Targeting protein acetylation for improving cancer therapy.

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dc.contributor.authorDwarakanath, B Sen_US
dc.contributor.authorVerma, Amiten_US
dc.contributor.authorBhatt, A Nen_US
dc.contributor.authorParmar, V Sen_US
dc.contributor.authorRaj, H Gen_US
dc.date.accessioned2008-07-30en_US
dc.date.accessioned2009-05-27T07:27:36Z
dc.date.available2008-07-30en_US
dc.date.available2009-05-27T07:27:36Z
dc.date.issued2008-07-30en_US
dc.description80 references.en_US
dc.description.abstractAcetylation is one of the most important post-translational modification of proteins determining the structure, function and intracellular localization that plays an important role in the signal transduction pathways related to diverse cell functions, both during unstimulated and stress conditions. Protein acetylation in cells is regulated by a co-ordinated action of histone acetyl transferases (HAT) and histone deacetylases(HDAC) that ensures the maintenance of homeostasis and execution of activities related to damage response viz. DNA repair, cell cycle delay, apoptosis and senescence. Since inhibition of histone deacetylation, stalls the progress of many nuclear events including proliferation and damage response events on the one hand and the levels of deacetylases are elevated in many tumours on the other. Histone deacetylase has been among the targets for the development of anticancer drugs and adjuvant. The recent observation showing acetylation of proteins by calreticulin (an endoplasmic reticulum resident protein) with a high efficiency when polyphenolic acetates are the acetyl group donating molecules and acetyl CoA as weak substrate extends the realm of protein acetylation beyond HAT/HDAC combination. Elucidation of the relative roles of HAT/HDAC mediated acetylation viz. a calreticulin mediated acetylation in cell function under a variety of stress conditions would hold key to the design of drugs targeting protein acetylation system.en_US
dc.description.affiliationInstitute of Nuclear Medicine & Allied Sciences, University of Delhi, Delhi, India. bsd@inmas.orgen_US
dc.identifier.citationDwarakanath BS, Verma A, Bhatt AN, Parmar VS, Raj HG. Targeting protein acetylation for improving cancer therapy. Indian Journal of Medical Research. 2008 Jul; 128(1): 13-21en_US
dc.identifier.urihttps://imsear.searo.who.int/handle/123456789/20795
dc.language.isoengen_US
dc.source.urihttps://icmr.nic.in/ijmr/ijmr.htmen_US
dc.subject.meshAcetylationen_US
dc.subject.meshAntineoplastic Agents --therapeutic useen_US
dc.subject.meshHistones --metabolismen_US
dc.subject.meshHumansen_US
dc.subject.meshNeoplasms --drug therapyen_US
dc.subject.meshSignal Transduction --drug effectsen_US
dc.titleTargeting protein acetylation for improving cancer therapy.en_US
dc.typeJournal Articleen_US
dc.typeReviewen_US
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