instead,
it contained a unique sequence of 60 nucleotides at the beginning of the
coding sequence as well as another unique sequence upstream of the putative
translation initiation site. It lacked the porin-binding domain which
facilitates binding to the mitochondria, thus explaining the exclusive
cytoplasmic localization of HKR. It was the major cDNA derived from
reticulocytes, consistent with the observation that HKR activity is
predominant in reticulocytes. Northern blot analysis showed that it was
expressed in the reticulocytes and in the K562 erythroleukemic cell line,
but not in a lymphocytic cell line. In the extract of K562 cells, HKR
activity co- eluted with the HKR of human RBCs on a MonoQ column
(Pharmacia, Piscataway, NJ) chromatography, using a salt gradient elution.
The separate genetic control of the RBC-specific HK isozyme explains the
clinical reports of two types of HK deficiency, one in which the HK
activity was reduced exclusively in the RBC (HKR defect) and another with
general decrease of HK activity in several tissues (HKI defect).
Volume 89,
Issue 3,
pp. 762-766,
02/01/1997
Copyright © 1997 by The American Society of Hematology
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