| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
* Department of Bioactivity Regulation, Tokyo Metropolitan Institute of Gerontology, Tokyo, and
Graduate School of Integrated Science, Yokohama City University, Yokohama, Japan
Correspondence: Michiyuki Yamada, Ph.D., Graduate School of Integrated Science, Yokohama City University, 22-2, Seto, Kanazawa-ku, Yokohama 236 0027, Japan. E-mail: myamada{at}yokohama-cu.ac.jp
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.
Key Words: citrullinated proteins • HL-60 cells • peripheral blood cells • granulocytes • monocytes • posttranslational modification enzyme • protein deimination
This article has been cited by other articles:
|
|
 |
|
  I. Neeli, S. N. Khan, and M. Radic Histone Deimination As a Response to Inflammatory Stimuli in Neutrophils J. Immunol., February 1, 2008; 180(3): 1895 - 1902. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 H. C. Looker, R. G. Nelson, E. Chew, R. Klein, B. E.K. Klein, W. C. Knowler, and R. L. Hanson Genome-Wide Linkage Analyses to Identify Loci for Diabetic Retinopathy Diabetes, April 1, 2007; 56(4): 1160 - 1166. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. Ireland, J. Herzog, and E. R. Unanue Cutting Edge: Unique T Cells That Recognize Citrullinated Peptides Are a Feature of Protein Immunization J. Immunol., August 1, 2006; 177(3): 1421 - 1425. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 Y Takizawa, A Suzuki, T Sawada, M Ohsaka, T Inoue, R Yamada, and K Yamamoto Citrullinated fibrinogen detected as a soluble citrullinated autoantigen in rheumatoid arthritis synovial fluids Ann Rheum Dis, August 1, 2006; 65(8): 1013 - 1020. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 E. Moisan and D. Girard Cell surface expression of intermediate filament proteins vimentin and lamin B1 in human neutrophil spontaneous apoptosis J. Leukoc. Biol., March 1, 2006; 79(3): 489 - 498. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 X. Chang, R. Yamada, A. Suzuki, T. Sawada, S. Yoshino, S. Tokuhiro, and K. Yamamoto Localization of peptidylarginine deiminase 4 (PADI4) and citrullinated protein in synovial tissue of rheumatoid arthritis Rheumatology, January 1, 2005; 44(1): 40 - 50. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
E R Vossenaar, T R D Radstake, A van der Heijden, M A M van Mansum, C Dieteren, D-J de Rooij, P Barrera, A J W Zendman, and W J van Venrooij Expression and activity of citrullinating peptidylarginine deiminase enzymes in monocytes and macrophages Ann Rheum Dis, April 1, 2004; 63(4): 373 - 381. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 K. Nakashima, T. Hagiwara, and M. Yamada Nuclear Localization of Peptidylarginine Deiminase V and Histone Deimination in Granulocytes J. Biol. Chem., December 13, 2002; 277(51): 49562 - 49568. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
