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 |
|---|---|
| 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 |
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Keywords
- cathepsin
- interferon
- interleukin
- lipopolysaccharide
- macrophages
ASJC Scopus subject areas
- Medicine (miscellaneous)
- Dentistry(all)
- Biochemistry, Genetics and Molecular Biology(all)
Cite this
Up-regulation, Enhanced Maturation, and Secretion of Cathepsin E in Mouse Macrophages Treated with Interferon-γ or Lipopolysaccharide. / Yanagawa, Michiyo; Tsukuba, Takayuki; Okamoto, Kuniaki; Takii, Ryosuke; Terada, Yoshihiro; Kadowaki, Tomoko; Yamamoto, Kenji.
In: Journal of Oral Biosciences, Vol. 48, No. 3, 2005, p. 218-225.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Up-regulation, Enhanced Maturation, and Secretion of Cathepsin E in Mouse Macrophages Treated with Interferon-γ or Lipopolysaccharide
AU - Yanagawa, Michiyo
AU - Tsukuba, Takayuki
AU - Okamoto, Kuniaki
AU - Takii, Ryosuke
AU - Terada, Yoshihiro
AU - Kadowaki, Tomoko
AU - Yamamoto, Kenji
PY - 2005
Y1 - 2005
N2 - 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.
AB - 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.
KW - cathepsin
KW - interferon
KW - interleukin
KW - lipopolysaccharide
KW - macrophages
UR - http://www.scopus.com/inward/record.url?scp=85009644904&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85009644904&partnerID=8YFLogxK
U2 - 10.2330/joralbiosci.48.218
DO - 10.2330/joralbiosci.48.218
M3 - Article
AN - SCOPUS:85009644904
VL - 48
SP - 218
EP - 225
JO - Journal of Oral Biosciences
JF - Journal of Oral Biosciences
SN - 1349-0079
IS - 3
ER -