Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 290, Issue 3, Pages 979-983Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1006/bbrc.2001.6303
Keywords
peptidylarginine deiminase; posttranslational modification; protein deimination; citrulline-containing proteins; nucleophosmin/B23; histones; granulocytes; HL-60 cells; calcium ion; calcium ionophore
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Peptidylarginine deiminases (PADS) convert arginine residues in proteins into citrulline residues Ca2+-dependently. PAD V was recently found in granulocyte-differentiated BL-60 cells. To find a target of PAD V, we incubated BL-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. (C) 2002 Elsevier Science (USA).
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