Production of Procollagen by Human Fibroblasts in Culture
- 1 November 1972
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 69 (11), 3260-3262
- https://doi.org/10.1073/pnas.69.11.3260
Abstract
Three hydroxyproline-containing proteins secreted into the medium by human fibroblasts in culture were isolated and characterized. A minor fraction was identical to the collagen monomer. The major fraction was a form of procollagen, which contained, in addition to pro alpha and alpha chains, a component estimated to have a molecular weight of 250,000. This component was a dimer of pro alpha chains joined by disulfide bonds. The third fraction, much lower in hydroxyproline and hydroxylysine content, was of still greater size. Pro alpha chains were released upon denaturation and reduction, indicating that this fraction may contain pro alpha chains linked by disulfide bonds to noncollagenous material.Keywords
This publication has 15 references indexed in Scilit:
- Collagen synthesis by cells II: Secretion of a disulfide linked materialBiochemical and Biophysical Research Communications, 1972
- A Transport Form of Collagen from Embryonic Tendon: Electron Microscopic Demonstration of an NH 2 -Terminal Extension and Evidence Suggesting the Presence of Cystine in the MoleculeProceedings of the National Academy of Sciences, 1972
- Collagen Biosynthesis: Synthesis and Secretion of a High Molecular Weight Collagen Precursor (Procollagen)Proceedings of the National Academy of Sciences, 1971
- Further evidence for a transport form of collagen. Its extrusion and extracellular conversion to tropocollagen in embryonic tendonFEBS Letters, 1971
- Studies on protocollagen: Identification of a precursor of proto α1Biochemical and Biophysical Research Communications, 1971
- Inhibition of proline and lysine hydroxylation prevents normal extrusion of collagen by 3T6 fibroblasts in cultureFEBS Letters, 1971
- Evidence for Procollagen, a Biosynthetic Precursor of CollagenProceedings of the National Academy of Sciences, 1971
- The Nature of the Collagen Synthesized by Cultured Human FibroblastsProceedings of the National Academy of Sciences, 1971
- Molecular weight determination of random coil polypeptides from collagen by molecular sieve chromatographyAnalytical Biochemistry, 1968
- Continuous scintillation counting of carbon-14 and tritium in effluent of the automatic amino acid analyzerAnalytical Biochemistry, 1962