Unknown

Dataset Information

0

Studying Histone Deacetylase Inhibition and Apoptosis Induction of Psammaplin A Monomers with Modified Thiol Group.


ABSTRACT: Psammaplin A (PsA) is a bromotyrosine disulfide dimer with histone deacetylase (HDAC) inhibition and acts through reduced monomer PsA-SH. We studied the connection of HDAC inhibition, cell growth inhibition, and apoptosis induction of PsA-SH by modifying the -SH group with deletion (6a) or replacement with hydroxamic acid (10b) or benzamide (12g). PsA-SH inhibits HDAC1/2/3 and 6a loses the HDAC inhibition ability. 10b inhibits HDAC1/2/3/6 while 12g shows selective inhibition of HDAC3. PsA-SH and 10b, but neither 6a nor 12g, induce apoptosis in human leukemia HL-60 cells associated with increased acetylation of Histone H3. PsA-SH and 10b inhibit growth of several solid tumor cell lines in vitro and Lewis lung cancer cell growth in vivo. PsA-SH is a simple scaffold for developing selective HDAC inhibitors and induces apoptosis through inhibiting HDAC1/2.

SUBMITTER: Bao Y 

PROVIDER: S-EPMC7812609 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature

altmetric image

Publications

Studying Histone Deacetylase Inhibition and Apoptosis Induction of Psammaplin A Monomers with Modified Thiol Group.

Bao Yu Y   Xu Qihao Q   Wang Lin L   Wei Yunfei Y   Hu Baichun B   Wang Jian J   Liu Dan D   Zhao Linxiang L   Jing Yongkui Y  

ACS medicinal chemistry letters 20210105 1


Psammaplin A (PsA) is a bromotyrosine disulfide dimer with histone deacetylase (HDAC) inhibition and acts through reduced monomer PsA-SH. We studied the connection of HDAC inhibition, cell growth inhibition, and apoptosis induction of PsA-SH by modifying the -SH group with deletion (<b>6a</b>) or replacement with hydroxamic acid (<b>10b</b>) or benzamide (<b>12g</b>). PsA-SH inhibits HDAC1/2/3 and <b>6a</b> loses the HDAC inhibition ability. <b>10b</b> inhibits HDAC1/2/3/6 while <b>12g</b> shows  ...[more]

Similar Datasets

| S-EPMC10377841 | biostudies-literature
| S-EPMC11223745 | biostudies-literature
| S-EPMC6496488 | biostudies-literature
| S-EPMC5398387 | biostudies-literature
| S-EPMC4198757 | biostudies-literature
| S-EPMC4467398 | biostudies-literature
| S-EPMC2939045 | biostudies-literature
| S-EPMC7643317 | biostudies-literature
| S-EPMC3804529 | biostudies-literature
| S-EPMC6562715 | biostudies-literature