Abstract
Activated neutrophils secrete two forms of IL-8 with 77 and 72 amino acids, IL-8(77) and IL-8(72), along with proteinases that could process these cytokines. Significant conversion of IL-8(77) to more potent, N-terminally truncated forms was observed upon incubation with neutrophil granule lysates and purified proteinase-3. IL-8(72) was considerably more resistant to proteolytic processing than IL-8(77). The present observations indicate that neutrophil proteinases released in inflamed tissues convert IL-8 to more active forms and therefore tend to conserve or enhance, rather than decrease IL-8 activity.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Cathepsin G
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Cathepsins / metabolism*
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Chemokine CXCL1
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Chemokines, CXC*
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Chemotactic Factors / metabolism
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Chymotrypsin / metabolism
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Extracellular Matrix Proteins / metabolism
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Growth Substances / metabolism
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Humans
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Intercellular Signaling Peptides and Proteins*
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Interleukin-8 / analogs & derivatives
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Interleukin-8 / chemical synthesis
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Interleukin-8 / genetics
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Interleukin-8 / metabolism*
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Leukocyte Elastase
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Molecular Sequence Data
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Myeloblastin
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Neutrophil Activation*
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Neutrophils / metabolism*
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Pancreatic Elastase / metabolism*
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Peptides / metabolism
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Protein Structure, Tertiary
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Serine Endopeptidases / metabolism*
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Trypsin / metabolism
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beta-Thromboglobulin
Substances
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CXCL1 protein, human
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Chemokine CXCL1
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Chemokines, CXC
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Chemotactic Factors
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Extracellular Matrix Proteins
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Growth Substances
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Intercellular Signaling Peptides and Proteins
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Interleukin-8
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PPBP protein, human
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Peptides
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beta-Thromboglobulin
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connective tissue-activating peptide
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Cathepsins
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Serine Endopeptidases
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Chymotrypsin
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CTSG protein, human
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Cathepsin G
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Pancreatic Elastase
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Leukocyte Elastase
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Trypsin
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Myeloblastin