2006
DOI: 10.1016/j.prp.2006.02.002
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HSP60 expression during carcinogenesis: Where is the pilot?

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Cited by 4 publications
(3 citation statements)
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“…For example, elevated levels of this protein in tumor cells have been linked to: (i) ability to survive apoptotic stimuli; (ii) loss of replicative senescence; (iii) uncontrolled proliferation; and (iv) neoplastic transformation. 17,[43][44][45] In addition, it has been shown in in vitro experiments that Hsp60 knockdown arrests osteosarcoma cell growth. 15 Likewise, inhibition of Hsp60 expression by short hairpin RNA plasmids stopped tumor cell growth.…”
Section: Hsp60 and Tumor Growthmentioning
confidence: 99%
“…For example, elevated levels of this protein in tumor cells have been linked to: (i) ability to survive apoptotic stimuli; (ii) loss of replicative senescence; (iii) uncontrolled proliferation; and (iv) neoplastic transformation. 17,[43][44][45] In addition, it has been shown in in vitro experiments that Hsp60 knockdown arrests osteosarcoma cell growth. 15 Likewise, inhibition of Hsp60 expression by short hairpin RNA plasmids stopped tumor cell growth.…”
Section: Hsp60 and Tumor Growthmentioning
confidence: 99%
“…Since it was realized that chaperones may be at the center of mechanisms that cause cell damage, tissue abnormalities, and disease, it was also realized that therapeutic means ought to use chaperones either as remedies or as targets for treatment agents [2], and we, in our research, have focused on the chaperonin HSP60 (also termed Cpn60 or, accordingly to the new terminology, HSPD1) [26][27][28]. This therapeutic approach, involving chaperones as central players or targets, i.e., chaperonotherapy, includes two modalities.…”
Section: Chaperonopathies and Chaperonotherapymentioning
confidence: 99%
“…Heat shock proteins (HSPs) are a group of highly conserved proteins that help protect cells from various type of stress (heat, cold, and abnormal levels of glucose or oxygen). ey help the correct folding of many proteins and protect cells from deleterious consequences as protein misfolding, premature degradation, or aggregation [3][4][5][6]. HSPs normally support other protein functions in normal cells, but they may be present at high levels in cancer cells.…”
Section: Introductionmentioning
confidence: 99%