The Lung Lectin Surfactant Protein A Aggregates Phospholipid Vesicles Via a Novel Mechanism

Overview

Journal Biochem J

Specialty Biochemistry

Date 1991 Apr 1

PMID 2018482

Citations 11

Authors

H P Haagsman

R H Elfring

B L van Buel

W F Voorhout

Affiliations

Soon will be listed here.

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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