title: Ubiquitous presence of piscidin-1 in Atlantic cod as evidenced by immunolocalisation.
abstract: BACKGROUND
  Antimicrobial peptides (AMPs), the natural antibiotics bestowed upon all forms of life, consist of small molecular weight proteins with a broad spectrum antimicrobial activity against a variety of pathogenic microorganisms. Piscidins are one of the AMP families that are imperative for the innate defence mechanisms of teleosts. Atlantic cod, a basal fish belonging to the superorder Paracanthopterygii also possesses multiple piscidin peptides. Two piscidin paralogues (pis1 and pis2) and a novel alternative splice variant of pis2 of this fish were previously described by us. To shed light on other potent roles of these molecules, now we have mapped the distribution of piscidin 1 (Pis1), in different tissues and organs of cod through immunohistochemistry (IHC) employing an affinity purified polyclonal antibody specific to Pis1.
  
  
  RESULTS
  Various cell types and tissues of Atlantic cod including those from the immune organs of naïve fish are armed with Pis1 peptide. Different types of the blood leucocytes and phagocytic cells among the leucocytes examined gave a relatively strong indication of Pis1 immunopositivity. In addition, other cell types such as hematopoietic cells, epithelial cells and multi-granular cells located in the mucosal and hematopoietic tissues were also Pis1-immunoreactive. More interestingly, chondrocytes appear to produce Pis1 and this is the first report on the presence of an AMP in cartilage tissue of fish. Furthermore, Pis1 immunopositivity was detected in other tissues and organs of naïve fish including neural tissues, exocrine and endocrine glands, compound gland cells, excretory kidney, intestinal and respiratory epithelial cells, swim bladder, skin and hypodermis layer, myosepta, liver, heart, eye and oocytes.
  
  
  CONCLUSIONS
  Pis1 peptide is produced by various cell types located in different tissues and organs of Atlantic cod. It is present in all immune-related organs of naïve fish and the elevated peptide expression following phagocytosis strongly suggest their involvement in innate defence. Further, its widespread occurrence in non-immune tissues and organs of apparently healthy fish implies that piscidin may have other functions in addition to its role as an immune effector molecule.
authors.affiliation: Faculty of Biosciences and Aquaculture, University of Nordland, 8049, Bodø, Norway.
authors.forename: Jareeporn
authors.initials: J
authors.lastname: Ruangsri
authors.forename: Jorge M O
authors.initials: JM
authors.lastname: Fernandes
authors.forename: Jan H W M
authors.initials: JH
authors.lastname: Rombout
authors.forename: Monica F
authors.initials: MF
authors.lastname: Brinchmann
authors.forename: Viswanath
authors.initials: V
authors.lastname: Kiron
mesh_terms: D000818:Animals; D023181:Antimicrobial Cationic Peptides / Q000276:immunology*; D029941:Fish Proteins / Q000276:immunology*; D048389:Gadus morhua / Q000276:immunology*; D007113:Immunity, Innate / Q000276:immunology; D007150:Immunohistochemistry / Q000662:veterinary
chemical_list: D023181:Antimicrobial Cationic Peptides; D029941:Fish Proteins; C449802:moronecidin protein, Morone saxatilis