Abstract
Cathepsin E is an intracellular aspartic proteinase that is predominantly localized in the endosomal compartments of antigen presenting cells including macrophages. Here, we have investigated the expression of cathepsin E in mouse macrophages treated with interferon (IFN)-γ, lipopolysaccharide (LPS), interleukin (IL)-10, and IL-4. The mRNA levels of cathepsin E in macrophages stimulated with IFN-γ and LPS were increased, but conversely, that with IL-10 was decreased. However, upon stimulation with IFN-γ or LPS, the activity levels of cathepsin E in the activated cells were markedly decreased, but those in the culture media were increased. Immunoblot analysis revealed that procathepsin E in the cells was largely converted to the mature form in the cells upon stimulation with IFN-γ. In addition, the extracellular enzyme was reacted with antibodies to mature cathepsin E but not with antibodies for procathepsin E. By contrast, when macrophages were treated with IL-4, cathepsin E production was significantly decreased in both the cell and the medium. These results indicate that, upon stimulation with IFN-γ and LPS, cathepsin E is up-regulated in macrophages, which is accompanied by the enhanced maturation and secretion of the enzyme. Conversely, cathepsin E is down-regulated by treatment with IL-4 and IL-10.
Original language | English |
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Pages (from-to) | 218-225 |
Number of pages | 8 |
Journal | Journal of Oral Biosciences |
Volume | 48 |
Issue number | 3 |
DOIs | |
Publication status | Published - 2005 |
Externally published | Yes |
Keywords
- cathepsin
- interferon
- interleukin
- lipopolysaccharide
- macrophages
ASJC Scopus subject areas
- Medicine (miscellaneous)
- Dentistry(all)
- Biochemistry, Genetics and Molecular Biology(all)