Unknown

Dataset Information

0

The antileishmanial activity of isoforms 6- and 8-selective histone deacetylase inhibitors.


ABSTRACT: Histone deacetylase inhibitors (HDACi) pleiotropy is largely due to their nonselective inhibition of various cellular HDAC isoforms. Connecting inhibition of a specific isoform to biological responses and/or phenotypes is essential toward deconvoluting HDACi pleiotropy. The contribution of classes I and II HDACs to the antileishmanial activity of HDACi was investigated using the amastigote and promastigote forms of Leishmania donovani. We observed that the antileishmanial activities of HDACi are largely due to the inhibition of HDAC6-like activity. This observation could facilitate the development of HDACi as antileishmanial agents.

SUBMITTER: Sodji Q 

PROVIDER: S-EPMC4225773 | biostudies-literature | 2014 Oct

REPOSITORIES: biostudies-literature

altmetric image

Publications

The antileishmanial activity of isoforms 6- and 8-selective histone deacetylase inhibitors.

Sodji Quaovi Q   Patil Vishal V   Jain Surendra S   Kornacki James R JR   Mrksich Milan M   Tekwani Babu L BL   Oyelere Adegboyega K AK  

Bioorganic & medicinal chemistry letters 20140904 20


Histone deacetylase inhibitors (HDACi) pleiotropy is largely due to their nonselective inhibition of various cellular HDAC isoforms. Connecting inhibition of a specific isoform to biological responses and/or phenotypes is essential toward deconvoluting HDACi pleiotropy. The contribution of classes I and II HDACs to the antileishmanial activity of HDACi was investigated using the amastigote and promastigote forms of Leishmania donovani. We observed that the antileishmanial activities of HDACi are  ...[more]

Similar Datasets

| S-EPMC2593472 | biostudies-other
| S-EPMC3403710 | biostudies-literature
| S-EPMC2818366 | biostudies-literature
| S-EPMC3542186 | biostudies-literature
| S-EPMC8640587 | biostudies-literature
| S-EPMC6017514 | biostudies-literature
| S-EPMC4310013 | biostudies-literature
| S-EPMC2766262 | biostudies-literature
| S-EPMC3812312 | biostudies-literature