Influence of ascorbic acid on ribosomal patterns and collagen biosynthesis in healing wounds of scorbutic guinea pigs
- 1 September 1974
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 142 (3) , 641-651
- https://doi.org/10.1042/bj1420641
Abstract
Scorbutic guinea pigs were wounded and the influence of administering ascorbic acid 6 days later was studied with respect to cellular morphology, ribosomal distribution and protein synthesis. Electron-microscopic studies revealed that the dilated endoplasmic reticulum observed in the fibroblasts of scorbutic wound tissue had reverted to a normal configuration 24h after intraperitoneal injection of 100mg of ascorbate. Quantitative determination of the distribution of free and membrane-bound ribosomes indicated a significant increase in membrane-bound ribosomes in wound tissue from ascorbate-supplemented (recovery) animals. Sucrose-density-gradient centrifugation indicated a significant increase in the proportion of large membrane-bound polyribosomes in the range 300–350S and a concomitant decrease in 80S monoribosomes in the ribosome sedimentation profile of recovery tissue. Determination of the synthesis of non-diffusible [3H]hydroxyproline in scorbutic and recovery wounds showed a 3–4-fold stimulation in peptidyl-proline hydroxylation in recovery tissues. Studies carried out in which scorbutic and recovery tissues were incubated with [14C]leucine indicated that general protein synthesis, as measured by14C incorporated into non-diffusible material/μg of DNA, was unaltered by ascorbate supplementation. Similar studies of [3H]proline incorporation suggested that in recovery tissues there was a small but significant increase in [3H]proline incorporated/μg of DNA, which probably represents an increase in protocollagen synthesis. This observation correlates well with the increase seen in recovery tissues of large polyribosomes on which collagen precursor polypeptides are known to be synthesized. Preliminary characterization of the repair collagen synthesized by recovery animals showed it to be a typical Type I collagen having the chain composition (α1)2α2. The extent of glycosylation of the hydroxylysine of the newly synthesized collagen was greater than that reported for either normal guinea-pig dermal collagen or dermal scar collagen.Keywords
This publication has 54 references indexed in Scilit:
- The thermal transition of a non-hydroxylated form of collagen. Evidence for a role for hydroxyproline in stabilizing the triple-helix of collagenPublished by Elsevier ,2004
- Rate of helix formation by intracellular procollagen and protocollagen. Evidence for a role for disulfide bonsBiochemical and Biophysical Research Communications, 1973
- Association of prolyl hydroxylase activity with membranesBiochemical and Biophysical Research Communications, 1973
- Hydroxyproline stabilizes the triple helix of chick tendon collagenBiochemical and Biophysical Research Communications, 1973
- A comparison between the reducible intermolecular crosslinks of the collagens from mature dermis and young dermal scar tissue of the guinea pigBiochemical and Biophysical Research Communications, 1972
- Collagen polysomes: Site of hydroxylation of proline residuesJournal of Molecular Biology, 1971
- Studies on free and membrane-bound ribosomes in rat liverJournal of Molecular Biology, 1967
- WOUND HEALING AND COLLAGEN FORMATIONThe Journal of cell biology, 1962
- An electron optical study of experimental scurvyJournal of Ultrastructure Research, 1962
- The precision of ultraviolet absorption measurements in the Schmidt-Thannhauser procedure for nucleic acid estimationBiochimica et Biophysica Acta, 1962