Interaction of Eglin c with polymorphonuclear cells: evidence for binding to the cell surface.
The interaction of Eglin c with human polymorphonuclear cells was investigated in order to explain the effect of this (and other) proteinase inhibitor(s) on the biological activities of neutrophils. We have identified binding sites on human neutrophils by using [3H]Eglin. Binding is rapid and reversible at 5 degrees C. There are approximately 100,000 binding sites per cell, with an equilibrium dissociation constant of 0.2microM. Eglin binding was not inhibited by other proteinase inhibitors (alpha 1-PI, PhCH2SO2F, Tos-Phe-CH2Cl), and was enhanced four-fold by the chemotactic peptide fMet-Leu-Phe. The results indicate that Eglin c, a peptide proteinase inhibitor, is able to bind to human PMN cells and that this initial interaction does not involve a known proteinase such as cathepsin G or elastase.
D056649:Cathepsin G; D002403:Cathepsins / Q000494:pharmacology; D002918:Chymotrypsin / Q000037:antagonists & inhibitors; D006801:Humans; D007700:Kinetics; D009240:N-Formylmethionine Leucyl-Phenylalanine / Q000494:pharmacology; D009504:Neutrophils / Q000187:drug effects* / Q000378:metabolism; D011480:Protease Inhibitors / Q000378:metabolism / Q000494:pharmacology*; D011485:Protein Binding; D011506:Proteins / Q000378:metabolism / Q000494:pharmacology*; D012697:Serine Endopeptidases; D015843:Serpins
D011480:Protease Inhibitors; D011506:Proteins; D015843:Serpins; C028656:eglin proteinase inhibitors; D009240:N-Formylmethionine Leucyl-Phenylalanine; D002403:Cathepsins; D012697:Serine Endopeptidases; D002918:Chymotrypsin; C534094:CTSG protein, human; D056649:Cathepsin G