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rdf:type |
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lifeskim:mentions |
|
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pubmed:issue |
5
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pubmed:dateCreated |
1994-4-20
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pubmed:abstractText |
Human recombinant superoxide dismutase (SOD) was modified into a mannosylated form (Man-SOD), and its cellular uptake and inhibitory effect on superoxide anion release were studied in vitro, using cultured mouse peritoneal macrophages. [111In]Man-SOD was taken up by the macrophages to a great extent, whereas no significant uptake was observed for native and galactosylated SOD. The uptake of Man-SOD was inhibited significantly at a low temperature and by the presence of mannan, mannose and colchicine, demonstrating the targeted delivery of Man-SOD via mannose receptor-mediated endocytosis. Man-SOD exhibited a superior inhibitory effect on superoxide anion release from inflammatory macrophages stimulated by phorbol-myristate acetate. The present study suggested the potential of Man-SOD as a therapeutic agent for the inflammatory disease mediated by superoxide anions generated by macrophages.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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|
pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0006-2952
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pubmed:author |
|
|
pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
47
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
853-8
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:8135860-Animals,
pubmed-meshheading:8135860-Cells, Cultured,
pubmed-meshheading:8135860-Humans,
pubmed-meshheading:8135860-Lectins, C-Type,
pubmed-meshheading:8135860-Macrophages,
pubmed-meshheading:8135860-Male,
pubmed-meshheading:8135860-Mannose-Binding Lectins,
pubmed-meshheading:8135860-Mice,
pubmed-meshheading:8135860-Mice, Inbred ICR,
pubmed-meshheading:8135860-Receptors, Cell Surface,
pubmed-meshheading:8135860-Recombinant Proteins,
pubmed-meshheading:8135860-Superoxide Dismutase,
pubmed-meshheading:8135860-Superoxides
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pubmed:year |
1994
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|
pubmed:articleTitle |
Targeted delivery of superoxide dismutase to macrophages via mannose receptor-mediated mechanism.
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pubmed:affiliation |
Department of Basic Pharmaceutics, Faculty of Pharmaceutical Sciences, Kyoto University, Japan.
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pubmed:publicationType |
Journal Article
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