1. Rat eosinophils: isolation and characterization of superoxide production
- Author
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Robert F. Lemanske, Jennifer Clough, Makoto Nagata, Ronald L. Sorkness, Julie B. Sedgwick, David Cypcar, and Michael R. Kaplan
- Subjects
Male ,Cytochalasin B ,Immunology ,Cell ,Ionophore ,chemistry.chemical_element ,Inflammation ,Cell Separation ,In Vitro Techniques ,Biology ,Calcium ,Allergic inflammation ,chemistry.chemical_compound ,Peritoneal cavity ,Superoxides ,medicine ,Animals ,Humans ,Immunology and Allergy ,Platelet Activating Factor ,Calcimycin ,Superoxide ,Zymosan ,Cell Biology ,Molecular biology ,Rats ,Eosinophils ,N-Formylmethionine Leucyl-Phenylalanine ,Kinetics ,medicine.anatomical_structure ,chemistry ,Biochemistry ,Tetradecanoylphorbol Acetate ,medicine.symptom - Abstract
Studies with isolated cells are important to the understanding of mechanisms by which eosinophils participate in allergic inflammation. Due to species variability, isolation techniques and cell biology need to be defined for each source. We developed methods to obtain rat eosinophils with purity and viability exceeding 90%, characterized the superoxide anion production of these cells in response to standard activators, and compared these results with those previously obtained in our laboratories with the use of human eosinophils. Rat eosinophils responded vigorously to phorbol myristate acetate and poorly to platelet-activating factor and to N-formyl-methionyl-leucyl-phenylalanine, parallel to the responses of human eosinophils. In contrast, rat eosinophils responded unlike human eosinophils to other activators, having a larger response to calcium ionophore A23187, a smaller response to serum-treated or serum-opsonized zymosan, and a negative rather than positive modulatory effect of cytochalasin B. We conclude that rat eosinophils can be obtained in high purity and with intact responsiveness to a number of different activators.
- Published
- 1996