Elastin metabolism during recovery from impaired crosslink formation.
Accelerated proteolysis of tropoelastin and elastin occurs in the arteries of chicks rendered nutritionally copper-deficient. The process results in part from decreased elastin crosslinking. Repletion of copper-deficient chicks with copper causes a deposition of elastin that is proteinase resistant. Resistance to proteolysis is conferred within 48 h of dietary copper repletion. Deposition of aorta elastin to near normal values occurs after 3-4 days in copper-repleted chicks. Moreover, elastolysis was enhanced when the content of dehydrolysinonorleucine in elastin was abnormally low. The chemical modification of lysyl residue in elastin by citroconylation, however, did not influence the rate of elastolysis. We have shown previously that tropoelastin messenger RNA activity and synthesis are not influenced by dietary copper deprivation (1986, Biochem. J. 236, 17-23). Rather, as demonstrated herein, the decrease in elastin content in arteries of copper-deficient birds appears to be more the result of enhanced degradation. Restoration of normal crosslinking restores deposition and imparts resistance to elastolysis. Moreover, serum appears to be a good source of elastolytic proteinases when the elastin substrate is partially or abnormally crosslinked.
Tinker
D
D
Department of Nutrition, College of Agriculture and Environmental Sciences, University of California, Davis 95616.
Romero-Chapman
N
N
Reiser
K
K
Hyde
D
D
Rucker
R
R
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001013:Aorta, Thoracic / Q000378:metabolism; D002645:Chickens; D003300:Copper / Q000378:metabolism; D003432:Cross-Linking Reagents; D004549:Elastin / Q000378:metabolism*; D006868:Hydrolysis; D009924:Organ Culture Techniques; D012995:Solubility; D014633:Valine / Q000378:metabolism
D000596:Amino Acids; D003432:Cross-Linking Reagents; D003300:Copper; D004549:Elastin; D014633:Valine