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Cited by 271Cellular transport and secretionAutophagy in Disease and TherapyPhagocytosis and Immune Regulation

The DOI matches its Crossref record; 54 of the 54 references it cites were found in a registry or an index.

Immunocytochemical characterization of the endocytic and phagolysosomal compartments in peritoneal macrophages

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Rabinowitz, S, Horstmann, H, Gordon, S, Griffiths, G·1992·The Journal of Cell Biology
DOI 10.1083/jcb.116.1.95PMC PMC2289258
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Abstract

We have used endocytic and phagocytic tracers in an EM immunocytochemical study to define the compartments of the phagocytic and endocytic pathways in mouse peritoneal macrophages. Endocytosed BSA-gold appeared successively in early endosomes, spherical endosomal vesicles, a late endosomal tubuloreticular compartment (TC), and terminal lysosomes. The TC appeared as an elaborate structure enriched for the lysosomal membrane glycoproteins Lamp 1 and Lamp 2, and expressing significant levels of rab7, a late endosome-specific GTP-binding protein. The cation-independent mannose-6-phosphate receptor was restricted to specialized regions of the TC that were predominantly adjacent to the Golgi complex. Both the early endosome and the TC had coated bud structures whose composition and function are presently unknown. Phagolysosomes containing latex beads expressed the same membrane antigens and received endocytic tracers simultaneously with the TC. Since the membrane surrounding both organelles was also in direct continuity, we assume that both structures form one functional compartment. Macrosialin, an antigen confined to macrophages and dendritic cells, was heavily expressed in TC and phagolysosomal membranes with low levels being detected in other endosomal compartments and on the cell surface. Treatment of cells with wheat germ agglutinin drastically altered the morphology of the TC, giving rise to sheets of tightly adherent membrane and greatly expanded vesicles, in which cell-associated wheat germ agglutinin was concentrated. The spherical endosomal carrier vesicles loaded with internalized gold tracers clustered nearby, often making contact without fusing. Since the delivery of endocytic tracer to the TC was significantly delayed these experiments suggest that the lectin is somehow preventing the endosome vesicles from fusing with the TC. Collectively, our data argue first that the PLC is equivalent to the "tubular lysosomes" commonly described in macrophages, and second that the meeting of the phagocytic and endocytic pathway occurs in this compartment.

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Metadata

Authors
Rabinowitz, S., Horstmann, H., Gordon, S., & Griffiths, G.
Affiliations
University of Oxford (GB)
ORCID
Venue
The Journal of Cell Biology
Publisher
Rockefeller University Press
Published
1992-01-01
Volume
116
Issue
1
Pages
95-112
ISSN
  • 0021-9525 (ISSN-L)
  • 1540-8140
DOI
10.1083/jcb.116.1.95
PMC
PMC2289258
OpenAlex
W2171821916
Cited by
271
References
54
Citations by year
2026: 1 · 2024: 2 · 2023: 1 · 2022: 1 · 2021: 1 · 2020: 3 · 2018: 1 · 2016: 1 · 2015: 5 · 2014: 4 · 2013: 3 · 2012: 2
FWCI
10.12
Type
journal article
Language
en
Open access
Licence
cc-by-nc-sa
Locations
  • The Journal of Cell Biology (publishedVersion)
  • PubMed Central (publishedVersion, cc-by-nc-sa)
  • PubMed (publishedVersion)
Funders
Wellcome Trust
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
  • Life Sciences › Immunology and Microbiology › Immunology › Phagocytosis and Immune Regulation
Keywords
peritoneal macrophages, endocytic pathway, phagolysosomes, late endosomes, lysosomes, LAMP1, LAMP2, Rab7, mannose 6-phosphate receptor, wheat germ agglutinin, endosome fusion
MeSH terms
Animals, Cells, Cultured, Endocytosis, Lysosomes, Macrophages, Male, Membrane Glycoproteins, Mice, Inbred C57BL, Microscopy, Electron, Models, Biological, Phagocytosis, Wheat Germ Agglutinins, Biomarkers, Antigens, CD, Fluorescein-5-isothiocyanate, Mice, Lysosomal Membrane Proteins

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