| one publication added to basket [297274] | Enzyme characterisation and gene expression profiling of Atlantic salmon chicken- and goose-type lysozymes
Myrnes, B.; Seppola, M.; Johansen, A.; Øverbø, K.; Callewaert, L.; Vanderkelen, L.; Michiels, C.W.; Nilsen, I.W. (2013). Enzyme characterisation and gene expression profiling of Atlantic salmon chicken- and goose-type lysozymes. Dev. Comp. Immunol. 40(1): 11-19. https://dx.doi.org/10.1016/j.dci.2013.01.010
In: Developmental and Comparative Immunology. Elsevier: New York,. ISSN 0145-305X; e-ISSN 0145-305X, more
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| Author keywords |
Lysozyme, Purification, Activity, Gene expression, Ivy, PliG |
| Authors | | Top |
- Myrnes, B.
- Seppola, M.
- Johansen, A.
- Øverbø, K.
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- Callewaert, L.
- Vanderkelen, L., more
- Michiels, C.W., more
- Nilsen, I.W.
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| Abstract |
Lysozymes represent important innate immune components against bacteria. In this study, Atlantic salmon (Salmo salar) goose (g-) and chicken (c-) types of lysozyme were subjected to protein characterisations and tissue expression analyses. Specific bacterial protein inhibitors of g- and c-type lysozymes were employed to discriminate between respective enzyme activities. Blood, gills and liver contained activities exclusive for the g-type lysozyme. Only haematopoietic organs (head kidney and spleen) contained enzyme activities of both g- and c-lysozyme enzymes and c-type activity was not found outside these organs. Gene transcript levels proportional to enzyme activity levels were detected for the g-type lysozyme but not for the c-type. In vitro studies revealed significant induction of c-type gene expression and enzyme activity in macrophages after incubation with lipopolysaccharide (LPS) while expression of the g-type lysozyme gene was unaffected. The activity of purified native c-type enzyme was profoundly reduced by divalent cations and displayed low tolerance to monovalent cations, while the native g-type lysozyme was stimulated by monovalent cations and tolerated low concentrations of divalent cations. Activities of both enzymes increased with temperature elevations up to 60 °C. The native g-type lysozyme responses to temperature in particular are in apparent conflict to the ones for the recombinant salmon g-lysozyme.Our results imply separate expression regulations and different functions of c- and g-type lysozymes in salmon. LPS-induced expression of c-type lysozyme and broad constitutive tissue distribution of g-type lysozyme in salmon is different from findings in other studied fish species. |
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