Influence of zinc deficiency on synthesis and cross-linking of rat skin collagen

Abstract

1. (1) The yield of salt-soluble collagen was significantly reduced in zinc-deficient rats, while the acid-soluble fraction was increased by approximately 20%. 2. (2) The incorporation of [2- 14C]glycine into the α 1 and α 2 chains and of L-[U- 14C]proline into the salt-soluble collagen fractions was reduced 30–50% in the zinc-deficient animals. 3. (3) The incorporation of [ Me- 3H]thymidine into skin DNA was 60–80% lower than that from zinc-supplemented animals. 4. (4) Muscle collagen synthesis per mg polyribosomal RNA was approximately the same in both groups. The polysome yield and consequently total muscle collagen synthetic activity per 100 g muscle was, however, 30% lower in the animals on a zinc-deficient diet. 5. (5) The content of β-dimers in the salt-soluble collagen from zinc-deficient skins was 1 3 higher than that from the control. No difference in β-subunits from the acid-soluble fraction was apparent. 6. (6) The aldehyde content of the salt-soluble collagen was markedly higher and that from insoluble collagen lower in the zinc-deficient group.