A trypsin-like protease with apparent dual function in early Lepeophtheirus salmonis (Krøyer) development

Abstract

<p>Abstract</p> <p>Background</p> <p>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 <it>Lepeophtheirus salmonis</it>. During these studies a trypsin-like peptidase which differed in a number of traits were identified.</p> <p>Results</p> <p>An intronless trypsin-like serine peptidase (<it>LsTryp10</it>) from <it>L., salmonis </it>was identified and characterized. <it>LsTryp10 </it>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. <it>LsTryp10 </it>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.</p> <p>Conclusion</p> <p>Based 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.</p