Macrosialin, a macrophage-restricted membrane sialoprotein differentially glycosylated in response to inflammatory stimuli.
Open accessAbstract
Rat monoclonal antibody FA/11 has been used to identify macrosialin, a sialoglycoprotein confined to murine mononuclear phagocytes and related cells. Originally identified as a macrophage-associated glycoprotein predominantly localized in intracellular membranes (Smith, M.J., and G.L.E. Koch. 1987. J. Cell Sci. 87:113), the antigen is widely expressed on tissue macrophages, including those in lymphoid areas, and is expressed at low levels on isolated dendritic cells. Immuno-adsorption experiments reported here show that macrosialin is identical to the major 87-115-kD sialoglycoprotein previously identified by lectin blotting in exudate but not resident peritoneal macrophages (Rabinowitz, S., and S. Gordon. 1989. J. Cell Sci. 93:623). Resident peritoneal macrophages express low levels of macrosialin antigen in a glycoform that does not bind 125I wheat germ agglutinin or 125I peanut agglutinin; inflammatory stimuli upregulate expression of this antigen (up to 17-fold), in an alternative glycoform that is detected by these lectins. Pulse-chase experiments reveal a 44-kD core peptide that initially bears high-mannose chains (giving Mr 66 kD) and is subsequently processed to a mature protein of Mr 87-104 kD. Each glycoform contains N-linked glycan, as well as O-linked sugar structures that show alternative processing. Poly-N-acetyllactosamine structures are detected in the exudate cell glycoform only. This new marker for mononuclear phagocytes illustrates two strategies by which macrophages remodel their membranes in response to inflammatory stimuli. Its predominantly intracellular location and restricted cell distribution suggest a possible role in membrane fusion or antigen processing.
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Old mice have higher CD68 mRNA and protein, a macrophage marker.
“mRNA and protein levels of the macrophage marker CD68 increased in old mice, consistent with more activated macrophage in old tissues33 (Fig. 4b,c).”
From Senescent cells promote tissue NAD+ decline during ageing via the activation of CD38+ macrophages (2020) · cites this paper as [33]
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References 48 · Cited by 233
- Authors
- Rabinowitz, S. S., & Gordon, S.
- Affiliations
- University of Oxford (GB)
- ORCID
- Gordon, S
- Venue
- The Journal of experimental medicine
- Publisher
- Rockefeller University Press
- Published
- 1991-10-01
- Volume
- 174
- Issue
- 4
- Pages
- 827-836
- ISSN
- 0022-1007 (ISSN-L)
- 1540-9538
- PMC
- PMC2118958
- OpenAlex
- W2143487048
- Cited by
- 233
- References
- 48
- Citations by year
- 2026: 6 · 2025: 4 · 2024: 3 · 2023: 12 · 2022: 4 · 2021: 1 · 2020: 9 · 2019: 6 · 2018: 2 · 2017: 5 · 2016: 6 · 2015: 4 · 2014: 4 · 2013: 5 · 2012: 8
- FWCI
- 2.51
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The Journal of Experimental Medicine (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- University of Cape Town
- Medical Research Council
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Physical Sciences › Chemistry › Organic Chemistry › Carbohydrate Chemistry and Synthesis
- Keywords
- sialoglycoproteins, macrophages, mononuclear phagocytes, membrane glycosylation, inflammatory stimuli, N-glycosylation, O-glycosylation, poly-N-acetyllactosamine, lectin binding, peritoneal macrophages, dendritic cells, membrane remodeling, antigen processing, membrane fusion
- MeSH terms
- Animals, Antibodies, Monoclonal, Cells, Cultured, Electrophoresis, Polyacrylamide Gel, Glycoside Hydrolases, Glycosylation, Immunoglobulin G, Immunohistochemistry, Inflammation, Macrophages, Membrane Glycoproteins, Mice, Inbred C57BL, Molecular Weight, Mycobacterium bovis, Propionibacterium acnes, Protein Processing, Post-Translational, Sialoglycoproteins, Blotting, Western, Mice
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