Skin lysyl oxidase activity is not rate limiting for collagen crosslinking in the glucocorticoid-treated rat.
Lysyl oxidase activity in the skin of rats receiving triamcinolone diacetate (12 mg/kg) for three consecutive days was decreased by sixty-four percent as compared to control values. A decrease of lysyl oxidase activity was observed twelve hours after the initial glucocorticoid injection. The decreased lysyl oxidase activity was accompanied by a forty-nine percent decrease of acetic acid extractable collagen. There was also a forty-two percent decrease in the alpha/beta ratio of the acetic acid soluble skin collagen of glucocorticoid-treated animals. These data indicate that although skin lysyl oxidase activity is decreased by glucocorticoid treatment, the crosslinking of acid extracted collagen as measured by the alpha/beta ratio and collagen solubility is increased. Accordingly lysyl oxidase activity is not rate limiting for collagen crosslink formation in the skins of rats treated with glucocorticoids.
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D000085:Acetates; D019342:Acetic Acid; D000594:Amino Acid Oxidoreductases / Q000378:metabolism*; D000818:Animals; D000831:Animals, Newborn / Q000378:metabolism; D003094:Collagen / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; D011499:Protein Processing, Post-Translational; D008249:Protein-Lysine 6-Oxidase / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D012867:Skin / Q000187:drug effects / Q000201:enzymology*; D012995:Solubility; D014221:Triamcinolone / Q000031:analogs & derivatives* / Q000494:pharmacology
D000085:Acetates; D014221:Triamcinolone; D003094:Collagen; C030262:triamcinolone diacetate; D000594:Amino Acid Oxidoreductases; D008249:Protein-Lysine 6-Oxidase; D019342:Acetic Acid