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Rat eosinophils: isolation and characterization of superoxide production
Author(s) -
Cypcar David,
Sorkness Ronald,
Sedgwick Julie,
Nagata Makoto,
Clough Jennifer,
Kaplan Michael,
Lemanske Robert F.
Publication year - 1996
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1002/jlb.60.1.101
Subject(s) - superoxide , zymosan , biology , immunology , chemotaxis , cytochalasin b , cytochalasin , biochemistry , in vitro , enzyme , cell , receptor , cytoskeleton
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.