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
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...
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Published in | Cytokine (Philadelphia, Pa.) Vol. 6; no. 2; pp. 124 - 134 |
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Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
Published |
England
Elsevier Ltd
01.03.1994
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Abstract | 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-leucyl-L-phenylalanine (fMLP). The huMIP-2 peptides were the least potent cytokine tested in triggering neutrophil degranulation. They were also less potent neutrophil chemotaxins than fMLP or huIL-8. However, they were more effective than NAP-2 in stimulating chemotaxis of neutrophils. The binding studies showed that huMIP-2 peptides could interact with specific receptors on human blood neutrophils. Moreover, huMIP-2 peptides competed for up to 60% of the huIL-8 binding sites on neutrophils whereas huIL-8 competed for almost 100% of either of the huMIP-2 peptide binding sites. These data suggest the huMIP-2 peptides have little or no affinity for 40% of the huIL-8 receptors. In addition, detectable amounts of mRNA for huMIP-2α were found in samples from human alveolar macrophages stimulated with
Staphylococcus aureus, toxic shock syndrome toxin-1 (TSST), but not in samples stimulated with
S. aureus enterotoxin A (SEA) or
Escherichia coli endotoxin (lipopolysaccharide = LPS). In conclusion, huMIP-2α and β are weak neutrophil stimulating agents, which may increase inflammation in diseases such as toxic shock syndrome. |
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AbstractList | 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-leucyl-L-phenylalanine (fMLP). The huMIP-2 peptides were the least potent cytokine tested in triggering neutrophil degranulation. They were also less potent neutrophil chemotaxins than fMLP or huIL-8. However, they were more effective than NAP-2 in stimulating chemotaxis of neutrophils. The binding studies showed that huMIP-2 peptides could interact with specific receptors on human blood neutrophils. Moreover, huMIP-2 peptides competed for up to 60% of the huIL-8 binding sites on neutrophils whereas huIL-8 competed for almost 100% of either of the huMIP-2 peptide binding sites. These data suggest the huMIP-2 peptides have little or no affinity for 40% of the huIL-8 receptors. In addition, detectable amounts of mRNA for huMIP-2α were found in samples from human alveolar macrophages stimulated with
Staphylococcus aureus, toxic shock syndrome toxin-1 (TSST), but not in samples stimulated with
S. aureus enterotoxin A (SEA) or
Escherichia coli endotoxin (lipopolysaccharide = LPS). In conclusion, huMIP-2α and β are weak neutrophil stimulating agents, which may increase inflammation in diseases such as toxic shock syndrome. We examined the biological and kinetic characteristics of two new members of the intercrine family of cytokines. Human macrophage inflammatory peptides 2 alpha and beta (huMIP-2 alpha and beta) were compared to human interleukin 8 (huIL-8), neutrophil activating peptide 2 (huNAP-2), and N-formyl-L-methionyl-L-phenylalanine (fMLP). The huMIP-2 peptides were the least potent cytokine tested in triggering neutrophil degranulation. They were also less potent neutrophil chemotaxins than fMLP or huIL-8. However, they were more effective than NAP-2 in stimulating chemotaxis of neutrophils. The binding studies showed that huMIP-2 peptides could interact with specific receptors on human blood neutrophils. Moreover, huMIP-2 peptides competed for up to 60% of the huIL-8 binding sites on neutrophils whereas huIL-8 competed for almost 100% of either of the huMIP-2 peptide binding sites. These data suggest the huMIP-2 peptides have little or no affinity for 40% of the huIL-8 receptors. In addition, detectable amounts of mRNA for huMIP-2 alpha were found in samples from human alveolar macrophages stimulated with Staphylococcus aureus, toxic shock syndrome toxin-1 (TSST), but not in samples stimulated with S. aureus enterotoxin A (SEA) or Escherichia coli endotoxin (lipopolysaccharide = LPS). In conclusion, huMIP-2 alpha and beta are weak neutrophil stimulating agents, which may increase inflammation in diseases such as toxic shock syndrome. |
Author | Stevens, Michael D. Miller, Edmund J. Kurdowska, Anna Tekamp-Olson, Patricia Mullenbach, Guy Carr, Ferdicia K. Cohen, Allen B. |
Author_xml | – sequence: 1 givenname: Anna surname: Kurdowska fullname: Kurdowska, Anna organization: Department of Biochemistry at The University of Texas Health Center at Tyler, USA – sequence: 2 givenname: Allen B. surname: Cohen fullname: Cohen, Allen B. organization: Department of Biochemistry at The University of Texas Health Center at Tyler, USA – sequence: 3 givenname: Ferdicia K. surname: Carr fullname: Carr, Ferdicia K. organization: Department of Biochemistry at The University of Texas Health Center at Tyler, USA – sequence: 4 givenname: Michael D. surname: Stevens fullname: Stevens, Michael D. organization: Department of Biochemistry at The University of Texas Health Center at Tyler, USA – sequence: 5 givenname: Edmund J. surname: Miller fullname: Miller, Edmund J. organization: Department of Biochemistry at The University of Texas Health Center at Tyler, USA – sequence: 6 givenname: Guy surname: Mullenbach fullname: Mullenbach, Guy organization: Chiron Corp., Emeryville, CA, USA – sequence: 7 givenname: Patricia surname: Tekamp-Olson fullname: Tekamp-Olson, Patricia organization: Chiron Corp., Emeryville, CA, USA |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/8031995$$D View this record in MEDLINE/PubMed |
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Keywords | Intercrine Inflammation Chemotaxis Macrophage Inflammatory Peptide Cytokine |
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Snippet | We examined the biological and kinetic characteristics of two new members of the intercrine family of cytokines. Human macrophage inflammatory peptides 2 α and... We examined the biological and kinetic characteristics of two new members of the intercrine family of cytokines. Human macrophage inflammatory peptides 2 alpha... |
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SubjectTerms | 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 |
Title | 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 |
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