Role of surfactant protein A (SP-A)/lipid interactions for SP-A functions in the lung

被引:46
作者
Casals, C [1 ]
机构
[1] Univ Complutense, Sch Biol, Dept Biochem & Mol Biol, E-28040 Madrid, Spain
来源
PEDIATRIC PATHOLOGY & MOLECULAR MEDICINE | 2001年 / 20卷 / 04期
关键词
membranes; phospholipids; pulmonary surfactant; SP-A; surfactant monolayer; vesicle aggregation;
D O I
10.1080/152279501750412216
中图分类号
R36 [病理学];
学科分类号
100104 ;
摘要
Surfactant protein A (SP-A), an oligomeric glycoprotein, is a member of a group of proteins named collectins that contain collagen-like and Ca2+-dependent carbohydrate recognition domains. SP-A interacts with a broad range of amphipathic lipids (glycerophospholipids, sphingophospholipids, glycosphingolipids, lipid A, and lipoglycans) that are present in surfactant or microbial membranes. This review summarizes SP-A/lipid interaction studies regarding the lipid system used (i.e., phospholipid vesicles, phospholipid monolayers, and lipids immobilized on silica or adsorbed on a solid support). The effect of calcium, ionic strength, and pH on the binding of SP-A to lipids and the subsequent lipid aggregation process is discussed. Current evidence suggests that hydrophobic-binding forces are involved in the peripherical association of SP-A to membranes. It is also proposed that fluid and liquid-ordered phase coexistence in surfactant membranes might favor partition of SP-A into those membranes. The binding of SP-A to surfactant membranes containing hydrophobic surfactant peptides makes possible the formation of a membrane reservoir in the alveolar fluid that is protected by SP-A against inactivation and improves the rate of surfactant film formation. In addition, the interaction of SP-A with membranes might enhance the affinity of SP-A for terminal carbohydrates of glycolipids or glycoproteins on the surface of invading microorganisms.
引用
收藏
页码:249 / 268
页数:20
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