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. 1987 Sep 15;246(3):599–603. doi: 10.1042/bj2460599

Collagen activates superoxide anion production by human polymorphonuclear neutrophils.

J C Monboisse 1, G Bellon 1, J Dufer 1, A Randoux 1, J P Borel 1
PMCID: PMC1148322  PMID: 2825644

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 micrograms/ml. In addition, this collagen induced a release of beta-glucuronidase and N-acetyl-beta-glucosaminidase from PMNs.

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Selected References

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