Abstract
BackgroundTrypsin-like serine proteases are involved in a large number of processes including digestive degradation, regulation of developmental processes, yolk degradation and yolk degradome activation. Trypsin like peptidases considered to be involved in digestion have been characterized in Lepeophtheirus salmonis. During these studies a trypsin-like peptidase which differed in a number of traits were identified.ResultsAn intronless trypsin-like serine peptidase (LsTryp10) from L., salmonis was identified and characterized. LsTryp10 mRNA is evenly distributed in the ovaries and oocytes, but is located along the ova periphery. LsTryp10 protein is deposited in the oocytes and all embryonic cells. LsTryp10 mRNA translation and concurrent degradation after fertilization was found in the embryos demonstrating that LsTryp10 protein is produced both by the embryo and maternally. The results furthermore indicate that LsTryp10 protein of maternal origin has a distribution pattern different to that of embryonic origin.ConclusionBased on present data and previous studies of peptidases in oocytes and embryos, we hypothesize that maternally deposited LsTryp10 protein is involved in regulation of the yolk degradome. The function of LsTryp10 produced by the embryonic cells remains unknown. To our knowledge a similar expression pattern has not previously been reported for any protease.
Highlights
Trypsin-like serine proteases are involved in a large number of processes including digestive degradation, regulation of developmental processes, yolk degradation and yolk degradome activation
During characterization of trypsins and trypsin-like peptidases in L. salmonis [30,31,32,33] we identified an intronless single domain trypsin that was transcribed by adult female L. salmonis (LsTryp10, accession# EF490878)
LsTryp10 is devoid of introns, which is a feature reported for functional digestive trypsins in Anopheles gambiae [39]
Summary
Trypsin-like serine proteases are involved in a large number of processes including digestive degradation, regulation of developmental processes, yolk degradation and yolk degradome activation. Trypsin like peptidases considered to be involved in digestion have been characterized in Lepeophtheirus salmonis. Trypsin-like serine peptidases of the S1A subfamily (hereafter referred to as S1A peptidases) are found in all metazoan groups and are involved in a variety of biological processes [1,2]. They are synthesized as inactive zymogens which are activated by proteolytic cleavage at a defined site N-terminal to the proteolytic domain. Trypsins are S1A peptidases with a specific architecture that cleave substrates after Arg and Lys [2] They are common digestive enzymes in metazoans and their zymogens are activated by trypsins or enteropeptidases [2]. Considering that localization of many transcripts, including bicoid mRNA and Vg1 mRNA, depends on elements in their 3' UTRs [41,42,43,44,45] the relatively long LsTryp mRNA 3' UTR may contain elements involved in control of mRNA localization and translation
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