Deimination of Arginine Residues in Nucleophosmin/B23 and Histones in HL-60 Granulocytes

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• 作者：Hagiwara ; Teruki ; Nakashima ; Katsuhiko ; Hirano ; Hisashi ; Senshu ; Tatsuo ; Yamada ; Michiyuki
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2002
• 出版时间：January 25, 2002
• 年：2002
• 卷：290
• 期：3
• 页码：979-983
• 全文大小：172 K

文摘

Peptidylarginine deiminases (PADs) convert arginine residues in proteins into citrulline residues Ca²⁺-dependently. PAD V was recently found in granulocyte-differentiated HL-60 cells. To find a target of PAD V, we incubated HL-60 granulocytes with the calcium ionophore A23187 and studied deiminated proteins by immunocytochemistry and immunoblotting using a monospecific antibody to modified citrulline residues. Immunocytochemical signals were found in the nucleus upon incubation with A23187. Immunoblotting indicated that 40-, 18-, 17-, and 14-kDa proteins were preferentially deiminated. The 40-kDa protein, which was focused to pI 5.0 on two-dimensional gel electrophoresis, was identified as nucleophosmin/B23 by mass spectrometry. The 18-, 17-, and 14-kDa proteins extracted with 0.4 N H₂SO₄ comigrated with histones H3, H2A, and H4, respectively, on two-dimensional gel electrophoresis specialized for histones. The citrulline content of histones amounted to about 10 % of the histone molecules. We discuss the implications of deimination of these proteins for their nuclear functions.