Three-dimensional structure of lung elastin demonstrated by scanning electron microscopy/stereo-pair images.
The aim of this study was to expose the inflated 3-D structure of lung elastin. Formic acid digestion followed by freeze-drying unveiled the lamellar framework. The 3-D structure of elastin was well preserved within the alveolar septa and ducts, as demonstrated by scanning electron microscopy/stereo-pair photography. Elastin fibers are seen in the alveolar septa, which are continuous with the lamellae. The removal of collagen fibers and cells by formic acid was visualised as a function of time: The optimum was 48 hours. Transverse sections still retained some collagen fibrils and partially digested cells in addition to elastin as shown by transmission electron microscopy (TEM). Formic acid digestion followed by critical point drying caused damage to the lamellar structures and they appeared to collapse. Sodium hydroxide digestion combined with freeze-drying did not preserve the 3-D lamellar structure of elastin, but converted it into flat ribbonlike bands. The main structures remaining following alkali treatment were identified by TEM as collagen fibrils well preserved in their original locations.
Department of Medicine and Therapeutics, University College Dublin, Belfield, Ireland.
M D
MD
O'Donnell
D C
DC
Cottell
K F
KF
McGeeney
D000818:Animals; D003094:Collagen / Q000032:analysis / Q000648:ultrastructure; D004549:Elastin / Q000032:analysis* / Q000648:ultrastructure*; D008168:Lung / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D008297:Male; D008854:Microscopy, Electron / Q000379:methods; D008855:Microscopy, Electron, Scanning / Q000379:methods; D051381:Rats; D017207:Rats, Sprague-Dawley
D003094:Collagen; D004549:Elastin