Measurement of environmental formylmethionyl‐peptides
| Autor: | T. A. Shahan, E. A. Ronk, P. R. Clark, Vincent Castranova, Paul D. Siegel |
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| Rok vydání: | 1994 |
| Předmět: |
Organic dust
Receptors Peptide Guinea Pigs In Vitro Techniques Toxicology High-performance liquid chromatography Amidohydrolases Radioligand Assay Environmental Microbiology Animals Humans Carbon Radioisotopes Receptors Immunologic Chromatography High Pressure Liquid Bacteria biology Chemistry Degranulation Biological activity Smooth muscle contraction biology.organism_classification Receptors Formyl Peptide Pollution Culture Media N-Formylmethionine Leucyl-Phenylalanine Biochemistry Toxicity Rabbits Oxidation-Reduction Quantitative analysis (chemistry) |
| Zdroj: | Journal of Toxicology and Environmental Health. 42:275-288 |
| ISSN: | 0098-4108 |
| DOI: | 10.1080/15287399409531879 |
| Popis: | Formylmethionyl-peptides are naturally occurring, biologically active ligands produced by bacteria. They produce a variety of biological effects including neutrophil chemotaxis, cellular degranulation, oxygen-free radical production, and smooth muscle contraction. Our studies have demonstrated that oxidized and reduced forms of formylmethionyl-leucyl-phenylalanine (fMLP) can be detected in bulk environmental organic dust samples. Organic dust fMLP content may not reflect total formylmethionyl-peptide content and pathological sequelae. Attempts to develop a total formylmethionyl-peptide assay that would reflect its pathological potential have thus far been unsuccessful. Information has been derived concerning the biology of formylmethionyl-peptides from these studies. Chromatographic, radioenzymatic, and radioreceptor-ligand binding studies were performed. High-performance liquid chromatography (HPLC) analysis of synthetic and environmental fMLP demonstrated that fMLP is labile, forming three oxidation products. HPLC is limited by inadequate sensitivity for air sample analysis and the probability of the presence of multiple formylmethionyl-peptides. Deformylases were isolated from Escherichia coli, but their usefulness in a competitive assay to detect formylmethionyl-peptides was limited by specificity differences from that for biological receptors. Receptor binding studies were conducted in an attempt to replace the deformylase with a biological receptor. The receptor binding patterns noted were consistent with the existence of three distinct formylmethionyl-peptide receptor subsets in neutrophils and alveolar macrophages. The plurality of fMLP receptor subtypes interfered with formylmethionyl-peptide measurement in a competitive assay. Formylmethionyl-peptides may contribute to organic dust-induced disease, but better techniques for the assessment of exposure to these agents are needed to properly assess their health impact. |
| Databáze: | OpenAIRE |
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