Volume 29, Issue 4 pp. 211-218
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Interspecies-specific Ovarian Autoantigens Involved in Neonatal Thymectomy-induced Murine Autoimmune Oophoritis

ZHU XUN

ZHU XUN

Faculty of Medicine

Institute for Immunology, Kyoto University, Kyoto, Japan

Zhu Xun is now at the Department of Immunology, Norman Bethune University of Medical Science, Changchun, China.

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HIDENORI MARUYAMA

HIDENORI MARUYAMA

Faculty of Medicine

Institute for Immunology, Kyoto University, Kyoto, Japan

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MASAMICHI UEDA

MASAMICHI UEDA

Department of Pathology, Institute for Virus Research, Kyoto University, Kyoto, Japan

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MANABU FUKUMOTO

MANABU FUKUMOTO

Department of Pathology, Faculty of Medicine, Kyoto University, Kyoto, Japan

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TOHRU MASUDA

Corresponding Author

TOHRU MASUDA

Faculty of Medicine

Institute for Immunology, Kyoto University, Kyoto, Japan

Institute for Immunology, Faculty of Medicine, Kyoto University, Yoshida-Konoe, Sakyo 606, Kyoto, Japan.Search for more papers by this author

Abstract

PROBLEM: Thymectomy of mice on day 3 after birth (3d-Tx) gives rise to the appearance of a particular type of ovarian lesion known as experimental autoimmune oophoritis (AIO).

METHOD: In the present study, the spleen cells from BALB/c mice having undergone 3 day-Tx AIO were fused with X63-Ag8-6.5.3 myeloma cells, and a number of hybridoma clones producing autoantibodies against ovarian tissue were established.

RESULTS: On the basis of immunohistochemical and protein-chemical analysis, two independent clones, designated as T2.2 and S1.6, were found to react with interstitial tissues surrounding the follicles. These monoclonal antibodies showed broad cross-species reactivity, in that they recognized similar antigenic macromolecules in the rat, pig, human, and mouse. The antigenic determinants were strongly resistant to heat and acid, especially to the treatment of periodic acid, indicating that the antigenic determinants had no relation with carbohydrate components.

CONCLUSIONS: By antibody affinity chromotography, two kinds of autoantigens were identified. SDS-PAGE, under reduced or nonreduced conditions, revealed an 80/85 kDa protein for T2.2, and an 82 kDa for S1.6, respectively.

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