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The formation of argpyrimidine, a methylglyoxal-arginine adduct, in the nucleus of neural cells

Journal Article · · Biochemical and Biophysical Research Communications
 [1];  [2]; ; ;  [1];  [3]; ;  [4];  [1]
  1. Department of Bioengineering, Graduate School of Engineering, Osaka City University, 3-3-138 Sugimoto, Sumiyoshi-ku, Osaka 558-8585 (Japan)
  2. Laboratory of Food and Biodynamics, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601 (Japan)
  3. Division of Brain Function, National Institute of Genetics, Graduate University for Advanced Studies, SOKENDAI, Yata 1111, Mishima 411-8540 (Japan)
  4. Departments of Anatomy and Neurobiology, Graduate School of Medicine, Osaka City University, Osaka 545-8585 (Japan)
Methylglyoxal (MG) is an endogenous metabolite in glycolysis and forms stable adducts primarily with arginine residues of intracellular proteins. The biological role of this modification in cell function is not known. In the present study, we found that a MG-detoxification enzyme glyoxalase I (GLO1) is mainly expressed in the ventricular zone (VZ) at embryonic day 16 which neural stem and progenitor cells localize. Moreover, immunohistochemical analysis revealed that argpyrimidine, a major MG-arginine adduct, is predominantly produced in cortical plate neurons not VZ during cerebral cortex development and is exclusively located in the nucleus. Immunoblotting experiment showed that the formation of argpyrimidine occurs on some nuclear proteins of cortical neurons. To our knowledge, this is first report of the argpyrimidine formation in the nucleus of neuron. These findings suggest that GLO1, which is dominantly expressed in the embryonic VZ, reduces the intracellular level of MG and suppresses the formation of argpyrimidine in neural stem and progenitor cells. Argpyrimidine may contribute to the neural differentiation and/or the maintenance of the differentiated state via the modification of nuclear proteins.
OSTI ID:
21255823
Journal Information:
Biochemical and Biophysical Research Communications, Journal Name: Biochemical and Biophysical Research Communications Journal Issue: 2 Vol. 378; ISSN 0006-291X; ISSN BBRCA9
Country of Publication:
United States
Language:
English

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