Culture of alveolar epithelial Type II cells isolated from adult rat lung

1983 ◽  
Vol 8 (2) ◽  
pp. 53-58
Author(s):  
Robert D. Greenleaf
FEBS Letters ◽  
1982 ◽  
Vol 147 (2) ◽  
pp. 171-174 ◽  
Author(s):  
J.J. Batenburg ◽  
W. Klazinga ◽  
L.M.G. van Golde

Author(s):  
Martin Post ◽  
Joseph J. Batenburg ◽  
Elisabeth A.J.M. Schuurmans ◽  
Lambert M.G. Van Golde

1990 ◽  
Vol 38 (2) ◽  
pp. 233-244 ◽  
Author(s):  
D J Taatjes ◽  
L A Barcomb ◽  
K O Leslie ◽  
R B Low

We used post-embedding cytochemical techniques to investigate the lectin binding profiles of rat lung alveolar epithelial cells. Sections from rat lung embedded in the hydrophilic resin Lowicryl K4M were incubated either directly with a lectin-gold complex or with an unlabeled lectin followed by a specific glycoprotein-gold complex. The binding patterns of the five lectins used could be divided into three categories according to their reactivity with alveolar epithelial cells: (a) the Limax flavus lectin and Ricinus communis I lectin bound to both type I and type II cell plasma membranes; (b) the Helix pomatia lectin and Sambucus nigra L. lectin bound to type II but not type I cells; and (c) the Erythrina cristagalli lectin reacted with type I cells but was unreactive with type II cells. The specificity of staining was assessed by control experiments, including pre-absorption of the lectins with various oligosaccharides and enzymatic pre-treatment of sections with highly purified glycosidases to remove specific sugar residues. The results demonstrate that these lectins can be used to distinguish between type I and type II cells and would therefore be useful probes for investigating cell dynamics during lung development and remodeling.


Author(s):  
Ellen C. Heesbeen ◽  
Gert Rijksen ◽  
Joseph J. Batenburg ◽  
Lambert M.G. van Golde ◽  
Gerard E.J. Staal

1981 ◽  
Vol 29 (2) ◽  
pp. 291-305 ◽  
Author(s):  
M C Williams ◽  
B J Benson

We investigated the cellular and subcellular sites of metabolism of the 72,000 dalton protein of pulmonary surfactant in order to provide insights into mechanisms of synthesis, intracellular assembly, and intraalveolar metabolism of this phospholipid-rich secretory product. Surfactant (approximately 90% lipid, 10% protein by weight) was purified by density gradient centrifugation of material obtained by lavaging rat lungs. The purified material was used to generate an antiserum from which a specific antibody was obtained by affinity chromatography. A horseradish peroxidase-labeled Fab was used to localize the antigen in rat lung. The antibody labeled the rough endoplasmic reticulum and Golgi apparatus of type II cells only. Some multivesicular bodies in type II cells were also labeled, but whether the antigen was present in lamellar bodies was uncertain. Phagosomes of alveolar macrophages were labeled as were similar inclusions in type I cells. Using indirect immunocytochemistry we determined that the labeling of alveolar cell surfaces does not represent the presence of a continuous layer of secreted surfactant. These results suggest that only the type II cell synthesizes surfactant protein and than mainly alveolar macrophages participate in its catabolism. The initial intracellular site of the association of protein with lipid may be multivesicular bodies as suggested previously by others.


1985 ◽  
Vol 9 (1-2) ◽  
pp. 67-84 ◽  
Author(s):  
Henk P. Haagsman ◽  
Els A. J. M. Schuurmans ◽  
Gerrit M. Alink ◽  
Joseph J. Batenburg ◽  
Lambert M. G. van Golde

Author(s):  
Martin Post ◽  
Els A.J.M. Schuurmans ◽  
Joseph J. Batenburg ◽  
Lambert M.G. Van Golde

1988 ◽  
Vol 14 (1) ◽  
pp. 1-17 ◽  
Author(s):  
Henk P. Haagsman ◽  
Els A. J. M. Schuurmans ◽  
Joseph J. Batenburg ◽  
Lambert M. G. Van Golde

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