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Erythroid 5‐aminolevulinate synthase mediates the upregulation of membrane band 3 protein expression by iron
Author(s) -
Huang Qianchuan,
Li Jinying,
Feng Weihua,
Xu Yanqun,
Huang Zhenxia,
Lv Shuqing,
Zhou Hong,
Gao Lei
Publication year - 2010
Publication title -
cell biochemistry and function
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.933
H-Index - 61
eISSN - 1099-0844
pISSN - 0263-6484
DOI - 10.1002/cbf.1629
Subject(s) - k562 cells , small hairpin rna , gene silencing , messenger rna , downregulation and upregulation , transfection , microbiology and biotechnology , western blot , band 3 , chemistry , protein expression , rna interference , biology , membrane protein , rna , biochemistry , cell , gene , membrane
Iron deficiency leads to abnormal expression and function of band 3 protein in erythrocytes, but the underlying mechanisms remain elusive. The mRNA of erythroid‐specific 5‐aminolevulinate synthase (eALAS) contains an iron response element and the eALAS protein is an important mediator of iron utilization by erythrocytes. In this study, we investigated the effect of short hairpin RNA (shRNA) mediated silencing of eALAS on the expression of band 3 protein induced by iron. By real‐time RT‐PCR and Western blot we showed that at mRNA and protein level iron‐induced expression of band 3 protein was lower in eALAS‐shRNA transfected K562 cells than in control cells. Of note, the lowest expression was detected in K562 cells cultured in iron deficiency condition ( p < 0.01). Thus either iron deficiency or depletion of eALAS could suppress the expression of erythroid band 3 protein. These results demonstrated for the first time that iron and the iron‐regulatory system regulate the expression of the erythrocyte membrane proteins. Copyright © 2010 John Wiley & Sons, Ltd.