- Tytuł:
- Analysis of Water-Soluble Proteins by Two-Dimensional Electrophoresis in the Encystment Process of Colpoda cucullus Nag-1 and Cytoskeletal Dynamics
- Autorzy:
-
Sogame, Yoichiro
Kojima, Katsuhiko
Takeshita, Toshikazu
Kikuchi, Shiho
Shimada, Yuto
Nakamura, Rikiya
Arikawa, Mikihiko
Miyata, Seiji
Kinoshita, Eiji
Suizu, Futoshi
Matsuoka, Tatsuomi - Powiązania:
- https://bibliotekanauki.pl/articles/52089860.pdf
- Data publikacji:
- 2020
- Wydawca:
- Uniwersytet Jagielloński. Wydawnictwo Uniwersytetu Jagiellońskiego
- Tematy:
-
resting cyst formation
microtubules
actin
lepidosomes
resorption of cilia - Opis:
- Assays of protein contained in water-soluble fraction of encysting cells Colpoda cucullus Nag-1 by two-dimensional electrophoresis (2-D PAGE) and mass spectrometry (MS) revealed that the amount of β-tubulin abruptly increased in 2.5–10 h after encystment induction. Judging from the results that total α-tubulin content did not decrease much until 12 h after encystment induction, the result indicates that disassembly of microtubules may occur soon after encystment is induced. Therefore, we tried to visualize dynamics of microtubules. Immunofluorescence microscopy using anti-α-tubulin antibody indicated that disassembly of axonemal microtubules of cilia became within 1.5 h after encystment induction, and resorbed in 3 days. Although the cytoplasmic microtubules failed to be visualized clearly, encystmentdependent globulation of cells was promoted by taxol, an inhibitor of disassembly of microtubules. It is possible that a temporary formation of cytoplasmic microtubules may be involved in cell globulation. The phosphorylation level of actin (43 kDa) became slightly elevated just after encystment induction. Lepidosomes, the sticky small globes surrounding encysting cells, were vividly stained with Acti-stain 555 phalloidin, suggesting that 43-kDa actin or its homologues may be contained in lepidosomes.
- Źródło:
-
Acta Protozoologica; 2020, 59, 3-4; 107-120
0065-1583
1689-0027 - Pojawia się w:
- Acta Protozoologica
- Dostawca treści:
- Biblioteka Nauki
Artykuł