Dependence of the Differentiated State on the Cellular Environment: Modulation of Collagen Synthesis in Tendon Cells

In an adequate environment, primary avian tendon cells are capable of retaining both the full expression of differentiated function and a correct morphological orientation for 1 week in culture. At high density and in the presence of ascorbate, they are fully stabilized in that they devote 25-30% of...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1977-10, Vol.74 (10), p.4453-4457
Main Authors: Schwarz, Richard I., Bissell, Mina J.
Format: Article
Language:English
Subjects:
Animals
Ascorbic Acid - pharmacology
Cell culture techniques
Cell Differentiation - drug effects
Cell lines
Cells
Cells, Cultured
Cellular differentiation
Chick Embryo
Collagen - biosynthesis
Collagens
Cultured cells
Flasks
Lactates
Protein Biosynthesis
Sodium
Tendons
Tendons - cytology
Tendons - metabolism
Time Factors
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Summary:In an adequate environment, primary avian tendon cells are capable of retaining both the full expression of differentiated function and a correct morphological orientation for 1 week in culture. At high density and in the presence of ascorbate, they are fully stabilized in that they devote 25-30% of their total protein synthesis to collagen, a level comparable to that in tendon cells in ovo. However, either at low density or in medium without ascorbate, they synthesize collagen at only a third of this level. If plated on a collagen matrix, these cells will orient themselves in a manner similar to that of tendon cells in vivo. Furthermore, they are capable of fully modulating the percentage of collagen synthesis upon addition or removal of ascorbate and serum. The variation in the percentage of collagen produced is a result of alterations in collagen synthesis rather than of changes in total protein synthesis or hydroxylation of proline in collagen. Primary avian tendon cells, therefore, provide a suitable model for understanding the stability of the differentiated state, the mechanism of action of ascorbate, and the regulation of collagen biosynthesis.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.74.10.4453