| Project/Area Number |
14572098
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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 |
医薬分子機能学
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| Research Institution | KITASATO UNIVERSITY |
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Principal Investigator |
OHTSUKI Kenzo Kitasato University, School of Allied Health Sciences, Professor, 医療衛生学部, 教授 (60124559)
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| Co-Investigator(Kenkyū-buntansha) |
KOMIYAMA Kanki Kitasato Institute, Pharmacology, Vice President, 臨床薬理研究所, 副部長 (00106676)
AKABOSHI Toru Kitasato University, School of Medicine, Associate Professor, 医学部, 助教授 (70159325)
FURUYA Teisuke Kitasato University, School of Allied Health Sciences, Lecture, 医療衛生学部, 講師 (70050630)
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| Project Period (FY) |
2002 – 2003
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| Project Status |
Completed (Fiscal Year 2003)
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| Budget Amount *help |
¥3,000,000 (Direct Cost: ¥3,000,000)
Fiscal Year 2003: ¥1,200,000 (Direct Cost: ¥1,200,000)
Fiscal Year 2002: ¥1,800,000 (Direct Cost: ¥1,800,000)
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| Keywords | Anti-inflammatory drug / Anti-allergic compound / Natural compound / Functional mediator / Selective inhibitor / Mechanical effect / Signal transduction / Clinical trial |
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| Research Abstract |
1. Characterization of glycyrrhizin (GL)-binding proteins in vitro:
The inhibitory effects of GL and choresterol 3'-sulfate (CH-3S) on the physiological activity of C3a (anaphylatoxin) generated from complement C3 were determined in vitro. It was found that (i) C3a is a GL-and CH-3S-binding protein ; and (ii) three compounds (GL, GA and CH-3S) inhibited the C3a-induced vascular permeability in a dose dependent manner.
2. Characerrization of the CK1-mediated phosphorylation of CH-3S-binding basic proteins in vitro:
The physiological interaction between CH-3S and Ca3 was examined in vitro. It was found that (i) C3a was phosphorylated by CK1 in the presence of CH-3S ; and (ii) this phosphorylation was reproduced by sulfatide instead of CH-3S ; and (iii) similar phosphorylation was observed with other basic proteins, such as HMG1, FGF-BP and myelin basic protein, in vitro.
3. Characterization of the CK2-mediated A-kinase (PKA) in vitro:
The physiological significance of the CK2-mediated phosphorylation of PKA on its activity was investigated in vitro. It was found that (i) phosphorylation of the R-subunit of PKA holoenzyme (C_2R_2) by CK2 resulted in the reduction of PKA activity ; and (ii) the CK2-mediated activation of PKA was selectively inhibited by quercetin (a CK2 inhibitor) in vitro.
4. Identification of lactoferrin (LF)-binding proteins:
At least four LF-binding proteins were isolated and purified from the LF fraction of bovine milk. Both p37 and p35 were identified as FGF-binding proteins. p17 and p15 was identified as lactogenin and angiogenin 1, respectively. These results suggest that LF may function as a carrier of these LF-binding functional proteins in vivo.
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