Preparation of an active recombinant peptide of crustacean androgenic gland hormone, a heterodimeric glycopeptide.
Project/Area Number |
21780186
|
Research Category |
Grant-in-Aid for Young Scientists (B)
|
Allocation Type | Single-year Grants |
Research Field |
General fisheries
|
Research Institution | Kanagawa University |
Principal Investigator |
OHIRA Tsuyoshi Kanagawa University, 理学部, 助教 (10361809)
|
Project Period (FY) |
2009 – 2010
|
Project Status |
Completed (Fiscal Year 2010)
|
Budget Amount *help |
¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2010: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2009: ¥2,860,000 (Direct Cost: ¥2,200,000、Indirect Cost: ¥660,000)
|
Keywords | 造雄腺ホルモン / オカダンゴムシ / オニテナガエビ / 十脚目 / 等脚目 / 甲殻類 / 性転換 / 性分化 |
Research Abstract |
The sex differentiation in crustaceans is known to be controlled by a peptide hormone called androgenic gland hormone (AGH). The primary structure of the terrestrial isopod Armadillidium vulgare AGH (Arv-AGH) was finally determined to be a heterodimeric glycoprotein. An N-linked glycan moiety in the mature Arv-AGH was found to be essential for biological activity. Therefore, in this study, a recombinant AGH with a glycan moiety was produced using a baculovirus expression system. Insect Sf9 cells were infected with a recombinant baculovirus expression vector containing an Arv-AGH cDNA insert and subsequently recombinant Arv-AGH was expressed. In Western blot analysis using an anti-Arv-AGH antibody, immunoreactive band of a glycosylated recombinant Arv-AGH was detected. Finally, a cDNA encoding AGH-like peptide (Mar-IAG) was cloned from the giant freshwater prawn Macrobrachium rosenbergii and subsequently a recombinant Mar-IAG with a glycan moiety was expressed by the same methods as recombinant Arv-AGH.
|
Report
(3 results)
Research Products
(13 results)