author_facet Oh, Y K
Swanson, J A
Oh, Y K
Swanson, J A
author Oh, Y K
Swanson, J A
spellingShingle Oh, Y K
Swanson, J A
The Journal of cell biology
Different fates of phagocytosed particles after delivery into macrophage lysosomes.
Cell Biology
author_sort oh, y k
spelling Oh, Y K Swanson, J A 0021-9525 1540-8140 Rockefeller University Press Cell Biology http://dx.doi.org/10.1083/jcb.132.4.585 <jats:p>Phagocytosis in macrophages is often studied using inert polymer microspheres. An implicit assumption in these studies is that such particles contain little or no specific information in their structure that affects their intracellular fate. We tested that assumption by examining macrophage phagosomes containing different kinds of particles and found that although all particles progressed directly to lysosomes, their subsequent fates varied. Within 15 min of phagocytosis, &amp;gt;90% of phagosomes containing opsonized sheep erythrocytes, poly-e-caprolactone microspheres, polystyrene microspheres (PS), or polyethylene glycol-conjugated PS merged with the lysosomal compartment. After that point, however, the characteristics of phagolysosomes changed in several ways that indicated differing degrees of continued interaction with the lysosomal compartment. Sheep erythrocyte phagolysosomes merged together and degraded their contents quickly, poly-e-caprolactone phagolysosomes showed intermediate levels of interaction, and PS phagolysosomes became isolated within the cytoplasm. PS were relatively inaccessible to an endocytic tracer, Texas red dextran, added after phagocytosis. Moreover, immunofluorescent staining for the lysosomal protease cathepsin L decreased in PS phagolysosomes to 23% by 4 h after phagocytosis, indicating degradation of the enzyme without replacement. Finally, PS surface labeled with fluorescein-labeled albumin showed a markedly reduced rate of protein degradation in phagolysosomes, when compared to rates measured for proteins in or on other particles. Thus, particle chemistry affected both the degree of postlysosomal interactions with other organelles and, consequently, the intracellular half-life of particle-associated proteins. Such properties may affect the ability of particles to deliver macromolecules into the major histocompatibility complex class I and II antigen presentation pathways.</jats:p> Different fates of phagocytosed particles after delivery into macrophage lysosomes. The Journal of cell biology
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title Different fates of phagocytosed particles after delivery into macrophage lysosomes.
title_unstemmed Different fates of phagocytosed particles after delivery into macrophage lysosomes.
title_full Different fates of phagocytosed particles after delivery into macrophage lysosomes.
title_fullStr Different fates of phagocytosed particles after delivery into macrophage lysosomes.
title_full_unstemmed Different fates of phagocytosed particles after delivery into macrophage lysosomes.
title_short Different fates of phagocytosed particles after delivery into macrophage lysosomes.
title_sort different fates of phagocytosed particles after delivery into macrophage lysosomes.
topic Cell Biology
url http://dx.doi.org/10.1083/jcb.132.4.585
publishDate 1996
physical 585-593
description <jats:p>Phagocytosis in macrophages is often studied using inert polymer microspheres. An implicit assumption in these studies is that such particles contain little or no specific information in their structure that affects their intracellular fate. We tested that assumption by examining macrophage phagosomes containing different kinds of particles and found that although all particles progressed directly to lysosomes, their subsequent fates varied. Within 15 min of phagocytosis, &amp;gt;90% of phagosomes containing opsonized sheep erythrocytes, poly-e-caprolactone microspheres, polystyrene microspheres (PS), or polyethylene glycol-conjugated PS merged with the lysosomal compartment. After that point, however, the characteristics of phagolysosomes changed in several ways that indicated differing degrees of continued interaction with the lysosomal compartment. Sheep erythrocyte phagolysosomes merged together and degraded their contents quickly, poly-e-caprolactone phagolysosomes showed intermediate levels of interaction, and PS phagolysosomes became isolated within the cytoplasm. PS were relatively inaccessible to an endocytic tracer, Texas red dextran, added after phagocytosis. Moreover, immunofluorescent staining for the lysosomal protease cathepsin L decreased in PS phagolysosomes to 23% by 4 h after phagocytosis, indicating degradation of the enzyme without replacement. Finally, PS surface labeled with fluorescein-labeled albumin showed a markedly reduced rate of protein degradation in phagolysosomes, when compared to rates measured for proteins in or on other particles. Thus, particle chemistry affected both the degree of postlysosomal interactions with other organelles and, consequently, the intracellular half-life of particle-associated proteins. Such properties may affect the ability of particles to deliver macromolecules into the major histocompatibility complex class I and II antigen presentation pathways.</jats:p>
