Rifampin affects polymorphonuclear leukocyte interactions with bacterial and synthetic chemotaxins but not interactions with serum-derived chemotaxins
| Autor: | D. E. Chenoweth, J C Hollers, C W Smith, R. D. Nelson, V. D. Fiegel, G D Gray |
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| Rok vydání: | 1983 |
| Předmět: |
Neutrophils
Complement C5a Receptors Cell Surface Pharmacology Granulocyte Biology In Vitro Techniques Binding Competitive chemistry.chemical_compound medicine polycyclic compounds Humans Pharmacology (medical) Receptor Complement component 5 Chemotactic Factors Complement C5 Chemotaxis hemic and immune systems N-Formylmethionine leucyl-phenylalanine biochemical phenomena metabolism and nutrition Ligand (biochemistry) Receptors Formyl Peptide In vitro N-Formylmethionine Leucyl-Phenylalanine Chemotaxis Leukocyte Infectious Diseases medicine.anatomical_structure Biochemistry Mechanism of action chemistry lipids (amino acids peptides and proteins) medicine.symptom Rifampin Research Article |
| Zdroj: | Antimicrobial agents and chemotherapy. 24(5) |
| ISSN: | 0066-4804 |
| Popis: | Three independent experimental approaches support the hypothesis that rifampin competes for receptors on polymorphonuclear leukocytes (PMLs) with small peptide chemoattractants, e.g., N-formylmethionylleucylphenylalanine (FMLP), but not with serum-derived chemoattractants (C5a). First, rifampin inhibited chemotaxis induced with FMLP but reversed the immobilization of PMLs that occurred at high FMLP concentrations. Second, rifampin competed with radiolabeled FMLP for binding sites on PMLs and displaced already-bound radiolabeled FMLP. Third, rifampin blocked and reversed the bipolar shape changes induced in PMLs by FMLP. These effects occurred at concentrations attained during rifampin therapy and were not due to rifampin toxicity. In contrast, no effect of rifampin was observed on serum-derived chemoattractants (C5a) in any of the three systems. The evidence suggests, therefore, that rifampin is a ligand for FMLP-type receptors on PMLs. |
| Databáze: | OpenAIRE |
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