Collagen activates superoxide anion production by human polymorphonuclear neutrophils.
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.
Monboisse
J C
JC
Laboratory of Biochemistry, CNRS UA 610, UFR Medicine, Reims, France.
Bellon
G
G
Dufer
J
J
Randoux
A
A
Borel
J P
JP
D002118:Calcium / Q000494:pharmacology; D003094:Collagen / Q000494:pharmacology*; D003574:Cytochrome c Group / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D066298:In Vitro Techniques; D009504:Neutrophils / Q000187:drug effects / Q000201:enzymology / Q000378:metabolism*; D010446:Peptide Fragments / Q000032:analysis; D013268:Stimulation, Chemical; D013481:Superoxides / Q000097:blood*
D003574:Cytochrome c Group; D010446:Peptide Fragments; D013481:Superoxides; D003094:Collagen; D002118:Calcium