title: The acute phase response and innate immunity of fish.
abstract: Tissue trauma or invasion by pathogens or parasites induce changes in the quantities of several macromolecules in animal body fluids. These changes comprise one aspect of the acute phase response (APR), which in toto involves metabolic changes in several organ systems. One clear indication of the response is the increase in synthesis and secretion by the liver of several plasma proteins, with simultaneous decreases in others. These acute phase proteins (APP) function in a variety of defense-related activities such as limiting the dispersal of infectious agents, repair of tissue damage, inactivation of proteases, killing of microbes and other potential pathogens, and restoration of the healthy state. Some APP are directly harmful to microbes, while others modify targets thus marking them for cell responses. Some work alone while others contribute to cascades. Proteins that are APP in mammals, and that have been identified in both teleosts and elasmobranchs include C-reactive protein, serum amyloid P, and several components of the Complement system. Others reported in teleosts include transferrin and thrombin. Of these, only CRP has been reported to increase in acute phase plasma. In trout, a precerebellin-like protein is an APP with unknown functions. A cDNA library enriched in fragments of transcripts that were more abundant in livers from fish undergoing an APR recently yielded sequences resembling 12 additional known APP, and as many others either not known to be APP, or not similar to others yet in public databases. It appears that, as in mammals, hepatocytes are the prime source of APP in fish, and that pro-inflammatory cytokines induce transcription of their genes.
authors.affiliation: Department of Zoology, Center for Fish Disease Research and Environmental Health Sciences Center, Oregon State University, Corvallis, OR 97331, USA. baynec@bcc.orst.edu
authors.forename: C J
authors.initials: CJ
authors.lastname: Bayne
authors.forename: L
authors.initials: L
authors.lastname: Gerwick
mesh_terms: D000209:Acute-Phase Proteins / Q000235:genetics / Q000276:immunology / Q000502:physiology; D000210:Acute-Phase Reaction / Q000276:immunology*; D000595:Amino Acid Sequence; D000818:Animals; D001053:Apolipoproteins / Q000235:genetics / Q000276:immunology / Q000502:physiology; D002097:C-Reactive Protein / Q000235:genetics / Q000276:immunology / Q000502:physiology; D003176:Complement C3 / Q000378:metabolism; D004784:Environmental Monitoring; D005399:Fishes / Q000235:genetics / Q000276:immunology* / Q000502:physiology; D008969:Molecular Sequence Data; D009113:Muramidase / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D000685:Serum Amyloid A Protein / Q000235:genetics / Q000276:immunology / Q000502:physiology; D000683:Serum Amyloid P-Component / Q000235:genetics / Q000276:immunology / Q000502:physiology; D014168:Transferrin / Q000235:genetics / Q000276:immunology / Q000502:physiology; D000511:alpha-Macroglobulins / Q000235:genetics / Q000276:immunology / Q000502:physiology
chemical_list: D000209:Acute-Phase Proteins; D001053:Apolipoproteins; D003176:Complement C3; D000685:Serum Amyloid A Protein; D000683:Serum Amyloid P-Component; D014168:Transferrin; D000511:alpha-Macroglobulins; D002097:C-Reactive Protein; D009113:Muramidase