Project/Area Number |
18570213
|
Research Category |
Grant-in-Aid for Scientific Research (C)
|
Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Developmental biology
|
Research Institution | The Institute of Physical and Chemical Research |
Principal Investigator |
YUKIHIKO Kubota The Institute of Physical and Chemical Research, Laboratory for cell migration, Research Scientist (70333325)
|
Project Period (FY) |
2006 – 2007
|
Project Status |
Completed (Fiscal Year 2007)
|
Budget Amount *help |
¥4,140,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥540,000)
Fiscal Year 2007: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
Fiscal Year 2006: ¥1,800,000 (Direct Cost: ¥1,800,000)
|
Keywords | fibulin-1 / type IV collagen / NC1 domain / nidogen-1 / organogenesis / suppressor / C. elegans / basement membrane / フイビュリンー1 / ナイドジェン / サプレッサ-解析 / 形態形成 / 発生遺伝 / 細胞認識 / 基底膜 |
Research Abstract |
Fibulin family of extracellular matrix (ECM) component is important for maintenance of various tissue in both vertebrate and invertebrate. However, the mechanisms by which these molecule modulate the ECM during development are mostly unexplored. The C. eleransfibulin-1C is secreted from intestine and localize to the gonadal basement membrane where it promote gonadal elongation. In this work, we performed suppressor screenings of fibulin-1 (tk45) null mutant by using EMS mutagenesis. In this screening, we identified a suppressor mutation tk75that specific mutation in the NC1 domain of the type IV collagen al component EMB-9 bypass the requirement of fibulin-1C in the gonadal elongation. In the absence of fibulin-1C, some ECM molecules such as EMB-9 and nidogen-1 localiiation of the gonadal basement membrane were diminished. However, the mutant EMB-9 (tk75) localized normally in the fibulin-1 (tk45) null background. Nidogen-1 localization did not diminish in emb-9 (tk75); fb1-1 (tk45) background. The mutation was localized in the interface of the NC1 domain to allow to make hexamer. We propose that the interface region may have important functions that stabilize type IV collagen network and promote gonadal elongation. We speculate that fibulin-1C may module the function of NC1 domain of type IV collagen to allow the maintenance of gonadal basement membrane structure and promotion of gonadal elongation.
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