Molecular cloning of two molluscan caspases and gene functional analysis during Crassostrea angulata (Fujian oyster) larval metamorphosis

Abstract

Caspases have been demonstrated to possess important functions in apoptosis and immune system in vertebrate. But there is less information reported on the oyster larval development. In the present work, two full-length molluscan caspase genes, named Cacaspase-2 and Cacaspase-3, were characterized for the first time from Fujian oyster, Crassostrea angulata. Which respectively encode two predicted proteins both containing two caspase domains of p20 and p10 including the cysteine active site pentapeptide "QACRG" and the histidine active site signature. Otherwise Cacaspase-2 also contains a caspase recruitment domain. Homology and phylogenetic analysis showed that Cacaspase-2 shared high similarity with initiator caspase-2 groups, but Cacaspase-3 clustered together with executioner caspase-3 groups. Cacaspase-2 and Cacaspase-3 mRNA were both highly expressed in gills and labial palp and were significantly expressed highly in larvae during settlement and metamorphosis. Through the whole mount in situ hybridization, the location of Cacaspase-2 is in the foot of the oyster larvae and the location of Cacaspase-3 is in both the foot and velum tissues. These results implied that Cacaspase-2 and Cacaspase-3 genes play a key role in the loss of foot and Cacaspase-3 gene has an important function in the loss of velum during larvae metamorphosis in C. angulata.

Molecular Characterization and Functional Analysis of a Putative Octopamine/Tyramine Receptor during the Developmental Stages of the Pacific Oyster, Crassostrea gigas

“…Once appropriate substrate is sensed, oyster will settle and undergo a complex process of metamorphosis. After metamorphosis, the foot will be lost [46]. The detection of CgGPR1 on the surface of foot at the pediveliger stage suggested its potential role in C .…”

Sulforaphane-cysteine-induced apoptosis via phosphorylated ERK1/2-mediated maspin pathway in human non-small cell lung cancer cells

“…Apoptotic caspases are sub-categorized initiator caspases, such as caspase-2, caspase-8, caspase-9 and caspase-10 and executioner caspases, such as caspase-3, caspase-6 and caspase-7. 14,15,16,17 Once initiator caspases are activated, they produce a series of chain reactions, activating several other executioner caspases. 15 Executioner caspases might degrade over 600 cellular components such as poly (ADP-ribose) polymerase (PARP) in order to induce the morphological changes for apoptosis.…”

“…14,15,16,17 Once initiator caspases are activated, they produce a series of chain reactions, activating several other executioner caspases. 15 Executioner caspases might degrade over 600 cellular components such as poly (ADP-ribose) polymerase (PARP) in order to induce the morphological changes for apoptosis. 18 Therefore, we think that SFN-Cys might induce apoptosis through ERK1/2-mediated maspin upregulation, mitochondria death pathway via regulating Bax/Bcl-2 and caspase-3.…”

Molecular cloning and characterization of four caspases members in Apostichopus japonicus

“…Once activated by initiator caspases, they cleave diverse cellular substrates, ultimately resulting in apoptosis and leading to cell death [12]. Caspase-3, one of the key executioners of apoptosis in the apoptotic pathway, being responsible either partially or totally for the proteolytic cleavage of many key proteins [23]. Activated caspase-3 mediates many of the characteristic morphological alterations of apoptosis, such as cleavage of polyadenosine dipeptide ribose polymerase (PARP), activate caspase-activated deoxyribonuclease (CAD), induce cell disintegration and lead cells toward death [13,24].…”

“…Nowadays, caspase-3 is reported to widely involve in various species of vertebrates and invertebrates. In mollusks, caspase-3 gene has been investigated from shrimp (Penaeus vannamei) and Fujian oyster (Crassostrea angulata) [23,25], however, little information is known in echinoderms. Caspase-6 is considered to be another important apoptotic executioner, which acts downstream target of the apoptotic initiators such as caspase-2, -8, -9, and -10 [26,27].…”