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Cloning of a soluble isoform of the SgIGSF adhesion molecule that binds the extracellular domain of the membrane-bound isoform

Oncogene volume 23, pages 5687–5692 (2004)Cite this article

Abstract

SgIGSF (spermatogenic immunoglobulin superfamily) is a recently identified intercellular adhesion molecule of the immunoglobulin superfamily. In a mast-cell cDNA library, we found a clone that resulted from the retention of intron 7 within the mature SgIGSF message. This clone was predicted to encode a soluble isoform of SgIGSF (sSgIGSF) with 336 amino-acid residues because its open reading frame ended just before the transmembrane domain. We constructed a plasmid expressing sSgIGSF fused to the human IgG Fc fragment at its C-terminus (sSgIGSF-Fc), and transfected it into COS-7 cells. The fusion protein was readily detectable in the culture supernatant. Solid-phase binding assay showed that sSgIGSF interacted directly the extracellular domain of membrane-bound SgIGSF (mSgIGSF). We next examined whether this interaction inhibited homophilic binding of mSgIGSF by aggregation assays using L cells that did not express mSgIGSF. A stable L-cell clone that overexpressed mSgIGSF aggregated with each other but not with mock-transfected L cells, indicating that a homophilic interaction of mSgIGSF mediated the aggregation. Addition of sSgIGSF-Fc inhibited the aggregation of L cells overexpressing mSgIGSF in a dose-dependent manner. Moreover, FACScan analyses revealed the specific binding of sSgIGSF-Fc to mSgIGSF expressed in L cells. Binding of sSgIGSF-Fc to mSgIGSF appeared to inhibit homophilic interactions of mSgIGSF.

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Acknowledgements

We thank Dr S Nagata for pEFBosFc, Dr T Akagi for pCX4bsr, and Dr A Kumanogoh and M Kohara for technical advice and assistance. The present work was supported by grants from the Ministry of Education, Culture, Sports, Science and Technology of Japan; the Osaka Cancer Society; the Sagawa foundation for promotion of cancer research; the Naito Foundation; and the Japanese Association for Metastasis Research.

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Author notes

  1. Yu-ichiro Koma & Akihiko Ito

    Present address: Division of Surgical Pathology, Kobe University Graduate School of Medicine, 7-5-1 Kusunoki-cho, Chuo-ku, Kobe, 650-0017, Japan

Authors and Affiliations

  1. Department of Pathology, Medical School/Graduate School of Frontier Bioscience, Osaka University, 2-2 Yamada-oka, Suita, Osaka, 565-0871, Japan

    Yu-ichiro Koma, Akihiko Ito, Kenji Watabe & Yukihiko Kitamura

  2. Department of Histology and Embryology, Graduate School of Medical Science, Kanazawa University, Kanazawa, Ishikawa, 920-8640, Japan

    Tomohiko Wakayama & Shoichi Iseki

  3. Department of Thoracic Surgery, Hyogo Medical Center for Adults, Akashi, Hyogo, 673-8558, Japan

    Morihito Okada & Noriaki Tsubota

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  1. Yu-ichiro Koma
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Correspondence to Akihiko Ito.

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Koma, Yi., Ito, A., Wakayama, T. et al. Cloning of a soluble isoform of the SgIGSF adhesion molecule that binds the extracellular domain of the membrane-bound isoform. Oncogene 23, 5687–5692 (2004). https://doi.org/10.1038/sj.onc.1207761

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