Role of prosaposin in the mouse embryogenesis
| Project/Area Number |
23700515
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Laboratory animal science
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| Research Institution | Tokai University |
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Principal Investigator |
YONESHIGE Azusa 東海大学, 糖鎖科学研究所, 特定研究員 (70586750)
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| Project Period (FY) |
2011 – 2012
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| Project Status |
Completed (Fiscal Year 2012)
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| Budget Amount *help |
¥3,120,000 (Direct Cost: ¥2,400,000、Indirect Cost: ¥720,000)
Fiscal Year 2012: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2011: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
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| Keywords | 胚発生 / プロサポシン / サポシン |
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| Research Abstract |
Prosaposin (PSAP) is the precursor protein of saposins (SAPs) which are required for the lysosomal hydrolysis of sphingolipids. Although PSAP itselfis known to be secreted into several body fluids, its physiological function is not well understood. PSAP deficient mice (Psap-/-) are born at the much lower frequency suggesting the function of PSAP during the mouse embryogenesis. In this study, we investigated the temporal and spatial expression of PSAP in the wild-type mouse embryo and the phenotype of Psap-/-embryo. Protein levels of PSAP in the mouse embryonic tissues were low at embryonic day (E) 6.5 and increased at E7.5 to 9.5. Immunohistochemical analyses showed high expressions of PSAP in decidua at E7.5 to 9.5 and in spongiotrophoblastic layer of placenta at E10.5. SAPs were highly expressed in the large lysosomes of visceral endoderm of yolk sac. Histopathological examination of Psap-/-embryos indicated the developmental abnormality as early as at around E7.5. Shrunken cells were observed in decidua. The number and the size of large lysosome in visceral endoderm of yolk sac were decreased. These lethal phenotypes of Psap-/-embryos were rescued by maternal overexpression of PSAP. Our findings suggest that PSAP and SAPs play important roles during the early stage of mouse pregnancy, at the site of decidua, yolk sac and placenta.
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Report
(4 results)
Research Products
(33 results)
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[Journal Article] Chemoenzymatic synthesis of hydrophobic glycoprotein: synthesis of saposin C carrying complex-type carbohydrate2012
Author(s)
Hojo H, Tanaka H, Hagiwara M, Asahina Y, Ueki A, Katayama H, Nakahara Y, Yoneshige A, Matsuda J, Ito Y, Nakahara Y
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Journal Title
Journal of OrganicChemistry
Volume: 77
Pages: 9437-9446
Related Report
Peer Reviewed
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[Journal Article] Synthesis of the sphingolipid activator protein, saposin C, using an azido-protected O-acyl isopeptide as an aggregation-disrupting element2011
Author(s)
Hojo H, Katayama H, Tano C, Nakahara Y, Yoneshige A, Matsuda J, Sohma Y, Kiso Y,Nakahara Y
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Journal Title
Tetrahedron Letters
Volume: 52
Pages: 635-639
Related Report
Peer Reviewed
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[Journal Article] Synthesis of the sphingolipid activator protein, saposin C, using an azido-protected O-acyl isopeptide as an aggregation-disrupting element.2011
Author(s)
Hojo H, Katayama H, Tano C, Nakahara Y, Yoneshige A, Matsuda J, Sohma Y, Kiso Y, Nakahara Y
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Journal Title
Tetrahedron Letters
Volume: 52
Pages: 635-639
Related Report
Peer Reviewed
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