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Article: Mortalin-p53 interaction in cancer cells is stress dependent and constitutes a selective target for cancer therapy
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TitleMortalin-p53 interaction in cancer cells is stress dependent and constitutes a selective target for cancer therapy
 
AuthorsLu, WJ1
Lee, NP1
Kaul, SC3
Lan, F2
Poon, RTP1
Wadhwa, R3
Luk, JM4 1
 
Keywordscancer
mortalin-p53 interaction
stress
target
therapy
 
Issue Date2011
 
PublisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/cdd
 
CitationCell Death And Differentiation, 2011, v. 18 n. 6, p. 1046-1056 [How to Cite?]
DOI: http://dx.doi.org/10.1038/cdd.2010.177
 
AbstractStress protein mortalin is a multifunctional protein and is highly expressed in cancers. It has been shown to interact with tumor suppressor protein-p53 (both wild and mutant types) and inactivates its transcriptional activation and apoptotic functions in cancer cells. In the present study, we found that, unlike most of the cancer cells, HepG2 hepatoma lacked mortalin-p53 interaction. We demonstrate that the mortalin-p53 interaction exists in cancer cells that are either physiologically stressed (frequently associated with p53 mutations) or treated with stress-inducing chemicals. Targeting mortalin-p53 interaction with either mortalin small hairpin RNA or a chemical or peptide inhibitor could induce p53-mediated tumor cell-specific apoptosis in hepatocellular carcinoma; p53-null hepatoma or normal hepatocytes remain unaffected. © 2011 Macmillan Publishers Limited All rights reserved.
 
ISSN1350-9047
2012 Impact Factor: 8.371
2012 SCImago Journal Rankings: 3.725
 
DOIhttp://dx.doi.org/10.1038/cdd.2010.177
 
PubMed Central IDPMC3131943
 
ISI Accession Number IDWOS:000290379300013
 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorLu, WJ
 
dc.contributor.authorLee, NP
 
dc.contributor.authorKaul, SC
 
dc.contributor.authorLan, F
 
dc.contributor.authorPoon, RTP
 
dc.contributor.authorWadhwa, R
 
dc.contributor.authorLuk, JM
 
dc.date.accessioned2011-07-27T01:37:00Z
 
dc.date.available2011-07-27T01:37:00Z
 
dc.date.issued2011
 
dc.description.abstractStress protein mortalin is a multifunctional protein and is highly expressed in cancers. It has been shown to interact with tumor suppressor protein-p53 (both wild and mutant types) and inactivates its transcriptional activation and apoptotic functions in cancer cells. In the present study, we found that, unlike most of the cancer cells, HepG2 hepatoma lacked mortalin-p53 interaction. We demonstrate that the mortalin-p53 interaction exists in cancer cells that are either physiologically stressed (frequently associated with p53 mutations) or treated with stress-inducing chemicals. Targeting mortalin-p53 interaction with either mortalin small hairpin RNA or a chemical or peptide inhibitor could induce p53-mediated tumor cell-specific apoptosis in hepatocellular carcinoma; p53-null hepatoma or normal hepatocytes remain unaffected. © 2011 Macmillan Publishers Limited All rights reserved.
 
dc.description.naturelink_to_OA_fulltext
 
dc.identifier.citationCell Death And Differentiation, 2011, v. 18 n. 6, p. 1046-1056 [How to Cite?]
DOI: http://dx.doi.org/10.1038/cdd.2010.177
 
dc.identifier.citeulike8670670
 
dc.identifier.doihttp://dx.doi.org/10.1038/cdd.2010.177
 
dc.identifier.epage1056
 
dc.identifier.hkuros188088
 
dc.identifier.isiWOS:000290379300013
 
dc.identifier.issn1350-9047
2012 Impact Factor: 8.371
2012 SCImago Journal Rankings: 3.725
 
dc.identifier.issue6
 
dc.identifier.pmcidPMC3131943
 
dc.identifier.pmid21233847
 
dc.identifier.scopuseid_2-s2.0-79955827220
 
dc.identifier.spage1046
 
dc.identifier.urihttp://hdl.handle.net/10722/135550
 
dc.identifier.volume18
 
dc.languageeng
 
dc.publisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/cdd
 
dc.publisher.placeUnited Kingdom
 
dc.relation.ispartofCell Death and Differentiation
 
dc.relation.referencesReferences in Scopus
 
dc.subject.meshApoptosis
 
dc.subject.meshCarcinoma, Hepatocellular - drug therapy - genetics - metabolism
 
dc.subject.meshHSP70 Heat-Shock Proteins - antagonists and inhibitors - metabolism
 
dc.subject.meshStress, Physiological
 
dc.subject.meshTumor Suppressor Protein p53 - genetics - metabolism
 
dc.subjectcancer
 
dc.subjectmortalin-p53 interaction
 
dc.subjectstress
 
dc.subjecttarget
 
dc.subjecttherapy
 
dc.titleMortalin-p53 interaction in cancer cells is stress dependent and constitutes a selective target for cancer therapy
 
dc.typeArticle
 
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<contributor.author>Lan, F</contributor.author>
<contributor.author>Poon, RTP</contributor.author>
<contributor.author>Wadhwa, R</contributor.author>
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Author Affiliations
  1. The University of Hong Kong Li Ka Shing Faculty of Medicine
  2. Stanford University School of Medicine
  3. National Institute of Advanced Industrial Science and Technology
  4. National University of Singapore