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Article: Quantitative nucleolar proteomics reveals nuclear re-organization during stress-induced senescence in mouse fibroblast
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TitleQuantitative nucleolar proteomics reveals nuclear re-organization during stress-induced senescence in mouse fibroblast
 
AuthorsKar, B2
Liu, B1
Zhou, Z1
Lam, YW2
 
Issue Date2011
 
PublisherBioMed Central Ltd. The Journal's web site is located at http://www.biomedcentral.com/bmccellbiol/
 
CitationBMC Cell Biology, 2011, v. 12, article no. 33 [How to Cite?]
DOI: http://dx.doi.org/10.1186/1471-2121-12-33
 
AbstractBACKGROUND: Nucleolus is the most prominent mammalian organelle within the nucleus which is also the site for ribosomal biogenesis. There have been many reports indicating the involvement of nucleolus in the process of aging. Several proteins related to aging have been shown to localize in the nucleolus, which suggests the role of this organelle in senescence. RESULTS: In this study, we used quantitative mass spectrometry to map the flux of proteins into and out of the nucleolus during the induction of senescence in cultured mammalian cells. Changes in the abundance of 344 nucleolar proteins in sodium butyrate-induced senescence in NIH3T3 cells were studied by SILAC (stable isotope labeling by amino acids in cell culture)-based mass spectrometry. Biochemically, we have validated the proteomic results and confirmed that B23 (nucleophosmin) protein was down-regulated, while poly (ADP-ribose) polymerase (PARP) and nuclear DNA helicase II (NDH II/DHX9/RHA) were up-regulated in the nucleolus upon treatment with sodium butyrate. Accumulation of chromatin in the nucleolus was also observed, by both proteomics and microscopy, in sodium butyrate-treated cells. Similar observations were found in other models of senescence, namely, in mitoxantrone- (MTX) treated cells and primary fibroblasts from the Lamin A knockout mice. CONCLUSION: Our data indicate an extensive nuclear organization during senescence and suggest that the redistribution of B23 protein and chromatin can be used as an important marker for senescence.
 
ISSN1471-2121
2013 Impact Factor: 2.844
2013 SCImago Journal Rankings: 1.605
 
DOIhttp://dx.doi.org/10.1186/1471-2121-12-33
 
PubMed Central IDPMC3163619
 
ISI Accession Number IDWOS:000294421400001
Funding AgencyGrant Number
University Grant Council, Hong Kong160670
Research Grant Council, Hong KongHKU7655/06M
CRF HKU3/07C
Funding Information:

We would like to thank Dr. Laura Trinkle-Mulchay (Dept. Cellular & Molecular Medicine, University of Ottawa) for critically reading the manuscript. We would also like to thank members of the Yun Lam laboratory for discussions and Kenneth Lau for his technical assistance. This work was supported by the General Research Fund (GRF project number 160670) from the University Grant Council, Hong Kong, HKU7655/06M and CRF HKU3/07C from the Research Grant Council, Hong Kong.

 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorKar, B
 
dc.contributor.authorLiu, B
 
dc.contributor.authorZhou, Z
 
dc.contributor.authorLam, YW
 
dc.date.accessioned2012-05-29T06:05:08Z
 
dc.date.available2012-05-29T06:05:08Z
 
dc.date.issued2011
 
dc.description.abstractBACKGROUND: Nucleolus is the most prominent mammalian organelle within the nucleus which is also the site for ribosomal biogenesis. There have been many reports indicating the involvement of nucleolus in the process of aging. Several proteins related to aging have been shown to localize in the nucleolus, which suggests the role of this organelle in senescence. RESULTS: In this study, we used quantitative mass spectrometry to map the flux of proteins into and out of the nucleolus during the induction of senescence in cultured mammalian cells. Changes in the abundance of 344 nucleolar proteins in sodium butyrate-induced senescence in NIH3T3 cells were studied by SILAC (stable isotope labeling by amino acids in cell culture)-based mass spectrometry. Biochemically, we have validated the proteomic results and confirmed that B23 (nucleophosmin) protein was down-regulated, while poly (ADP-ribose) polymerase (PARP) and nuclear DNA helicase II (NDH II/DHX9/RHA) were up-regulated in the nucleolus upon treatment with sodium butyrate. Accumulation of chromatin in the nucleolus was also observed, by both proteomics and microscopy, in sodium butyrate-treated cells. Similar observations were found in other models of senescence, namely, in mitoxantrone- (MTX) treated cells and primary fibroblasts from the Lamin A knockout mice. CONCLUSION: Our data indicate an extensive nuclear organization during senescence and suggest that the redistribution of B23 protein and chromatin can be used as an important marker for senescence.
 
dc.description.naturepublished_or_final_version
 
dc.identifier.citationBMC Cell Biology, 2011, v. 12, article no. 33 [How to Cite?]
DOI: http://dx.doi.org/10.1186/1471-2121-12-33
 
dc.identifier.citeulike9686452
 
dc.identifier.doihttp://dx.doi.org/10.1186/1471-2121-12-33
 
dc.identifier.hkuros194500
 
dc.identifier.isiWOS:000294421400001
Funding AgencyGrant Number
University Grant Council, Hong Kong160670
Research Grant Council, Hong KongHKU7655/06M
CRF HKU3/07C
Funding Information:

We would like to thank Dr. Laura Trinkle-Mulchay (Dept. Cellular & Molecular Medicine, University of Ottawa) for critically reading the manuscript. We would also like to thank members of the Yun Lam laboratory for discussions and Kenneth Lau for his technical assistance. This work was supported by the General Research Fund (GRF project number 160670) from the University Grant Council, Hong Kong, HKU7655/06M and CRF HKU3/07C from the Research Grant Council, Hong Kong.

 
dc.identifier.issn1471-2121
2013 Impact Factor: 2.844
2013 SCImago Journal Rankings: 1.605
 
dc.identifier.pmcidPMC3163619
 
dc.identifier.pmid21835027
 
dc.identifier.scopuseid_2-s2.0-80051504639
 
dc.identifier.urihttp://hdl.handle.net/10722/147636
 
dc.identifier.volume12, article no. 33
 
dc.languageeng
 
dc.publisherBioMed Central Ltd. The Journal's web site is located at http://www.biomedcentral.com/bmccellbiol/
 
dc.publisher.placeUnited Kingdom
 
dc.relation.ispartofBMC Cell Biology
 
dc.relation.referencesReferences in Scopus
 
dc.rightsBMC Cell Biology. Copyright © BioMed Central Ltd.
 
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License
 
dc.subject.meshAging - metabolism
 
dc.subject.meshCell Nucleolus - metabolism
 
dc.subject.meshCell Nucleus - metabolism
 
dc.subject.meshFibroblasts - metabolism
 
dc.subject.meshNuclear Proteins - analysis - metabolism
 
dc.titleQuantitative nucleolar proteomics reveals nuclear re-organization during stress-induced senescence in mouse fibroblast
 
dc.typeArticle
 
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Author Affiliations
  1. The University of Hong Kong
  2. City University of Hong Kong