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Rat peritoneal macrophages were shown to have two distinct mannose/fucose/N-acetylglucosamine-specific lectins. The major lectin of 180 kDa, which is similar in size to the mannose receptor first isolated from alveolar macrophages (Wileman, T.E., Lennartz, M.R., & Stahl, P.D. (1986) Proc. Natl. Acad. Sci. U.S. 83, 2501-2505), was shown to occur as a dimer under nondenaturing conditions. The 29 and 32 kDa lectins were identified as members of the liver mannan-binding protein family on the basis of their immunochemical crossreactivity, collagenase sensitivity, and molecular sizes (Oka, S., Ikeda, K., Kawasaki, T., & Yamashina, I. (1988) Arch. Biochem. Biophys. 260, 257-266). Despite the similarity in the sugar binding specificity, these two types of lectin were clearly differentiated with regard to the binding to IgM molecules. The 29 and 32 kDa lectins bound to IgM most likely through high-mannose type oligosaccharides on IgM, whereas the 180 kDa lectin did not.
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