help button home button Am J Pathol R & D Systems
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS

This Article
Right arrow Order Full text via Infotrieve
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Dvorak, A. M.
Right arrow Articles by Galli, S. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Dvorak, A. M.
Right arrow Articles by Galli, S. J.

American Journal of Pathology, Vol 118, 425-438, Copyright © 1985 by American Society for Investigative Pathology


REGULAR ARTICLES

Vesicular uptake of eosinophil peroxidase by guinea pig basophils and by cloned mouse mast cells and granule-containing lymphoid cells

AM Dvorak, SJ Klebanoff, WR Henderson, RA Monahan, K Pyne and SJ Galli

Guinea pig basophils, cloned mouse mast cells, and cloned mouse granule- containing lymphoid cells were found to utilize a vesicular transport system to internalize eosinophil peroxidase (EPO) added in vitro. Kinetic analysis indicated that EPO internalization involved the binding of EPO to the plasma membrane, the formation of complex surface invaginations, and the movement of EPO-laden vesicles, tubules, and vacuoles toward the center of the cells. EPO became associated with multivesicular bodies in granule-containing lymphoid cells and mast cells, with immature granules in mast cells, and with mature granules in basophils. In other cells, the endogenous production of granule peroxidases (neutrophils and eosinophils) or the prior uptake of exogenous peroxidatic substances (some basophils) precluded cytochemical analysis of granules for EPO. Vesicular transport of EPO provides a possible explanation for the variable detection of peroxidase activity in mast cells or basophils. It also provides a mechanism for sequestration of this potentially toxic material or for its storage for possible future use.


This article has been cited by other articles:


Home page
J. Pharmacol. Exp. Ther.Home page
S. He, M. D. A. Gaça, A. R. McEuen, and A. F. Walls
Inhibitors of Chymase as Mast Cell-Stabilizing Agents: Contribution of Chymase in the Activation of Human Mast Cells
J. Pharmacol. Exp. Ther., November 1, 1999; 291(2): 517 - 523.
[Abstract] [Full Text]


Home page
Pharmacol. Rev.Home page
M. A. Giembycz and M. A. Lindsay
Pharmacology of the Eosinophil
Pharmacol. Rev., June 1, 1999; 51(2): 213 - 340.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
K Xu, R. Williams, D Holowka, and B Baird
Stimulated release of fluorescently labeled IgE fragments that efficiently accumulate in secretory granules after endocytosis in RBL-2H3 mast cells
J. Cell Sci., January 8, 1998; 111(16): 2385 - 2396.
[Abstract] [PDF]


Home page
Arch DermatolHome page
A. J. Scheman, M. D. Hordinsky, D. W. Groth, G. M. Vercellotti, and K. M. Leiferman
Evidence for Eosinophil Degranulation in the Pathogenesis of Herpes Gestationis
Arch Dermatol, August 1, 1989; 125(8): 1079 - 1083.
[Abstract] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1985 by the American Society for Investigative Pathology.