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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1987-1-16
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pubmed:abstractText |
The interaction between liposomes coated with covalently linked rabbit immunoglobulin (RbIg-liposomes), and rat liver macrophages (Kupffer cells) in monolayer culture was studied biochemically with radioactive tracers and morphologically by electron microscopy. The attachment of immunoglobulin (Ig) to liposomes caused a five-fold increase in liposome uptake by the Kupffer cells at 37 degrees C, in comparison with uncoated liposomes. The uptake was linear with time for at least 4 h and linear with liposome concentration up to a lipid concentration of 0.2 mM. At 4 degrees C uptake, probably representing cell surface-bound liposomes, was reduced to a level of approx. 20% of the 37 degrees C values. Involvement of the Fc receptor in the uptake process was indicated by the reduction of RbIg-liposome uptake by more than 75% as a result of preincubating the cells with heat-aggregated human or rabbit Ig at concentrations (less than 2 mg/ml) at which bovine serum albumin (BSA) had virtually no effect on uptake. At high concentrations (10-35 mg/ml), however, albumin also reduced liposome uptake significantly (20-30%), which suggests an interaction of the RbIg-liposomes with the Kupffer cells that is partially non-specific. RbIg-liposome uptake was dependent on the amount of RbIg coupled to the liposomes. Maximal uptake values were reached at about 200 micrograms RbIg/mumol liposomal lipid. Electron microscopic observations on cells incubated with horseradish peroxidase-containing RbIg-liposomes demonstrated massive accumulation of peroxidase reaction product in intracellular vacuoles, showing that the uptake observed by label association represents true internalization.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin Fc Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulins,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Liposomes,
http://linkedlifedata.com/resource/pubmed/chemical/Peroxidase,
http://linkedlifedata.com/resource/pubmed/chemical/Peroxidases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Fc,
http://linkedlifedata.com/resource/pubmed/chemical/Serum Albumin, Bovine
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0014-4827
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
168
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
105-15
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:3023116-Animals,
pubmed-meshheading:3023116-Cells, Cultured,
pubmed-meshheading:3023116-Endocytosis,
pubmed-meshheading:3023116-Female,
pubmed-meshheading:3023116-Hot Temperature,
pubmed-meshheading:3023116-Immunoglobulin Fc Fragments,
pubmed-meshheading:3023116-Immunoglobulins,
pubmed-meshheading:3023116-Isoenzymes,
pubmed-meshheading:3023116-Kupffer Cells,
pubmed-meshheading:3023116-Liposomes,
pubmed-meshheading:3023116-Microscopy, Electron,
pubmed-meshheading:3023116-Particle Size,
pubmed-meshheading:3023116-Peroxidase,
pubmed-meshheading:3023116-Peroxidases,
pubmed-meshheading:3023116-Rats,
pubmed-meshheading:3023116-Rats, Inbred Strains,
pubmed-meshheading:3023116-Receptors, Fc,
pubmed-meshheading:3023116-Serum Albumin, Bovine
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pubmed:year |
1987
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pubmed:articleTitle |
Interaction of immunoglobulin-coupled liposomes with rat liver macrophages in vitro.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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