Abstract:
:In this study the sea bass (Dicentrarchus labrax) pepsinogen C gene was isolated. The nucleotide sequences of all exons are presented. The organization of the gene is compatible with that of other aspartic proteinases. The predicted 388-residue amino acid (aa) sequence of sea bass pepsinogen C consists of a signal sequence of 16 amino acid residues, an activation peptide of 43 residues, and the mature pepsin of 329 residues containing the two characteristic active-site aspartic acids. We also analyzed fasting-induced changes in the expression of progastricsin mRNA, using real-time RT-PCR absolute quantification. Progastricsin mRNA copy number was downregulated under conditions of negative energy balance, such as starvation, and upregulated during positive energy balance, such as refeeding. These findings offer new information about the sea bass progastricsin gene and support a role of this gastric digestive enzyme in the regulation of food intake in sea bass.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Terova G,Rimoldi S,Larghi S,Bernardini G,Gornati R,Saroglia Mdoi
10.1016/j.bbrc.2007.09.013subject
Has Abstractpub_date
2007-11-23 00:00:00pages
591-6issue
3eissn
0006-291Xissn
1090-2104pii
S0006-291X(07)01958-4journal_volume
363pub_type
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