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Surfactant proteins A and D (SP-A and SP-D) are members of a large family of proteins termed the C-type lectins, which are located on the cell surface and in lysosomes of many types of cells. A third family of C-type lectins, SP-B, which are most closely related to the tetraspanin superfamily, are also known to be distributed on the surface of alveolar type II cells. We have analyzed the structure and cellular distribution of SP-B by Western blotting and immunofluorescence microscopy, using a SP-B specific monoclonal antibody (SP-B2) raised to a synthetic peptide corresponding to the C-terminus of mature rat SP-B. We confirmed the presence of SP-B in the lung by comparing the SP-B band with that observed for surfactant-associated protein D (SP-D). In the steady state, SP-B2 immunofluorescence was observed in numerous types of cells including alveolar type I and II cells. During alveolar type II cell regeneration, neutrophils, which are known to be the major source of SP-D, were the only cells to stain for SP-B2. SP-B2 immunoreactivity was also observed in the circulation of rats following administration of concanavalin A (Con A) suggesting that plasma contains a non-glycosylated form of SP-B. To further define the cellular distribution of SP-B in the lung, pulmonary parenchyma, bronchoalveolar lavage fluid and lung washings were fractionated by differential centrifugation. SP-B immunofluorescence was observed in the fraction of lavageable material which sedimented at 1.03-1.1 M sucrose. In contrast, the SP-B band was not observed in the 10-60% and 60-80% sucrose fractions
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