| Project/Area Number |
06454158
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| Research Category |
Grant-in-Aid for General Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
General pharmacology
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| Research Institution | Kagawa Medical School |
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Principal Investigator |
KOBAYASHI Ryoji Kagawa Medical School, Faculty of Medicine, Professor, 医学部, 教授 (00020917)
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| Project Period (FY) |
1994 – 1995
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| Project Status |
Completed (Fiscal Year 1995)
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| Budget Amount *help |
¥7,100,000 (Direct Cost: ¥7,100,000)
Fiscal Year 1995: ¥1,400,000 (Direct Cost: ¥1,400,000)
Fiscal Year 1994: ¥5,700,000 (Direct Cost: ¥5,700,000)
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| Keywords | extracellular matrix protein / Ca^<2+> binding protein / Smith-Magenis syndrome / elasitn / EF hand protein / blood vessel / microfibril / inhibitor / カルシウム / 血管 / 細胞内情報伝達 |
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| Research Abstract |
A new extracellular matrix protein of 36kDa has been purified from bovine and porcine aorta. The protein, 36kDa microfibril associated glycoprotein (36kDa-MAGP), has a fibrinogen-like domain and contained the sequence Arg-Gly-Asp in the N-terminal region, which is the site for the association with cell and extracellular matrix. Immunoelection microscopy specified its location to elastin-microfibrils.
Using Ca^<2+>-dependent affinity chromatography on an isoquinoline sulfonamide (CKA1303) coupled agarose, we obtained pure form of 36kDa-MAGP.This compound should serve as a useful tool for clarifying the physiological roles of 36kDa-MAGP.During the synthesis and selection of S-100 protein antagonists derived from cinnamic acid and anthranilic acid, we discovered that N-acetyl anthranilic acid and 0-(3', 4'-dimethoxy cinnamoyl) salicilic acid strongly bind to 36kDa-MAGP.
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