Three-Dimensional Reconstruction of Tubular Myelin

Abstract

The lipid and protein components of pulmonary surfactant are synthesized by alveolar type II cells and stored in their secretory granules, the lamellar bodies. Tubular myelin is a highly ordered surfactant structure that is lung specific and produced in the alveolar airspace. Recent work identified Ca²⁺, surfactant apoproteins A and B, and saturated phospholipids as necessary for tubular myelin structure and function. We have used serial ultrathin sections from fetal rat lungs and reconstructed the three-dimensional structure of tubular myelin. The spheres of tubular myelin we viewed were 2-3 ixm in diameter and were surrounded by up to 20 lamellar bodies, each apparently simultaneously contributing material to the tubules. We measured a long-range symmetry of the tubules, which were folded about a central axis and showed a repeated crossing of invididual tubes from one side to the other of the large structure. The tubes appeared closed on their outer edges and there was a delay in the penetration of tubules by cationic ferritin added to tissue slices containing the tubular myelin, although within a few minutes tracer appeared in the lumina and on the walls of the tubules. The three-dimensional images were compatible with existing views of tubular myelin.