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Three‐dimensional structure of lung elastin demonstrated by scanning electron microscopy/stereo‐pair images
Author(s) -
O'Donnell M. D.,
Cottell D. C.,
McGeeney K. F.
Publication year - 1994
Publication title -
microscopy research and technique
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.536
H-Index - 118
eISSN - 1097-0029
pISSN - 1059-910X
DOI - 10.1002/jemt.1070290312
Subject(s) - elastin , scanning electron microscope , electron microscope , microscopy , materials science , lung , biophysics , chemistry , optics , pathology , biology , physics , medicine , composite material
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). Forme 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. © 1994 Wiley‐Liss, Inc.