Interaction of immunoglobulin-coupled liposomes with rat liver macrophages in vitro
Autor: | Dharamdajal Kalicharan, Caesar E. Hulstaert, Jtp Derksen, Gerrit L. Scherphof, Hwm Morselt |
---|---|
Rok vydání: | 1987 |
Předmět: |
Hot Temperature
Kupffer Cells Fc receptor Immunoglobulins Receptors Fc Animals Bovine serum albumin Particle Size Cells Cultured Peroxidase Liposome biology Albumin Rats Inbred Strains Serum Albumin Bovine Cell Biology Mononuclear phagocyte system Molecular biology In vitro Endocytosis Immunoglobulin Fc Fragments Rats Isoenzymes Microscopy Electron Biochemistry Peroxidases Liposomes biology.protein Female Antibody Intracellular |
Zdroj: | Experimental cell research. 168(1) |
ISSN: | 0014-4827 |
Popis: | 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. |
Databáze: | OpenAIRE |
Externí odkaz: |