Biological and kinetic characterization of recombinant human macrophage inflammatory peptides 2 alpha and beta and comparison with the neutrophil activating peptide 2 and interleukin 8

• Published in: Cytokine (Philadelphia, Pa.) Vol. 6; no. 2; pp. 124 - 134
• Main Authors: Kurdowska, Anna, Cohen, Allen B., Carr, Ferdicia K., Stevens, Michael D., Miller, Edmund J., Mullenbach, Guy, Tekamp-Olson, Patricia
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 01.03.1994
• Subjects: Bacterial Toxins; Base Sequence; Binding Sites; Blotting, Southern; Cells, Cultured; Chemokine CXCL2; Chemotaxis; Chemotaxis, Leukocyte - drug effects; Cytokine; Cytokines - biosynthesis; Cytokines - metabolism; Cytokines - pharmacology; DNA Primers; Enterotoxins - pharmacology; Escherichia coli; Humans; Inflammation; Intercrine; Interleukin-8 - metabolism; Interleukin-8 - pharmacology; Kinetics; Leukocyte Elastase; Lipopolysaccharides - pharmacology; Macrophage Inflammatory Peptide; Macrophages, Alveolar - drug effects; Macrophages, Alveolar - physiology; Molecular Sequence Data; Monokines - biosynthesis; Monokines - metabolism; Monokines - pharmacology; N-Formylmethionine Leucyl-Phenylalanine - pharmacology; Neutrophils - drug effects; Neutrophils - enzymology; Neutrophils - physiology; Pancreatic Elastase - blood; Peroxidase - blood; Polymerase Chain Reaction; Recombinant Proteins - pharmacology; RNA, Messenger - analysis; RNA, Messenger - biosynthesis; Staphylococcus aureus; Superantigens; Intercrine; Inflammation; Chemotaxis; Macrophage Inflammatory Peptide; Cytokine

We examined the biological and kinetic characteristics of two new members of the intercrine family of cytokines. Human macrophage inflammatory peptides 2 α and β (huMIP-2α and β) were compared to human interleukin 8 (huIL-8), neutrophil activating peptide 2 (huNAP-2), and N-formyl-L-methionyl-L-leuc...