Abstract
The structural heterogeneity of rabbit lung collagen was examined by extracting labeled collagen from short-term cultures of lung minces with 1 M NaCl-50 mM Tris.HCl (pH 7.4), 0.5 M acetic acid, or 0.4 ionic strength phosphate buffer. The extracted collagens were purified by carboxymethyl-cellulose chromatography, and their cyanogen bromide peptides were mapped by ion exchange chromatography and acrylamide gels. Rabbit skin alpha1(I) and alpha2 chains and rabbit sternal cartilage alpha1(II) chains were used as markers. The peripheral lung, containing alveoli, small blood vessels, and small airways, synthesized alpha1(I) and alpha2 chains. The trachea and the bronchial tree (first through seventh order branches) both synthesized alpha1(II) chains. Lung alpha1(I), alpha2, and alpha1(II) chains all have a molecular weight of about 100,000 and are all sensitive to Clostridial collagenase. The extraction and purification methods used isolate only 50% of the collagen synthesized by these structures in vitro. Once all collagen types in lung can be described and quantitated, it should be possible to utilize lung collagen types as biochemical markers to study normal lung development and to define the lung fibrotic diseases.