Skip Navigation

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Ito, I.
Right arrow Articles by Yoshida, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ito, I.
Right arrow Articles by Yoshida, M.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

J. Biochem, 2004, Vol. 136, No. 2 155-162
© 2004 The Japanese Biochemical Society

BIOCHEMISTRY

Conformational Difference in HMGB1 Proteins of Human Neutrophils and Lymphocytes Revealed by Epitope Mapping of a Monoclonal Antibody

Ichiaki Ito1, Nobuyoshi Mitsuoka1, Junko Sobajima2, Hiroko Uesugi3, Shoichi Ozaki4, Kazuhiko Ohya5 and Michiteru Yoshida1,*

1 Department of Biological Science and Technology, Science University of Tokyo, 2641 Yamazaki, Noda 278-8510; 2 Department of Rheumatology and Clinical Immunology, Kyoto University Graduate School of Medicine, 54 Shogoin-Kawahara-cho, Sakyo-ku, Kyoto 606-8507; 3 Saiseikai Noe Hospital, 2-2-3 Imafuku Higashi, Joto-ku, Osaka 536-0002; 4 Division of Rheumatology and Allergy, Department of Internal Medicine, St. Marianna University School of Medicine, 2-16-1 Sugao, Miyamae-ku, Kawasaki 216-8511; and 5 Department of Product Development, Medical and Biological Laboratories Company, Ltd., 5-10 Marunouchi 3-chome, Naka-ku, Nagoya 460

HMGB1 and HMGB2 are abundant nonhistone chromosomal proteins in eukaryotic organisms. Their respective primary sequences are highly conserved. Our previous studies showed that these proteins are novel autoantigens of anti-neutrophil cytoplasmic antibodies in sera from patients with ulcerative colitis (UC), rheumatic disease and autoimmune hepatitis (AIH). In the present paper, we showed that anti-HMGB1 and HMGB2 antibodies in sera of patients with UC do not recognize HMGB1 in neutrophils while they recognize the protein in lymphocytes. Anti-HMGB2 monoclonal antibody FBH7, recognizing HMGB1 in lymphocytes, showed a similar profile to the antibodies in the patients’ sera. In order to elucidate the difference in immunoreactivity to HMGB1 between neutrophils and lymphocytes, we mapped the epitope for FBH7 by means of several methods. The results showed that FBH7 recognizes the intact conformation composed of 52–56 residues of HMGB1 in lymphocytes. This suggested that HMGB1 in neutrophils is conformationally changed in the epitope or the peripheral structure of the epitope from the protein in lymphocytes. The apparent conformational change of HMGB1 between neutrophils and lymphocytes will be important for understanding the functional difference of HMGB1 in these cells.

* To whom correspondence should be addressed. Tel: +81-4-7122-9705, Fax: +81-4-7125-1841, E-mail: myoshida{at}rs.noda.tus.ac.jp


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
I. Ito, J. Fukazawa, and M. Yoshida
Post-translational Methylation of High Mobility Group Box 1 (HMGB1) Causes Its Cytoplasmic Localization in Neutrophils
J. Biol. Chem., June 1, 2007; 282(22): 16336 - 16344.
[Abstract] [Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.