1998 Fiscal Year Final Research Report Summary
Pathobiological role of 36 kDa microfibril-associated glycoprotein in Smith-Magenis syndrome.
| Project/Area Number |
09470044
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Pathological medical chemistry
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| Research Institution | Kagawa Medical University |
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Principal Investigator |
KOBAYASHI Ryoji Kagawa Medical University, Faculty of Medicine, Professor, 医学部, 教授 (00020917)
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| Co-Investigator(Kenkyū-buntansha) |
SUGANUMA Tatsuo Miyazaki Medical College, Faculty of Medicine, Professor, 医学部, 教授 (60115350)
OKABE Akinobu Kagawa Medical University, Faculty of Medicine, Professor, 医学部, 教授 (20093677)
MAETA Hajime Kagawa Medical University, Faculty of Medicine, Professor, 医学部, 教授 (00075508)
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| Project Period (FY) |
1997 – 1998
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| Keywords | extracellular matrix protein / Ca^<2+> binding protein / Smith-Magenis syndrome / elasith / EF hand protein / blood vessel / microfibril / inhibitor |
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| Research Abstract |
A new extracellular matrix protein of 36 kDa has been purified from bovine and porcine aorta. The protein, 36 kDa 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 (CKA 1303 ) coupled agarose, we obtained pure form of 36 kDa -MAGP.This compound should serve as a useful tool for clarifying the physiological roles of 36 kDa - 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 O - (3', 4' - dimethoxy cinnamoyl) salicilic acid strongly bind to 36kDa-MAGP.
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[Publications] Oyama.Y, Shishibori T, Yamashita K, Naya T, Nakagiri S, Maeta H, Kobayashi R: "Two distinct anti-allergic drugs, amlexanox and cromolyn, bind to the same kinds of calcium binding proteins, except calmodulin, in bovine lung extrat." Biochem.Biophys.Res.Commun.240. 341-347 (1997)
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[Publications] Shishibori T, Oyama Y, Matsushita O, Yamashita K, Furuichi H, Okabe A, Maeta H, Hata Y, Kobayashi R: "Three distinct anti-allergic drugs, amlexanox, cromolyn and tranilast, bind to S100A12 and S100A13 of the S100 protein family." Biochem.J.15 ; 338. 583-589 (1999)
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「研究成果報告書概要(欧文)」より
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