THE LUNG LECTIN SURFACTANT PROTEIN-A AGGREGATES PHOSPHOLIPID-VESICLES VIA A NOVEL MECHANISM

被引：50

作者：

HAAGSMAN, HP ^{[1
]}

ELFRING, RH ^{[1
]}

VANBUEL, BLM ^{[1
]}

VOORHOUT, WF ^{[1
]}

机构：

[1] STATE UNIV UTRECHT,FAC MED,DEPT CELL BIOL,3508 TD UTRECHT,NETHERLANDS

来源：

BIOCHEMICAL JOURNAL | 1991年 / 275卷

关键词：

D O I：

10.1042/bj2750273

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：273 / 276

页数：4

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