Alteration of neutrophil trafficking by a lipocortin 1 N-terminus peptide
| Autor: | Roderick J. Flower, Jeanette G. Harris, Mauro Perretti |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
Male
medicine.drug_class Neutrophils Molecular Sequence Data Macrophage-1 Antigen Neuraminidase Biology Sialidase Monoclonal antibody Mice In vivo Polysaccharides medicine Cell Adhesion Animals Humans Interleukin 8 Amino Acid Sequence Platelet Activating Factor Annexin A1 Pharmacology Interleukin-8 Anticoagulants Biological activity Macrophage Activation Molecular biology In vitro Neutrophilia Kinetics Biochemistry Mechanism of action CD18 Antigens Antigens Surface medicine.symptom Peptides |
| Zdroj: | European journal of pharmacology. 279(2-3) |
| ISSN: | 0014-2999 |
| Popis: | Sialidase, fucoidin and a peptide corresponding to most of lipocortin 1 N-terminus, termed LC1-(Ac2-26)-peptide, induced an intense 2 h neutrophilia whereas a monoclonal antibody to murine CD11b induced an effect by 1 h. The neutropenic response stimulated by platelet-activating factor (PAF) was significantly reduced in the presence of sialidase, fucoidin, LC1-(Ac2-26)-peptide and monoclonal antibody anti-CD11b. Neutrophil migration into a 6-day-old mouse air-pouch induced by interleukin-1 was inhibited by all the pharmacological agents. In vitro, PAF up-regulated CD11b expression on the neutrophil surface but neither human or mouse LC1-(Ac2-26)-peptide inhibited this response. CD11b up-regulation on neutrophils occurred after PAF administration in vivo and was maximal at 2 min. LC1-(Ac2-26)-peptide mimics the action of agents interfering with leucocyte rolling and adhesion in vivo, however, does not inhibit CD11b up-regulation in vitro suggesting other phenomena are important in the activity of this peptide. |
| Databáze: | OpenAIRE |
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