Extracellular hydrolysis of formyl peptides and subsequent uptake of liberated amino acids by alveolar macrophages
Identifieur interne : 003391 ( Main/Exploration ); précédent : 003390; suivant : 003392Extracellular hydrolysis of formyl peptides and subsequent uptake of liberated amino acids by alveolar macrophages
Auteurs : James P. Basilion [États-Unis] ; Douglas F. Stickle [États-Unis] ; Andrij Holian [États-Unis]Source :
- BBA - Molecular Cell Research [ 0167-4889 ] ; 1986.
English descriptors
- Teeft :
- Alveolar macrophage, Alveolar macrophages, Balanced salt solution, Biol, Cell biol, Cell viability, Extracellular, Extracellular hydrolysis, Extracellular medium, Extracellular phenylalanine, Formyl, Formyl peptide, Formyl peptide binding, Formyl peptide receptor, Formyl peptides, Holian, Hptlc, Hydrolysis, Intact peptide, Internalization, Intracellular, Intracellular phenylalanine, Ligand, Liquid scintillation, Macrophage, Neutrophil, Nonspecific binding, Peptide, Phenylalanine, Phenylalanine uptake, Polymorphonuclear, Polymorphonuclear neutrophils, Proteinase, Radioactivity, Receptor, Receptor binding, Scintillation, Scintillation vials, Steady state, Supernatant, Superoxide, Superoxide anion production, Surface proteinase, Unlabelled, Unpublished data.
Abstract
Abstract: The mechanism of accumulation of radioactive label from fNle-Leu-[3H]Phe by guinea pig alveolar macrophages was investigated. The binding of fNle-Leu-[3H]Phe to macrophages reached equilibrium within 5 min at 4°C, but equilibrium could not be achieved at temperatures where fNle-Leu-Phe stimulated superoxide anion production is observed (e.g., 21–23°C). At this temperature a rapid phase of initial binding of fNle-Leu-[3H]Phe to its receptor was followed by continued accumulation of cell-associated radioactivity which was linear and was dependent on the extracellular pH, i.e., the rate increased as the pH was lowered from pH 8 to pH 6. Examination for possible intracellular hydrolysis of fNle-Leu-[3H]Phe revealed the presence of extensive amounts of [3H]phenylalanine, both cell-associated and in the medium. The increases in cell-associated [3H]phenylalanine correlated in time and pH with cell-associated radioactivity that was accumulated after stimulation with fNle-Leu-[3H]Phe. The addition of 1 mM unlabelled phenylalanine blocked the long term accumulation of label from fNle-Leu-[3H]Phe by macrophages. 1 mM phenylalanine had no measureable effect on fNle-Leu-Phe stimulated O−2 production, fNle-Leu-[3H]Phe hydrolysis or on fNle-Leu-[3H]Phe binding to its receptor. These results indicated that the long term accumulation of radioactivity by alveolar macrophages was due to extracellular hydrolysis of fNle-Leu-[3H]Phe followed by transport of liberated [3H]phenylalanine into the cells. A high affinity (Km = 3.56·10−8 M) transport system for phenylalanine was measured in alveolar macrophages, which was not stimulated by the addition of fNle-Leu-Phe. The extracellular hydrolysis of fNle-Leu-[3H]Phe could not be attributed to release of macrophage enzymes into the medium. The responsible proteinase appears to be membrane bound and has a Km for the hydrolysis of fNle-Leu-[3H]Phe of 2.6·10−7 M which is similar to the Kd (1.5·10−7 M) for fNle-Leu-Phe binding. Taken together, these data suggest that for the alveolar macrophage: (1) formyl peptides are not internalized by a receptor-mediated process; (2) a surface proteinase can catalyze the hydrolysis of formyl peptides; and (3) [3H]phenylalanine formed by fNle-Leu-[3H]Phe hydrolysis is transported into the interior of the macrophage.
Url:
DOI: 10.1016/0167-4889(86)90143-6
Affiliations:
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Le document en format XML
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<term>Cell biol</term>
<term>Cell viability</term>
<term>Extracellular</term>
<term>Extracellular hydrolysis</term>
<term>Extracellular medium</term>
<term>Extracellular phenylalanine</term>
<term>Formyl</term>
<term>Formyl peptide</term>
<term>Formyl peptide binding</term>
<term>Formyl peptide receptor</term>
<term>Formyl peptides</term>
<term>Holian</term>
<term>Hptlc</term>
<term>Hydrolysis</term>
<term>Intact peptide</term>
<term>Internalization</term>
<term>Intracellular</term>
<term>Intracellular phenylalanine</term>
<term>Ligand</term>
<term>Liquid scintillation</term>
<term>Macrophage</term>
<term>Neutrophil</term>
<term>Nonspecific binding</term>
<term>Peptide</term>
<term>Phenylalanine</term>
<term>Phenylalanine uptake</term>
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<term>Radioactivity</term>
<term>Receptor</term>
<term>Receptor binding</term>
<term>Scintillation</term>
<term>Scintillation vials</term>
<term>Steady state</term>
<term>Supernatant</term>
<term>Superoxide</term>
<term>Superoxide anion production</term>
<term>Surface proteinase</term>
<term>Unlabelled</term>
<term>Unpublished data</term>
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<front><div type="abstract" xml:lang="en">Abstract: The mechanism of accumulation of radioactive label from fNle-Leu-[3H]Phe by guinea pig alveolar macrophages was investigated. The binding of fNle-Leu-[3H]Phe to macrophages reached equilibrium within 5 min at 4°C, but equilibrium could not be achieved at temperatures where fNle-Leu-Phe stimulated superoxide anion production is observed (e.g., 21–23°C). At this temperature a rapid phase of initial binding of fNle-Leu-[3H]Phe to its receptor was followed by continued accumulation of cell-associated radioactivity which was linear and was dependent on the extracellular pH, i.e., the rate increased as the pH was lowered from pH 8 to pH 6. Examination for possible intracellular hydrolysis of fNle-Leu-[3H]Phe revealed the presence of extensive amounts of [3H]phenylalanine, both cell-associated and in the medium. The increases in cell-associated [3H]phenylalanine correlated in time and pH with cell-associated radioactivity that was accumulated after stimulation with fNle-Leu-[3H]Phe. The addition of 1 mM unlabelled phenylalanine blocked the long term accumulation of label from fNle-Leu-[3H]Phe by macrophages. 1 mM phenylalanine had no measureable effect on fNle-Leu-Phe stimulated O−2 production, fNle-Leu-[3H]Phe hydrolysis or on fNle-Leu-[3H]Phe binding to its receptor. These results indicated that the long term accumulation of radioactivity by alveolar macrophages was due to extracellular hydrolysis of fNle-Leu-[3H]Phe followed by transport of liberated [3H]phenylalanine into the cells. A high affinity (Km = 3.56·10−8 M) transport system for phenylalanine was measured in alveolar macrophages, which was not stimulated by the addition of fNle-Leu-Phe. The extracellular hydrolysis of fNle-Leu-[3H]Phe could not be attributed to release of macrophage enzymes into the medium. The responsible proteinase appears to be membrane bound and has a Km for the hydrolysis of fNle-Leu-[3H]Phe of 2.6·10−7 M which is similar to the Kd (1.5·10−7 M) for fNle-Leu-Phe binding. Taken together, these data suggest that for the alveolar macrophage: (1) formyl peptides are not internalized by a receptor-mediated process; (2) a surface proteinase can catalyze the hydrolysis of formyl peptides; and (3) [3H]phenylalanine formed by fNle-Leu-[3H]Phe hydrolysis is transported into the interior of the macrophage.</div>
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