In vivo effects of β-glucan and LPS on regulation of lysozyme activity and mRNA expression in Atlantic salmon (Salmo salar L.)

• Published in: Fish & shellfish immunology 2003-01, Vol.14 (1), p.39-54
• Main Authors: Paulsen, Steinar M, Lunde, Halvor, Engstad, Rolf E, Robertsen, Børre
• Format: Article
• Language: English
• Subjects: Animals; Atlantic salmon, lysozyme transcription, intracellular lysozyme activity, induced lysozyme production, β-glucan, lipopolysaccharide; Bacteria; beta -glucan; Brackish; Escherichia coli; Freshwater; Gene Expression Regulation - drug effects; Glucans - pharmacology; Injections, Intraperitoneal - veterinary; Intestines - enzymology; Kidney - enzymology; Leukocytes - enzymology; lipopolysaccharides; Lipopolysaccharides - pharmacology; Liver - enzymology; Marine; Muramidase - drug effects; Muramidase - genetics; Muramidase - metabolism; Random Allocation; RNA, Messenger - metabolism; Saccharomyces cerevisiae; Salmo salar; Salmo salar - immunology; Salmo salar - metabolism; Spleen - enzymology; Transcription, Genetic - drug effects
• ISSN: 1050-4648; 1095-9947
• DOI: 10.1006/fsim.2002.0416

The present study was undertaken to compare the effects of intraperitoneally injected bacterial lipopolysaccharide (LPS) and yeast β-glucan on lysozyme activity in Atlantic salmon, and to explore what organ(s) are responsible for the increase in plasma lysozyme activity induced by the compounds. The results indicated that LPS stimulates plasma lysozyme activity at least as efficiently as β-glucan. The lysozyme gene was shown to be transcribed in head kidney, spleen, liver and intestine, and accumulation of transcript was demonstrated in response to both β-glucan and LPS in all of these organs. Intracellular lysozyme activity was detected in the same organs and in isolated blood polymorphonuclear cells (PMN) and lymphocytes. Increased lysozyme activity in response to both β-glucan and LPS was demonstrated in blood PMN and cells isolated from head kidney and intestine. In spleen and liver on the other hand, there was no increase in lysozyme activity in response to the stimulants. Based on previous work and the present results it is suggested that plasma lysozyme induced by LPS and β-glucan originate from macrophages in the different organs. The head kidney is likely to be the main supplier of plasma lysozyme considering its high contents of macrophages. This work supports the notion that microbial compounds containing phylogenetically conserved structures (β-glucan and LPS) are able to stimulate the non-specific defence of animals against infection by enhancing the lysozyme expression.