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Localization and subcellular distribution of prolyl oligopeptidase in the mouse placenta
Shin Matsubara1, Takayuki Takahashi, Atsushi P Kimura
1Graduate School of Life Science, Hokkaido University, Sapporo 060-0810, Japan.
Abstract:
Prolyl oligopeptidase (POP) is a serine endopeptidase which selectively digests a -Pro-X- peptide bond. Our previous study showed that POP mRNA was strongly expressed in the spongiotrophoblast of the mouse placenta at E17.5, suggesting its importance in development. To gain more insight into POP's role during gestation, we investigated its expression using different developmental stages of placenta. As a result of in situ hybridization, we found that localization of POP mRNA changed at E12.5. POP mRNA was strongly expressed in the spongiotrophoblast and labyrinth at E10.5 and E11.5 but thereafter only in the spongiotrophoblast. Immunohistochemistry revealed that POP was present in the parietal trophoblast giant cell, the spongiotrophoblast cell, and the labyrinth at E11.5 but the strong expression in the labyrinth was maintained only in the canal-associated and sinusoidal trophoblast giant cells at E16.5 and E18.5. To determine subcellular distribution of the POP protein, we fractionated the placental extract into cytoplasmic, membrane, and nuclear subfractions. By Western blot analysis, POP was detected in the cytoplasmic and membrane fractions but not in the nuclear fraction at E11.5 and E16.5. Interestingly, the cytoplasmic POP exhibited higher enzymatic activity than the membrane-associated type. These data suggest that the cytoplasmic and membrane-associated POP have distinct roles in different types of placental cells.
Insights
Prolyl oligopeptidase (POP) expression in the mouse placenta changes throughout gestation. This serine endopeptidase is found in different cell types and subcellular locations, suggesting distinct developmental roles.
Area of Science:
- Reproductive Biology
- Developmental Biology
- Biochemistry
Background:
- Prolyl oligopeptidase (POP) is a serine endopeptidase known to cleave peptide bonds containing proline.
- Previous research indicated strong POP mRNA expression in the mouse placenta at E17.5, suggesting a role in placental development.
Purpose of the Study:
- To investigate the spatiotemporal expression and subcellular localization of prolyl oligopeptidase (POP) in the developing mouse placenta.
- To understand the potential distinct roles of POP in different placental cell types and compartments during gestation.
Main Methods:
- In situ hybridization was used to analyze POP mRNA localization across various placental developmental stages (E10.5-E18.5).
- Immunohistochemistry was employed to detect POP protein distribution in placental tissues.
- Western blot analysis of fractionated placental extracts (cytoplasmic, membrane, nuclear) determined subcellular POP distribution.
Main Results:
- POP mRNA localization shifted from the spongiotrophoblast and labyrinth (E10.5-E11.5) to primarily the spongiotrophoblast (post-E12.5).
- POP protein was detected in parietal trophoblast giant cells, spongiotrophoblast cells, and labyrinthine cells, with specific localization in canal-associated and sinusoidal trophoblast giant cells later in gestation.
- POP was found in cytoplasmic and membrane fractions, but not nuclear fractions, of placental extracts, with higher enzymatic activity in the cytoplasmic fraction.
Conclusions:
- The expression pattern and subcellular localization of POP change significantly during mouse placental development.
- Distinct POP expression in various placental cell types and its presence in cytoplasmic and membrane fractions suggest specialized functions in placental development and physiology.
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