2012 Fiscal Year Final Research Report
Biological activities of ovine and bovine placental prolactin family proteins
Project/Area Number |
22580327
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Applied animal science
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Research Institution | National Institute of Agrobiological Sciences |
Principal Investigator |
TAKAHASHI Toru 独立行政法人農業生物資源研究所, 動物生産生理機能研究ユニット, 上級研究員 (20355738)
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Project Period (FY) |
2010 – 2012
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Keywords | ウシ / 胎盤 / プロラクチン |
Research Abstract |
Bovine prolactin-related protein-I (PRP1) is a non-classical member of prolactin (PRL) family proteins. However, its function is still unknown. PRL, when cleaved by cathepsin D and matrix metalloproteinases (MMPs), resulted in N-terminal 16 kDa fragments (16K-PRL) that have antiangiogenetic properties in human and rodents. We examined the possibility of similar activity of bovine PRP1. PRP1 (normally 33 kDa) was cleaved by cathepsins (CTSs), MMPs, and bovine cotyledonary-conditioned medium (BCCM), and generated mainly 26 kDa N-terminal fragments. Two specific enzyme families, CTSs and MMPs cleaved intact PRP1, and BCCM also contained PRP1 cleavage activity. Bioactivity of cleaved PRP1 was examined in a cell proliferation assay using bovine brain vascular endothelial cells. The cleaved PRP1 stimulated the proliferation of endothelial cells in vitro. The endothelial cell proliferation activity of cleaved PRP1 may be shared in specific bovine placentomal angiogenesis.
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[Journal Article]2010
Author(s)
Mishra B, Kizaki K, Koshi K, Ushizawa K, Takahashi T, Hosoe M, Sato T, Ito A, Hashizume K
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Journal Title
Reproductive Biology and Endocrinology
Volume: 8
Pages: 60
Peer Reviewed
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