Then we examined the expression of several HATs was proved a

Then we examined the Fmoc-Val-Cit-PAB-MMAE expression of several HATs was proved as substrate of Curcumin, Cdyl and Myst4 were reported particularly in elongating spermatids. We revealed a decreased mRNA level of these genes after Curcumin treatment, shown that at least a part of their products were newly synthesized in round spermatids. We had tried to determine their protein levels and dynamics in spermatids, either by Western blot or immunochemistry. Unfortunately, no reliable data was obtained maybe due to their step-specific little content. For the already translated HAT proteins in late round spermatids, their activities might be considerably inhibited by Curcumin treatment. Apoptosis is a process of programmed cell death essential for homeostasis maintenance in multicellular organisms, which is regulated by a subset of caspases in charge of propagating, once activated, the apoptotic signal to the nucleus. The suppression of caspase activity occurs in the presence of specific members of the IAP family. In particular, cIAP1 and cIAP2 are indirect inhibitors of caspases activity, whereas XIAP is able to directly inhibit both initiator and effector caspases. All IAPs host one to three BIR domains that are critical for their anti-apoptotic activity. In particular, it has been shown that the XIAP-BIR2 domain is responsible for the inhibition of effector caspases, whereas XIAPBIR3 directly binds to and inhibits initiator caspase-9, which can also be recognized by cIAP1-BIR3. The caspase inhibitory activity of XIAP is endogenously antagonized by Smac which is released from mitochondria together with cytochrome c in response to death stimuli. The N-terminal tetrapeptides of Smac/DIABLO and caspases competitively bind to the same XIAP active Ribociclib hydrochloride pocket, resulting in activation or inhibition of apoptosis, respectively. Since the structural details of IBM interactions with XIAP and cIAPs have been previously described, the IBM peptides provide a natural basis for the design of Smac-mimetics. These compounds have been shown to displace caspases 3, 7 and 9 from XIAP-BIR2 and �CBIR3 inhibitory pockets, and to induce auto-ubiquitination and degradation of cIAPs by perturbing BIR3/RING domain interaction. Therefore, the Smac-mimetics can restore the apoptotic cascade ope