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Uptake of human eosinophil peroxidase and myeloperoxidase by cells involved in the inflammatory process.
Author(s) -
Giuliano Zabucchi,
Maria Rosa Soranzo,
Renzo Menegazzi,
Paolo Bertoncin,
Ermanno Nardon,
Pierluigi Patriarca
Publication year - 1989
Publication title -
journal of histochemistry and cytochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.971
H-Index - 124
eISSN - 1551-5044
pISSN - 0022-1554
DOI - 10.1177/37.4.2538504
Subject(s) - eosinophil peroxidase , myeloperoxidase , eosinophil , peroxidase , chemistry , microbiology and biotechnology , internalization , granulocyte , monocyte , inflammation , cell , immunology , biochemistry , biology , enzyme , asthma
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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