Selective inhibition of human diploid fibroblast collagen synthesis by interferons

J Clin Invest. 1984 Sep;74(3):1112-6. doi: 10.1172/JCI111480.


The effects of alpha- and gamma-interferons (IFNs) on collagen production by confluent human diploid fibroblasts in culture were examined. It was found that partially purified alpha-IFNs and affinity purified gamma-IFNs caused greater than 50% inhibition of collagen synthesis by these cells independently of their effect on cell proliferation. Recombinant alpha-IFNs showed a similar effect (38.8% inhibition), indicating that collagen synthesis inhibition was a constitutive property of IFNs. Collagen synthesis inhibition by IFNs was concentration dependent. Gel filtration chromatography of the newly synthesized proteins from the media of fibroblasts incubated with partially purified alpha-IFNs demonstrated a selective depression of molecules eluting in the region of procollagen. No detectable increase in collagen degradation products or underhydroxylation of procollagen was observed. Short-term kinetic studies further demonstrated that the major effect of IFNs was due to a net decrease in fibroblast collagen production rather than to impairment of secretion or increased extracellular degradation of the newly synthesized molecules. These results indicate that alpha- and gamma-IFNs are potent inhibitors of human fibroblast collagen production and suggest that they may play an important role in the regulation of normal and pathologic fibrogenesis.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Carbon Radioisotopes
  • Cells, Cultured
  • Collagen / biosynthesis*
  • Fibroblasts / drug effects
  • Fibroblasts / metabolism
  • Humans
  • Hydroxyproline / biosynthesis
  • Interferon Type I / pharmacology*
  • Interferon-gamma / pharmacology*
  • Kinetics
  • Proline / metabolism
  • Protein Biosynthesis
  • Proteins / isolation & purification
  • Skin / metabolism


  • Carbon Radioisotopes
  • Interferon Type I
  • Proteins
  • Interferon-gamma
  • Collagen
  • Proline
  • Hydroxyproline