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author Oh, Y K, Swanson, J A
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description <jats:p>Phagocytosis in macrophages is often studied using inert polymer microspheres. An implicit assumption in these studies is that such particles contain little or no specific information in their structure that affects their intracellular fate. We tested that assumption by examining macrophage phagosomes containing different kinds of particles and found that although all particles progressed directly to lysosomes, their subsequent fates varied. Within 15 min of phagocytosis, &amp;gt;90% of phagosomes containing opsonized sheep erythrocytes, poly-e-caprolactone microspheres, polystyrene microspheres (PS), or polyethylene glycol-conjugated PS merged with the lysosomal compartment. After that point, however, the characteristics of phagolysosomes changed in several ways that indicated differing degrees of continued interaction with the lysosomal compartment. Sheep erythrocyte phagolysosomes merged together and degraded their contents quickly, poly-e-caprolactone phagolysosomes showed intermediate levels of interaction, and PS phagolysosomes became isolated within the cytoplasm. PS were relatively inaccessible to an endocytic tracer, Texas red dextran, added after phagocytosis. Moreover, immunofluorescent staining for the lysosomal protease cathepsin L decreased in PS phagolysosomes to 23% by 4 h after phagocytosis, indicating degradation of the enzyme without replacement. Finally, PS surface labeled with fluorescein-labeled albumin showed a markedly reduced rate of protein degradation in phagolysosomes, when compared to rates measured for proteins in or on other particles. Thus, particle chemistry affected both the degree of postlysosomal interactions with other organelles and, consequently, the intracellular half-life of particle-associated proteins. Such properties may affect the ability of particles to deliver macromolecules into the major histocompatibility complex class I and II antigen presentation pathways.</jats:p>
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spelling Oh, Y K Swanson, J A 0021-9525 1540-8140 Rockefeller University Press Cell Biology http://dx.doi.org/10.1083/jcb.132.4.585 <jats:p>Phagocytosis in macrophages is often studied using inert polymer microspheres. An implicit assumption in these studies is that such particles contain little or no specific information in their structure that affects their intracellular fate. We tested that assumption by examining macrophage phagosomes containing different kinds of particles and found that although all particles progressed directly to lysosomes, their subsequent fates varied. Within 15 min of phagocytosis, &amp;gt;90% of phagosomes containing opsonized sheep erythrocytes, poly-e-caprolactone microspheres, polystyrene microspheres (PS), or polyethylene glycol-conjugated PS merged with the lysosomal compartment. After that point, however, the characteristics of phagolysosomes changed in several ways that indicated differing degrees of continued interaction with the lysosomal compartment. Sheep erythrocyte phagolysosomes merged together and degraded their contents quickly, poly-e-caprolactone phagolysosomes showed intermediate levels of interaction, and PS phagolysosomes became isolated within the cytoplasm. PS were relatively inaccessible to an endocytic tracer, Texas red dextran, added after phagocytosis. Moreover, immunofluorescent staining for the lysosomal protease cathepsin L decreased in PS phagolysosomes to 23% by 4 h after phagocytosis, indicating degradation of the enzyme without replacement. Finally, PS surface labeled with fluorescein-labeled albumin showed a markedly reduced rate of protein degradation in phagolysosomes, when compared to rates measured for proteins in or on other particles. Thus, particle chemistry affected both the degree of postlysosomal interactions with other organelles and, consequently, the intracellular half-life of particle-associated proteins. Such properties may affect the ability of particles to deliver macromolecules into the major histocompatibility complex class I and II antigen presentation pathways.</jats:p> Different fates of phagocytosed particles after delivery into macrophage lysosomes. The Journal of cell biology
spellingShingle Oh, Y K, Swanson, J A, The Journal of cell biology, Different fates of phagocytosed particles after delivery into macrophage lysosomes., Cell Biology
title Different fates of phagocytosed particles after delivery into macrophage lysosomes.
title_full Different fates of phagocytosed particles after delivery into macrophage lysosomes.
title_fullStr Different fates of phagocytosed particles after delivery into macrophage lysosomes.
title_full_unstemmed Different fates of phagocytosed particles after delivery into macrophage lysosomes.
title_short Different fates of phagocytosed particles after delivery into macrophage lysosomes.
title_sort different fates of phagocytosed particles after delivery into macrophage lysosomes.
title_unstemmed Different fates of phagocytosed particles after delivery into macrophage lysosomes.
topic Cell Biology
url http://dx.doi.org/10.1083/jcb.132.4.585