Journal of Histochemistry & Cytochemistry · 1989 · 51 citations · 41 references
Life SciencesCell BiologyImmunologyEndocytosisImmunopathologyInflammationInflammatory MediatorsInflammatory SignalingLeukocyte AdhesionLeukocyte RecruitmentNeutrophil BiologyBiological Activity FeaturesEndothelial-leukocyte InteractionsEosinophil InteractionsEosinophil-mediated InflammationInflammatory ActivationLeukocyte-endothelium Interactions
We have recently shown that human neutrophils bind and internalize human eosinophil peroxidase (EPO) but not myeloperoxidase (MPO). In the present work, we studied the interactions of human EPO and MPO with other cells that may be involved in the inflammatory process, i.e., lymphocytes, monocytes, platelets, fibroblasts, and endothelial cells. The results indicate that EPO is bound by all the cell types considered, but is efficiently internalized only by lymphocytes, monocytes, and endothelial cells. Conversely, MPO binds appreciably only to fibroblasts and endothelial cells, although with a lower affinity than EPO, but its internalization by any of the cell types studied is hardly detectable. Furthermore, both peroxidases bind strongly to collagen fibers, whereas only EPO binds to elastin. The results suggest that EPO, owing to its high cytophilia, exerts its biological activity close to the site at which it is released from the eosinophil.
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SIMPLIFIED MYELOPEROXIDASE STAIN USING BENZIDINE DIHYDROCHLORIDE.
Leonard S. Kaplow · PubMed · 1965 · 530 citations
Medicine, Hematology, Pathology +8
Cellular and extracellular myeloperoxidase in pyogenic inflammation
PP Bradley, RD Christensen, Gerald Rothstein · Blood · 1982 · 514 citations · Full text
Oxidative Autoactivation of Latent Collagenase by Human Neutrophils
Stephen J. Weiss, Gary J. Peppin, X. Ortiz et al. · Science · 1985 · 469 citations