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

Overview
TitleA trypsin-like protease with apparent dual function in early Lepeophtheirus salmonis (Krøyer) development
AuthorsSkern-Mauritzen R, Frost P, Dalvin S, Kvamme BO, Sommerset I, Nilsen F
TypeJournal Article
Journal NameBMC molecular biology
Volume10
IssueN/A
Year2009
Page(s)44
CitationSkern-Mauritzen R, Frost P, Dalvin S, Kvamme BO, Sommerset I, Nilsen F. A trypsin-like protease with apparent dual function in early Lepeophtheirus salmonis (Krøyer) development. BMC molecular biology. 2009; 10:44.

Abstract

BACKGROUND
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. During these studies a trypsin-like peptidase which differed in a number of traits were identified.

RESULTS
An 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.

CONCLUSION
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.

Author Details
Additional information about authors:
Details
1Rasmus Skern-Mauritzen
2Petter Frost
3Sussie Dalvin
4Bjørn Olav Kvamme
5Ingunn Sommerset
6Frank Nilsen
Properties
Additional details for this publication include:
Property NameValue
Publication ModelElectronic
ISSN1471-2199
eISSN1471-2199
Publication Date2009
Journal AbbreviationBMC Mol. Biol.
DOI10.1186/1471-2199-10-44
Elocation10.1186/1471-2199-10-44
Publication TypeJournal Article
Journal CountryEngland
LanguageEnglish
Language Abbreng
Publication TypeResearch Support, Non-U.S. Gov't
Cross References
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DatabaseAccession
PMID: PMID:19439101