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 α1(I) and α2 chains and rabbit sternal cartilage α1(II) chains were used as markers. The peripheral lung, containing alveoli, small blood vessels, and small airways, synthesized α1(I) and α2 chains. The trachea and the bronchial tree (first through seventh order branches) both synthesized α1(II) chains. Lung α1(I), α2, and α1(II) chains all have a mol wt 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.
|Number of pages||5|
|Journal||Proceedings of the National Academy of Sciences of the United States of America|
|Publication status||Published - 1 Jan 1974|
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