| Project/Area Number |
16580235
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Applied animal science
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| Research Institution | National Institute of Agrobiological Sciences |
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Principal Investigator |
TAKAHASHI Toru National Institute of Agrobiological Sciences, Senior Researcher, 動物科学研究領域・生殖機構研究ユニット, 主任研究員 (20355738)
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| Co-Investigator(Kenkyū-buntansha) |
HASHIZUME Kazuyoshi Iwate University, Faculty of Agriculture, Professor, 農学部, 教授 (10355737)
金山 佳奈子 独立行政法人農業生物資源研究所, 発生分化研究グループ, 研究員 (40391578)
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| Project Period (FY) |
2004 – 2006
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| Project Status |
Completed (Fiscal Year 2006)
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| Budget Amount *help |
¥3,700,000 (Direct Cost: ¥3,700,000)
Fiscal Year 2006: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 2005: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 2004: ¥2,500,000 (Direct Cost: ¥2,500,000)
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| Keywords | bovine / placenta / prolactin / matrix / alkaline phosphatase / fusion protein / collagen / type IV / プロラクチン関連タンパク質 / Nb2 / 7Sドメイン / NC1ドメイン |
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| Research Abstract |
The bovine placenta produces an array of proteins structurally similar to pituitary prolactin (PRL). At least ten genes of the bovine placental PRL family, including bovine placental lactogen (bPL) and ten bovine PRL-related proteins bPRP-I to-XI), encode hormones/cytokines predicted to be involved in the establishment and maintenance of pregnancy. Targets and biological roles for most members of the bovine PRL family have yet to be specified. This study focused on three members of bovine PRL family, bPL, bPRP-I and bPRP-VI. An alkaline phosphatase (AP) tagging strategy was used to monitor interactions of the ligands with their targets. AP-bPRP-I and APbPRP-VI specifically bound to tissue sections of the bovine placentome. AP-bPRP-I and AP-bPRP-VI binding within the placentome mimicked the distribution of the extracellular matrix (ECM). Consequently, AP fusion protein binding to individual extracellular matrix components (heparin, laminin, fibronectin, type I collagen and type IV collagen) was evaluated. AP-bPRP-I specifically bound to type IV collagen, but not to the other ECM components. AP-bPRP-VI exhibited weak interactions with ECM components, while AP-bPL and AP did not show significant binding to any of the ECM components. Binding of AP-bPRP-I to type IV collagen was concentration dependent, influenced by salt concentrations, and specific to the N-terminal cross-linking domain (7S) of type IV collagen but not its triple-helical domain. The interaction of bPRP-I with type IV collagen suggests that bPRP-I accumulates in the extracellular matrix where it likely acts on cells traversing the bovine placentome.
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