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Immunocytochemical localization of nucleophosmin and RH-II/Gu protein in nucleoli of HeLa cells after treatment with actinomycin D
K Smetana, R Busch, PK Chan, K Jr Smetana, H Busch
Jazyk angličtina Země Německo
Typ dokumentu práce podpořená grantem
Grantová podpora
NC5929
MZ0
CEP - Centrální evidence projektů
PubMed
11482378
Knihovny.cz E-zdroje
- MeSH
- buněčné jadérko * chemie MeSH
- daktinomycin farmakologie MeSH
- HeLa buňky MeSH
- imunohistochemie MeSH
- inhibitory syntézy nukleových kyselin farmakologie MeSH
- jaderné proteiny * analýza chemie MeSH
- lidé MeSH
- RNA-helikasy * analýza chemie MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- práce podpořená grantem MeSH
HeLa cells were studied with the use of light microscopical immunocytochemistry to obtain more information on the nucleolar localization of nucleophosmin (B23 protein) and RH-II/Gu protein. In control cells these proteins are colocalized. After structural rearrangement of nucleoli induced by actinomycin D, nucleophosmin was present in the nucleolar periphery and nucleolar peripheral caps. In contrast, RH-II/Gu protein was observed mainly in central regions of nucleoli as a compact body. However, in some nucleoli the proteins colocalized in a small portion of the peripheral nucleolar cap. The proteins were also colocalized in micronucleoli but occasionally RH-II/Gu protein was absent or both proteins were not present
Anatomical Institute 1st Medical Faculty of the Charles University Prague Czech Republic
Department of Pharmacology Baylor College of Medicine Houston USA
Institute of Hematology and Blood Transfusion Prague Czech Republic
Obsahuje tabulky
Bibliografie atd.Literatura
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- $a HeLa cells were studied with the use of light microscopical immunocytochemistry to obtain more information on the nucleolar localization of nucleophosmin (B23 protein) and RH-II/Gu protein. In control cells these proteins are colocalized. After structural rearrangement of nucleoli induced by actinomycin D, nucleophosmin was present in the nucleolar periphery and nucleolar peripheral caps. In contrast, RH-II/Gu protein was observed mainly in central regions of nucleoli as a compact body. However, in some nucleoli the proteins colocalized in a small portion of the peripheral nucleolar cap. The proteins were also colocalized in micronucleoli but occasionally RH-II/Gu protein was absent or both proteins were not present
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