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Expression of human mitochondrial NADP‐dependent isocitrate dehydrogenase during lymphocyte activation
Author(s) -
Luo Hongyu,
Shan Xiaochuan,
Wu Jiangping
Publication year - 1996
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/(sici)1097-4644(19960315)60:4<495::aid-jcb6>3.0.co;2-n
Subject(s) - microbiology and biotechnology , biology , complementary dna , gene expression , isocitrate dehydrogenase , mitochondrion , jurkat cells , messenger rna , gene , t cell , biochemistry , enzyme , immunology , immune system
In the process of identifying genes involved in optimization of lymphocyte activation, we have cloned the human mitochondrial NADP‐dependent isocitrate dehydrogenase (mNADP‐IDH) cDNA. The cDNA and its deduced amino acid (AA) sequence had a high degree of homology with those of the porcine and bovine. The heart and muscle had the highest constitutive expression of the gene. The expression of steady‐state mRNA in the resting T and B lymphocytes was low but was induced after mitogen stimulation. The mRNA levels peaked around 48 h and remained elevated at 72 h. At the protein level, the micothondrial but not cytosolic NADP‐IDH activity was augmented after the mitogen stimulation. There was no cell cycle‐dependent fluctuation of mNADP‐IDH expression in synchronized Jurkat cells. In T and B cells, rapamycin (RAPA) could repress the mitogen‐stimulated mNADP‐IDH expression, although most of the early or late phase activation‐related genes including a G‐protein β subunit‐related gene H12.3 were not affected by the drug. The restricted expression of the gene in certain tissues and the activation‐related expression in lymphocytes suggest that this gene might be necessary for optimal functions in heart, muscle, and the activated lymphocytes. © 1996 Wiley‐Liss, Inc.