A novel cleavage product of beta-thromboglobulin formed in cultures of stimulated mononuclear cells activates human neutrophils.
A neutrophil-activating peptide, NAP-2, was found to be produced in cultures of human mononuclear cells in the presence of E. coli lipopolysaccharide or phytohaemagglutinin. NAP-2 induced the release of elastase from cytochalasin B-treated human neutrophils. Amino- and carboxy-terminal sequencing and electrophoretic analysis showed that NAP-2 is a single peptide of 70 amino acids (Mr 7,628, IEP 8.7) corresponding to a carboxyterminal fragment of beta-thromboglobulin. NAP-2 is homologous to NAF/NAP-1. When aligned on the basis of their two first cysteines, 13 out of 20 amino-terminal residues are identical. The overall homology between the two peptides is 46%.
Walz
A
A
Theodor-Kocher-Institut, University of Bern, Switzerland.
Baggiolini
M
M
D000595:Amino Acid Sequence; D002478:Cells, Cultured; D006801:Humans; D008969:Molecular Sequence Data; D009000:Monocytes / Q000378:metabolism*; D009504:Neutrophils / Q000502:physiology*; D010446:Peptide Fragments / Q000302:isolation & purification; D001620:beta-Thromboglobulin / Q000378:metabolism*
D010446:Peptide Fragments; D001620:beta-Thromboglobulin