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The lung lectin surfactant protein A aggregates phospholipid vesicles via a novel mechanism
H P Haagsman1, R H Elfring, B L van Buel
1Laboratory of Veterinary Biochemistry, Medical Faculty, University of Utrecht, The Netherlands.
The Biochemical Journal
|April 1, 1991
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.