Effect of protein malnutrition on the crosslinking of dermal collagen in aging.
The effect of protein malnutrition on collagen crosslinking was studied in different age groups of rats. The percent of reversibility of neutral salt-soluble collagen gel and the susceptibility of insoluble collagen to denaturing agents and pronase decreased with aging. The electrophoretic pattern of neutral salt-soluble collagen on sodium dodecyl sulphate polyacrylamide gels showed a decrease of alpha 1 and alpha 2 subunits and an increase of beta-components, resulting in a decrease of alpha/beta ratio in aging. There was a significant decrease in the aldehyde content of neutral salt-soluble collagen during age. Protein deficiency was found to impair the crosslinking and the effect was greater in younger animals than in older ones.
D000367:Age Factors; D000818:Animals; D003094:Collagen / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D011502:Protein-Energy Malnutrition / Q000378:metabolism*; D051381:Rats; D012867:Skin / Q000378:metabolism*; D012995:Solubility
D003094:Collagen