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Clinical and Developmental Immunology
Volume 12, Issue 1, Pages 67-73
http://dx.doi.org/10.1080/17402520400014168

Characterization of a Murine Anti-laminin-1 Monoclonal Antibody (AK8) Produced by Immunization with Mouse-derived Laminin-1

1Department of Obstetrics and Gynecology, Center for Specialized Clinical Science, Tokai University, School of Medicine, Ishehara, Japan
2Department of Cell Chemistry, Okayama University Graduate School of Medicine and Dentistry, Shikata-cho, 2-5-1 Shikata-cho, Okayama 700-8558, Japan
3Department of Laboratory for Molecular Science Research, Tokai University, School of Medicine, Ishehara, Japan
4Biomedical Computation Center, Osaka Medical College, Takatsuki, Japan
5Department of Obstetrics and Gynecology, Okayama University Hospital, Okayama, Japan
6Tokyo University of Pharmacy and Life Science, Hachiouji, Japan
7Shiseido Life Science Research Center, Yokohama, Japan
8Corgenix Inc, Westminster, Colorado, USA
9Department of Medicine B and Center for Autoimmune Diseases, Sheba Medical Center, Tel-hashomer, Israel

Copyright © 2005 Hindawi Publishing Corporation. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

Laminin-1 is a structural glycoprotein that forms an integral part of the scaffolding of basement membranes, and plays an important role during embryonic development. We have recently demonstrated a significant association between anti-laminin-1 antibodies (Abs) and reproductive failure, such as recurrent spontaneous abortions and infertility-associated endometriosis in both human and mouse studies. In the present study, we established an IgM (μ,κ) monoclonal anti-laminin-1 Ab (AK8) by immunizing mice with mouse Engelbreth-Holm-Swarm sarcoma (EHS)-derived laminin-α1. The AK8 monoclonal antibody (mAb) reacted with particular peptide sequences from the globular G domain of mouse laminin-α1 chain of using ELISA and Western blot techniques. The peptide tertiary structure of the epitope recognized by AK8 mAb was predicted using eight synthesized domain peptide sequences and three consensus sequences obtained by phage displayed random peptide library. Basement membranes of endometrium of pregnant mice and humans were immunostained with AK8 mAb. Thus, AK8 mAb recognized a common structure present in the G domain of the laminin-1 chain in both mice and humans. The passive immunization of mice with AK8 mAb may represent a suitable animal model for anti-laminin-1 Ab-mediated reproductive failure.