Structure of pulmonary surfactant membranes and films:: The role of proteins and lipid-protein interactions

被引:376
作者
Perez-Gil, Jesus [1 ]
机构
[1] Univ Complutense, Fac Biol, Dept Bioquim, E-28040 Madrid, Spain
来源
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES | 2008年 / 1778卷 / 7-8期
关键词
lamellar body; tubular myelin; collectin; saposin; membrane domain; raft; lipid phase; monolayer; membrane fusion; SP-A; SP-B; SP-C; air-liquid interface;
D O I
10.1016/j.bbamem.2008.05.003
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
The pulmonary surfactant system constitutes an excellent example of how dynamic membrane polymorphism governs some biological functions through specific lipid-lipid, lipid-protein and protein-protein interactions assembled in highly differentiated cells. Lipid-protein surfactant complexes are assembled in alveolar pneumocytes in the form of tightly packed membranes, which are stored in specialized organelles called lamellar bodies (LB). Upon secretion of LBs, surfactant develops a membrane-based network that covers rapidly and efficiently the whole respiratory surface. This membrane-based surface layer is organized in a way that permits efficient gas exchange while optimizing the encounter of many different molecules and cells at the epithelial surface, in a cross-talk essential to keep the whole organism safe from potential pathogenic invaders. The present review summarizes what is known about the structure of the different forms of surfactant, with special emphasis on current models of the molecular organization of surfactant membrane components. The architecture and the behaviour shown by surfactant structures in vivo are interpreted, to some extent, from the interactions and the properties exhibited by different surfactant models as they have been studied in vitro, particularly addressing the possible role played by surfactant proteins. However, the limitations in structural complexity and biophysical performance of surfactant preparations reconstituted in vitro will be highlighted in particular, to allow for a proper evaluation of the significance of the experimental model systems used so far to study structure-function relationships in surfactant, and to define future challenges in the design and production of more efficient clinical surfactants. (c) 2008 Elsevier B.V. All rights reserved.
引用
收藏
页码:1676 / 1695
页数:20
相关论文
共 194 条
[41]   Lateral phase separation in interfacial films of pulmonary surfactant [J].
Discher, BM ;
Maloney, KM ;
Schief, WR ;
Grainger, DW ;
Vogel, V ;
Hall, SB .
BIOPHYSICAL JOURNAL, 1996, 71 (05) :2583-2590
[42]   Lipid trafficking to the outer membrane of Gram-negative bacteria [J].
Doerrler, WT .
MOLECULAR MICROBIOLOGY, 2006, 60 (03) :542-552
[43]   RAT LUNG TYPE-II CELL AND LAMELLAR BODY - ELEMENTAL COMPOSITION INSITU [J].
ECKENHOFF, RG ;
SOMLYO, AP .
AMERICAN JOURNAL OF PHYSIOLOGY, 1988, 254 (05) :C614-C620
[44]   Structure of a truncated human surfactant protein D is less effective in agglutinating bacteria than the native structure and fails to inhibit haemagglutination by influenza A virus [J].
Eda, S ;
Suzuki, Y ;
Kawai, T ;
Ohtani, K ;
Kase, T ;
Fujinaga, Y ;
Sakamoto, T ;
Kurimura, T ;
Wakamiya, N .
BIOCHEMICAL JOURNAL, 1997, 323 :393-399
[45]   MINIMAL SURFACE-TENSION, SQUEEZE-OUT AND TRANSITION-TEMPERATURES OF BINARY-MIXTURES OF DIPALMITOYLPHOSPHATIDYLCHOLINE AND UNSATURATED PHOSPHOLIPIDS [J].
EGBERTS, J ;
SLOOT, H ;
MAZURE, A .
BIOCHIMICA ET BIOPHYSICA ACTA, 1989, 1002 (01) :109-113
[46]   Surfactant protein D increases phagocytosis and aggregation of pollen-allergen starch granules [J].
Erpenbeck, VJ ;
Malherbe, DC ;
Sommer, S ;
Schmiedl, A ;
Steinhilber, W ;
Ghio, AJ ;
Krug, N ;
Wright, JR ;
Hohlfeld, JM .
AMERICAN JOURNAL OF PHYSIOLOGY-LUNG CELLULAR AND MOLECULAR PHYSIOLOGY, 2005, 288 (04) :L692-L698
[47]   Lipid lateral diffusion in ordered and disordered phases in raft mixtures [J].
Filippov, A ;
Orädd, G ;
Lindblom, G .
BIOPHYSICAL JOURNAL, 2004, 86 (02) :891-896
[48]   Multilayers at the surface of solutions of exogenous lung surfactant: Direct observation by neutron reflection [J].
Follows, D. ;
Tiberg, F. ;
Thomas, R. K. ;
Larsson, M. .
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 2007, 1768 (02) :228-235
[49]   In vitro surfactant protein B deficiency inhibits lamellar body formation [J].
Foster, CD ;
Zhang, PX ;
Gonzales, LW ;
Guttentag, SH .
AMERICAN JOURNAL OF RESPIRATORY CELL AND MOLECULAR BIOLOGY, 2003, 29 (02) :259-266
[50]   Secretion in alveolar type II cells at the interface of constitutive and regulated exocytosis [J].
Frick, M ;
Eschertzhuber, S ;
Haller, T ;
Mair, N ;
Dietl, P .
AMERICAN JOURNAL OF RESPIRATORY CELL AND MOLECULAR BIOLOGY, 2001, 25 (03) :306-315