Regulation of body mass growth through activin type IIB receptor in teleost fish

Structural and functional characterizations of activin type 2B receptor (acvr2b) ortholog from the marine fish, gilthead sea bream, Sparus aurata: evidence for gene duplication of acvr2b in fish

“…Fractions eluted with 250 mM imidazole showed a band of w23 kDa along with a broad smearing band above the 23 kDa band. The smearing pattern was also observed previously during human, pig, chicken, and goldfish ACVR2B-ECD expression in P. pastoris (Daly & Hearn 2006, Carpio et al 2009, Kim et al 2012.…”

“…Essentially similar results regarding N-glycosylation were reported for the pig ACVR2B-ECD expressed in P. pastoris (Kim et al 2012). By contrast, ACVR2B-ECD from goldfish, chicken, and human produced in P. pastoris (Daly & Hearn 2006, Carpio et al 2009, Kim et al 2012 and mouse ACVR2B-ECD produced in baculovirus-insect cell culture system (Donaldson et al 1999) also seem to undergo O-linked glycosylation (on serine or threonine residues).…”

“…The situation is complicated by the presence of two mstn genes. In a single report, immersion of fish larvae in Pichia pastoris culture supernatant containing recombinant goldfish (Carassius auratus) Acvr2b-ECD enhanced larval growth (Carpio et al 2009). However, no direct evidence was provided that indeed Acvr2b-ECD binds MSTN and that the inhibition of MSTN activity is responsible for the growth enhancement.…”

Expression of Neuropeptide Y of GIFT Tilapia (Oreochromis sp.) in Yeast Pichia Pastoris and Its Stimulatory Effects on Food Intake and Growth

“…Therefore, these deficiencies limit its application in protein expression studies. As a eukaryote, yeast Pichia pastoris, a useful system for the expression of milligram-to-gram quantities of proteins for both basic laboratory research and industrial manufacture, owns advantages of higher eukaryotic expression systems such as protein processing, protein folding, and posttranslational modification, while being as easy to manipulate as E. coli or Saccharomyces cerevisiae (Carpio et al, 2009;Cregg et al, 2000). Expression of target protein in Pichia pastoris can be either intracellular or secreted, and secretion requires a signal sequence on the expressed protein to target it to the secretory pathway.…”

“…Additionally, it has recently been demonstrated that the culture www.intechopen. (Carpio et al, 2009). These characteristics make P. pastoris a very useful heterologous proteins expression system in production of recombinant proteins for aquaculture purposes.…”