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. 1991 Apr 1;275(Pt 1):273–276. doi: 10.1042/bj2750273

The lung lectin surfactant protein A aggregates phospholipid vesicles via a novel mechanism.

H P Haagsman 1, R H Elfring 1, B L van Buel 1, W F Voorhout 1
PMCID: PMC1150045  PMID: 2018482

Abstract

Surfactant protein A (SP-A), a lung-specific glycoprotein, consists of an N-terminal collagen-like domain and a C-terminal domain with a sequence similar to that of several Ca2(+)-dependent lectins. SP-A induces a rapid Ca2(+)-dependent aggregation of phospholipid vesicles. We report here that vesicle aggregation is mediated by Ca2(+)-induced interactions between carbohydrate-binding domains and oligosaccharide moieties of SP-A. This novel mechanism of membrane interactions may be relevant to the formation of the membrane lattice of tubular myelin, an extracellular form of surfactant.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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