mRNA expression patterns of the BPI/LBP molecule in the Atlantic cod (Gadus morhua L.).
Bactericidal/permeability-increasing protein (BPI) and lipopolysaccharide-binding protein (LBP) are important components of the mammalian innate defence system against Gram-negative infections. cDNA encoding a protein related to mammalian BPI and LBP have been cloned from several teleosts including the Atlantic cod (Gadus morhua L.). Using real-time PCR an increase in cod BPI/LBP expression in whole blood and peritoneal cells was demonstrated one, two and four days after intraperitoneal injection of inactivated Vibrio anguillarum. Although constitutively produced in the head kidney, a moderate rise of BPI/LBP mRNA production was seen on day two in this organ. After seven days the BPI/LBP mRNA levels at the three locations examined were almost back to normal. In situ hybridisation demonstrated a leucocytic localisation and morphology of the BPI/LBP expressing cells in various tissues. A combination of in situ hybridisation and peroxidase staining of head kidney leucocytes showed that the BPI/LBP producing cells are peroxidase positive and possible neutrophil like cells. The results suggest that the cod BPI/LBP is important in the first-line defence against bacterial infections and has a function more related to the mammalian BPI molecule than the LBP counterpart.
Solstad
Terese
T
Department of Marine Biotechnology, The Norwegian College of Fishery Science, University of Tromsø, N-9037 Tromsø, Norway. tereses@nrh.uit.no
Stenvik
Jørgen
J
Jørgensen
Trond Ø
TØ
D000209:Acute-Phase Proteins / Q000096:biosynthesis* / Q000235:genetics / Q000276:immunology; D000818:Animals; D023181:Antimicrobial Cationic Peptides / Q000096:biosynthesis* / Q000097:blood / Q000235:genetics / Q000276:immunology; D001798:Blood Proteins / Q000096:biosynthesis* / Q000235:genetics / Q000276:immunology; D002352:Carrier Proteins / Q000096:biosynthesis* / Q000097:blood / Q000235:genetics / Q000276:immunology; D048389:Gadus morhua / Q000235:genetics* / Q000276:immunology* / Q000382:microbiology; D017403:In Situ Hybridization / Q000662:veterinary; D007963:Leukocytes, Mononuclear / Q000276:immunology; D008562:Membrane Glycoproteins / Q000096:biosynthesis* / Q000097:blood / Q000235:genetics / Q000276:immunology; D008565:Membrane Proteins / Q000096:biosynthesis* / Q000097:blood / Q000235:genetics / Q000276:immunology; D009195:Peroxidase / Q000737:chemistry; D016133:Polymerase Chain Reaction / Q000662:veterinary; D012333:RNA, Messenger / Q000096:biosynthesis* / Q000235:genetics; D014733:Vibrio / Q000276:immunology; D000099231:Lipopolysaccharide-Binding Protein
D000209:Acute-Phase Proteins; D023181:Antimicrobial Cationic Peptides; D001798:Blood Proteins; D002352:Carrier Proteins; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D009195:Peroxidase; D012333:RNA, Messenger; D000099231:Lipopolysaccharide-Binding Protein; C021623:bactericidal permeability increasing protein