Immunocytochemical localization of peptidylarginine deiminase in human eosinophils and neutrophils.
Peptidylarginine deiminase, registered as PAD V in the DDBJ/GenBank/EMBL data banks, is expressed in HL-60 cells differentiated into granulocytes or monocytes. We analyzed PAD activities in density-fractionated human peripheral blood cell fractions. PAD activity with similar substrate specificity to that of PAD V was found in the eosinophil and neutrophil fractions, which showed single bands comigrating with authentic PAD V on immunoblotting with an anti-PAD V antibody. Both the biochemical and immunoblotting analyses showed marked enrichment of PAD V in the eosinophil fraction. Its immunoreactivity appeared to localize in eosinophilic granules at high density and in myeloperoxidase-negative cytoplasmic granules of neutrophils at low density, as determined by confocal laser-scanning microscopy. Possible roles of PAD V in myeloid differentiation and granulocyte function are discussed. In addition, we present evidence for the presence of PAD(s) that are antigenically different from PAD V in monocytes and lymphocytes.
Asaga
H
H
Department of Bioactivity Regulation, Tokyo Metropolitan Institute of Gerontology, Tokyo, and Graduate School of Integrated Science, Yokohama City University, Yokohama, Japan.
Nakashima
K
K
Senshu
T
T
Ishigami
A
A
Yamada
M
M
D015153:Blotting, Western; D002454:Cell Differentiation / Q000502:physiology; D004804:Eosinophils / Q000201:enzymology*; D006098:Granulocytes / Q000201:enzymology; D018922:HL-60 Cells / Q000166:cytology / Q000201:enzymology; D006801:Humans; D006867:Hydrolases / Q000097:blood*; D007150:Immunohistochemistry; D009504:Neutrophils / Q000201:enzymology*; D000080002:Protein-Arginine Deiminase Type 4; D000076342:Protein-Arginine Deiminases; D013379:Substrate Specificity
D006867:Hydrolases; C000629235:PADI4 protein, human; D000080002:Protein-Arginine Deiminase Type 4; D000076342:Protein-Arginine Deiminases