2020 Fiscal Year Final Research Report
Functional analysis of muscle proteins in the myostracum formed on the shell surface attached to the adductor muscle
| Project/Area Number |
19K22331
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| Research Category |
Grant-in-Aid for Challenging Research (Exploratory)
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| Allocation Type | Multi-year Fund |
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| Review Section |
Medium-sized Section 40:Forestry and forest products science, applied aquatic science, and related fields
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| Research Institution | Mie University |
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Principal Investigator |
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| Co-Investigator(Kenkyū-buntansha) |
鈴木 道生 東京大学, 大学院農学生命科学研究科(農学部), 准教授 (10647655)
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| Project Period (FY) |
2019-06-28 – 2021-03-31
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| Keywords | 二枚貝 / 光輝層 / 炭酸カルシウム結晶 / アラゴナイト / パラミオシン / アコヤガイ / 閉殻筋 / 貝殻 |
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| Outline of Final Research Achievements |
Myostracum, columnar calcium crystals, is formed on shell surfaces attached to adductor muscles. It is unknown how the myostracum is formed. We revealed that the myostracum contains some muscle proteins, such as paramyosin, tropomyosin, and calponin. In vitro calcium crystallization analysis in the presence of paramyosin produced columnar aragonite crystals like myostracum. Immunostaining using the anti-paramyosin antibody against the shells showed that paramyosin is localized only in the myostracum. Our study raised the possibility that paramyosin participates in the formation of myostracum.
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| Free Research Field |
生体高分子化学
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| Academic Significance and Societal Importance of the Research Achievements |
二枚貝は強い力で貝殻をとじ続けることができるが、これは閉殻筋が貝殻に強力に接着しているからである。閉殻筋と貝殻の接着面に形成される光輝層が両者の接着に重要であると考えられているが、光輝層の形成メカニズムは分かっていない。本研究では光輝層の形成に筋肉タンパク質であるパラミオシンが関与している可能性が明らかとなった。これは閉殻筋と貝殻の接着メカニズムの解明につながるものである。
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