Rock bream (Oplegnathus fasciatus) serpin, protease nexin-1: Transcriptional analysis and characterization of its antiprotease and anticoagulant activities

A teleostean angiotensinogen from Oplegnathus fasciatus responses to immune and injury challenges

“…The hematic cell expression levels of AGT and two other inhibitory serpins, HCII and PN-1, in rock bream [17,22] were determined and surprisingly, RbAGT demonstrated a concurrent response synchronized with the mRNA expression of RbHCII and RbPN-1 (Fig. 4).…”

“…As the roles of AGT in post-injury events are emerging in the mammalian literature [6], we examined RbAGT expression following injury in the rock bream, and based on our previous findings [17], we hypothesized that serpins may have a common response pattern following injury. The hematic cell expression levels of AGT and two other inhibitory serpins, HCII and PN-1, in rock bream [17,22] were determined and surprisingly, RbAGT demonstrated a concurrent response synchronized with the mRNA expression of RbHCII and RbPN-1 (Fig.…”

“…The library construction, normalization and GS-FLX sequencing were described in our previous report [17]. A cDNA, highly homologous to known AGTs, was identified using the NCBI, BLAST (http://blast.ncbi.nlm.nih.gov/Blast) and its nucleotide and protein homologs were retrieved.…”

Insights into molecular profiles and genomic evolution of an IRAK4 homolog from rock bream (Oplegnathus fasciatus): Immunogen- and pathogen-induced transcriptional expression

“…Sequence data of a previously constructed normalized cDNA library was searched for genes involved in TLR signaling [23], and a cDNA of Oplegnathus fasciatus IRAK4-like gene was identified. In addition, two partial sequences of a putative IRAK1 gene and three overlapping partial sequences of a IRAK3 (IRAKM) gene were also identified.…”

Caspase 3 from rock bream (Oplegnathus fasciatus): Genomic characterization and transcriptional profiling upon bacterial and viral inductions

“…Subsequently, the three dimensional (3D) image was generated utilizing RasMol 2.7.5.2 software. Recombinant Rbcasp3, excluding the pro-domain, was expressed as a fusion protein with Maltose Binding Protein (MBP) and purified as described previously with some modifications [29]. Briefly, the Rbcasp3 gene encoding residues 33e283 was amplified using the sequence specific primers Rbcasp3-F and Rbcasp3-R with restriction enzyme sites for EcoRI and PstI respectively ( Table 1).…”