Ascorbate deficiency results in decreased collagen production: Under-hydroxylation of proline leads to increased intracellular degradation

Richard A. Berg, Beat Steinmann, Stephen I. Rennard, Ronald Crystal

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Collagen production by cultured human lung fibroblasts was examined when the cells were made deficient in ascorbate. Cells grown in the absence of ascorbate produced 30% less collagen during a 6-h labeling period than cells incubated with as little as 1 μg/ml ascorbate during the labeling period. Cells grown without ascorbate produced under-hydroxylated collagen which was subject to increased intracellular degradation from a basal level of 16% to an enhanced level of 49% of all newly synthesized collagen. The likely mechanism for increased intracellular degradation is the inability of under-hydroxylated collagen to assume a triple-helical conformation causing it to be susceptible to intracellular degradation. Measurement of collagen production by enzyme linked immunoassay (ELISA) using antibodies directed against triple-helical determinants of collagen showed that both types I and III collagens were affected. In contrast, another connective tissue component, fibronectin, was not affected. Analysis by ELISA showed a greater decrease in collagen production than did analysis by the collagenase method, suggesting that some non-helical collagen chains (detected by collagenase but not by ELISA) were secreted in the absence of ascorbate. These results provide a mechanism to account, in part, for the deficiency of collagen in connective tissues which occurs in a state of ascorbate deficiency.

Original languageEnglish
Pages (from-to)681-686
Number of pages6
JournalArchives of Biochemistry and Biophysics
Issue number2
Publication statusPublished - 15 Oct 1983
Externally publishedYes


ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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