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Published April 1, 1981 | public
Journal Article Open

Phagocytosis of carbohydrate-modified phospholipid vesicles by macrophage


Modification of the surface of distearoyl phosphatidylcholine vesicles with synthetic glycolipids dramatically affects the rate of uptake of these vesicles by mouse peritoneal macrophage. The high rate of uptake of 6-aminomannose-modified vesicles is effectively inhibited by cytochalasin B and chloroquine but not by colchicine, indicating that the mechanism of vesicle uptake is phagocytosis. Other modified vesicles appear to have some effect on the rate of uptake of 6-aminomannose-modified vesicles suggesting that the various vesicle types compete for the same initial binding sites. Analysis of 6-aminomannose-modified vesicles by γ-ray perturbed angular correlation spectroscopy shows that the rotational correlation time of the encapsulated (111)In(3+) does not change when the vesicles associate with macrophage. This result is consistent with transmission electron microscopy, which indicates that the aminomannose-modified vesicles remain intact after phagocytosis as aggregates of fused and intact vesicles surrounded by a single bilayer membrane structure.

Additional Information

Copyright © 1981 by the National Academy of Sciences. Contributed by John D. Baldeschwieler, November 20, 1980. We thank Drs. T. Y. Shen and M. M. Ponpipom (Merck Sharp & Dohme) and Drs. William S. Sly and Paul H. Schlesinger (Washington University School of Medicine, St. Louis, MO) for valuable discussions during the course of these studies. This work was supported by National Institutes of Health Grant GM 21111-07, National Science Foundation Grant CHE79-18401, and a grant from Merck & Co., Inc. This is contribution no. 6342 from the Arthur Amos Noyes Laboratory of Chemical Physics. The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U. S. C. §1734 solely to indicate this fact.


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