|
|
||||||||
1 Department of Molecular
Biology and Genetics,
Pulmonary surfactant, a mixture of lipids and
surfactant proteins (SPs), plays an important role in respiration and
gas exchange. SP-A, the major SP, exists as an octadecamer that can
self-associate to form elongated protein filaments in vitro. We have
studied here the association of purified bovine SP-A with lipid vesicle bilayers in vitro with negative staining with uranyl acetate and transmission electron microscopy. Native bovine surfactant was also
examined by transmission electron microscopy of thinly sectioned embedded material. Lipid vesicles made from
dipalmitoylphosphatidylcholine and egg phosphatidylcholine (1:1
wt/wt) generally showed a smooth surface morphology, but some
large vesicles showed a corrugated one. On the smooth-surfaced
vesicles, SP-As primarily interacted in the form of separate
octadecamers or as multidirectional protein networks. On the surfaces
of the striated vesicles, SP-As primarily formed regularly spaced
unidirectional filaments. The mean spacing between adjacent striations
and between adjacent filaments was 49 nm. The striated surfaces were
not essential for the formation of filaments but appeared to stabilize
them. In native surfactant preparations, SP-A was detected in the dense
layers. This latter arrangement of the lipid bilayer-associated SP-As
supported the potential relevance of the in vitro structures to the in
vivo situation.
pulmonary surfactant; tubular myelin; lipid-protein interaction; membrane structure; ripple phase
This article has been cited by other articles:
![]() |
N. Palaniyar, R. A. Ridsdale, S. A. Hearn, F. Possmayer, and G. Harauz Formation of membrane lattice structures and their specific interactions with surfactant protein A Am J Physiol Lung Cell Mol Physiol, April 1, 1999; 276(4): L642 - L649. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| Visit Other APS Journals Online |