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Article: Mortalin-p53 interaction in cancer cells is stress dependent and constitutes a selective target for cancer therapy

TitleMortalin-p53 interaction in cancer cells is stress dependent and constitutes a selective target for cancer therapy
Authors
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
Citation
Cell Death And Differentiation, 2011, v. 18 n. 6, p. 1046-1056 How to Cite?
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.
Persistent Identifierhttp://hdl.handle.net/10722/135550
ISSN
2014 Impact Factor: 8.184
PubMed Central ID
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLu, WJen_HK
dc.contributor.authorLee, NPen_HK
dc.contributor.authorKaul, SCen_HK
dc.contributor.authorLan, Fen_HK
dc.contributor.authorPoon, RTPen_HK
dc.contributor.authorWadhwa, Ren_HK
dc.contributor.authorLuk, JMen_HK
dc.date.accessioned2011-07-27T01:37:00Z-
dc.date.available2011-07-27T01:37:00Z-
dc.date.issued2011en_HK
dc.identifier.citationCell Death And Differentiation, 2011, v. 18 n. 6, p. 1046-1056en_HK
dc.identifier.issn1350-9047en_HK
dc.identifier.urihttp://hdl.handle.net/10722/135550-
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.en_HK
dc.languageengen_US
dc.publisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/cdden_HK
dc.relation.ispartofCell Death and Differentiationen_HK
dc.subjectcanceren_HK
dc.subjectmortalin-p53 interactionen_HK
dc.subjectstressen_HK
dc.subjecttargeten_HK
dc.subjecttherapyen_HK
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.titleMortalin-p53 interaction in cancer cells is stress dependent and constitutes a selective target for cancer therapyen_HK
dc.typeArticleen_HK
dc.identifier.emailLee, NP: nikkilee@hku.hken_HK
dc.identifier.emailPoon, RTP: poontp@hkucc.hku.hken_HK
dc.identifier.emailLuk, JM: jmluk@hkucc.hku.hken_HK
dc.identifier.authorityLee, NP=rp00263en_HK
dc.identifier.authorityPoon, RTP=rp00446en_HK
dc.identifier.authorityLuk, JM=rp00349en_HK
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1038/cdd.2010.177en_HK
dc.identifier.pmid21233847-
dc.identifier.pmcidPMC3131943-
dc.identifier.scopuseid_2-s2.0-79955827220en_HK
dc.identifier.hkuros188088en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-79955827220&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume18en_HK
dc.identifier.issue6en_HK
dc.identifier.spage1046en_HK
dc.identifier.epage1056en_HK
dc.identifier.isiWOS:000290379300013-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridLu, WJ=35187521100en_HK
dc.identifier.scopusauthoridLee, NP=7402722690en_HK
dc.identifier.scopusauthoridKaul, SC=7403092602en_HK
dc.identifier.scopusauthoridLan, F=36349345200en_HK
dc.identifier.scopusauthoridPoon, RTP=7103097223en_HK
dc.identifier.scopusauthoridWadhwa, R=7006876025en_HK
dc.identifier.scopusauthoridLuk, JM=7006777791en_HK
dc.identifier.citeulike8670670-

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