Volume 272, Number 16, Issue of April 18, 1997 pp. 10579-10584
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

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Lectin-like Characteristics of Recombinant Human Interleukin-1 Recognizing Glycans of the Glycosylphosphatidylinositol Anchor

(Received for publication, January 14, 1997, and in revised form, February 10, 1997)

Keiko Fukushima , Sayuri Hara-Kuge , Takashi Ohkura , Akira Seko , Hiroko Ideo , Toshiyuki Inazu and Katsuko Yamashita

From the Department of Biochemistry, Sasaki Institute, Kanda-Surugadai, Chiyoda-ku, Tokyo 101 and the  Noguchi Institute, Kaga, Itabashi-ku, Tokyo 173, Japan

We found that ³⁵S-labeled recombinant human interleukin-1 (rhIL-1) binds phosphatidylinositol-specific phospholipase C-treated human placental alkaline phosphatase, phosphatidylinositol-specific phospholipase C-treated trypanosome surface variant glycoproteins, and urinary uromodulin immobilized on plates or immobilized on CNBr-activated Sepharose 4B. The interaction between rhIL-1 and these glycoproteins was lectin-like, since it was inhibited in the presence of specific saccharides, i.e. mannose 6-phosphate or synthetic Ac-NH·CH₂·CH₂·PO₄6Man1(±2Man1±6Man1)propyl at about 1 µM. On the other hand, a wide variety of compounds including biantennary sugar chains derived from these glycoproteins as well as ethanolamine phosphate, inositol phosphate, mannose 6-sulfate, mannose 1-phosphate, glucose 6-phosphate, and mannitol 6-phosphate did not show any inhibitory effect at concentrations up to 1 mM. These results indicate that rhIL-1 interacts with these glycoproteins via the mannose 6-phosphate diester of glycans on the glycosylphosphatidylinositol (GPI) anchor. Furthermore, when monolayers of polarized Madin-Darby canine kidney cells on polycarbonate filter membranes were incubated with ³⁵S-rhIL-1 in either the apical or basolateral chamber, ³⁵S-interleukin-1 was found to bind specifically to the apical membranes with a K_a value of 4.6 × 10⁷ M¹, and the specific interaction was inhibited by 1 µM mannose 6-phosphate. Since the mannose 6-phosphate diester moiety exists only in the GPI glycans on plasma membranes, it was evident that interleukin-1 can directly interact with the mannose 6-phosphate diester component of the intact glycan of GPI anchors on plasma membranes.

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