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Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Life Science / Faculty of Advanced Life Science >
Peer-reviewed Journal Articles, etc >
Immunological Detection and Characterization of Poly(A) Polymerase, Poly(A)-Binding Protein and Cytoplasmic Polyadenylation Element-Binding Protein in Goldfish and Xenopus Oocytes
| Title: | Immunological Detection and Characterization of Poly(A) Polymerase, Poly(A)-Binding Protein and Cytoplasmic Polyadenylation Element-Binding Protein in Goldfish and Xenopus Oocytes |
| Authors: | Nakahata, Shingo Browse this author | | Mita, Koichi Browse this author | | Katsu, Yoshinao Browse this author | | Nagahama, Yoshitaka Browse this author | | Yamashita, Masakane Browse this author |
| Issue Date: | Apr-2001 |
| Publisher: | 日本動物学会 |
| Journal Title: | Zoological Science |
| Volume: | 18 |
| Issue: | 3 |
| Start Page: | 337 |
| End Page: | 343 |
| Publisher DOI: | 10.2108/zsj.18.337 |
| Abstract: | Cytoplasmic polyadenylation regulates translational activation of dormant cyclin B1 mRNA stored in immature oocytes, a process required for the initiation of oocyte maturation in goldfish and Xenopus. As a first step towards understanding the molecular mechanisms of translational activation of cyclin B1 during oocyte maturation, we have isolated cDNA clones encoding proteins involved in cytoplasmic polyadenylation and produced specific antibodies against recombinant proteins. These include poly(A) polymerase (PAP), poly(A)-binding protein (PABP) and cytoplasmic polyadenylation element-binding protein (CPEB). Monoclonal antibodies raised against goldfish PAP recognized several forms of PAP in goldfish and Xenopus oocytes. Besides ordinary PAPs with high molecular weight (ca. 100 kDa), the antibodies also detected those with low molecular weight (ca. 40 kDa) that are present specifically in the cytoplasm, raising new players that might be responsible for cytoplasmic polyadenylation. An antibody against goldfish PABP showed for the first time in Xenopus oocytes the protein expression of PABPII, another PABP distinct from the well-characterized PABPI. Monoclonal antibodies raised against Xenopus CPEB recognized both unphosphorylated 62-kDa and phosphorylated 64-kDa forms but did not cross-react with goldfish CPEB, which was specifically detected by anti-goldfish CPEB monoclonal antibodies produced previously. The cDNAs, recombinant proteins and antibodies produced in this study are expected to provide useful tools for investigating the regulatory mechanisms of cyclin B1 translation during oocyte maturation in goldfish and Xenopus. |
| Rights: | (c) 日本動物学会 / 本文献の公開は著者の意思に基づくものである |
| Relation: | http://www.bioone.org/perlserv/?request=get-archive&issn=0289-0003 |
| Type: | article |
| URI: | http://hdl.handle.net/2115/32944 |
| Appears in Collections: | 生命科学院・先端生命科学研究院 (Graduate School of Life Science / Faculty of Advanced Life Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 山下 正兼
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