Collagen activates superoxide anion production by human polymorphonuclear neutrophils

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Abstract
Human polymorphonuclear neutrophils (PMNs), purified on Ficoll-Hypaque cushions, were incubated for 5 min with calf skin acid-soluble collagen and the released superoxide anions (O2-) measured spectrophotometrically by reduction of ferricytochrome c or by chemiluminescence analysis. This collagen stimulated the release of O2- unless it had been treated with pepsin. The stimulatory activity remained in denatured collagen, was contained only in the .alpha.1(I) chain and was present in the .alpha.1(I)-CB 6(CNBr-cleaved) peptide, which is C-terminal. The activity was linearly dependent on the collagen concentration up to about 200 .mu.g/ml. In addition, this collagen induced a release of .beta.-glucuronidase and N-acetyl-.beta.-glucosaminidase from PMNs.