Collagen activates superoxide anion production by human polymorphonuclear neutrophils. |
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| Authors: | J C Monboisse G Bellon J Dufer A Randoux J P Borel |
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| Affiliation: | Laboratory of Biochemistry, CNRS UA 610, UFR Medicine, Reims, France. |
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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 micrograms/ml. In addition, this collagen induced a release of beta-glucuronidase and N-acetyl-beta-glucosaminidase from PMNs. |
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