ArticleProceedings of the National Academy of Sciences of the United States of America1996
Multiple forms of complement C3 in trout that differ in binding to complement activators.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- Inside job: Roles of intracellular C3.The Journal of allergy and clinical immunology · 2025Review
- Secretory IgM regulates gut microbiota homeostasis and metabolism.Nature microbiology · 2025Article
- A guide to complement biology, pathology and therapeutic opportunity.Nature reviews. Immunology · 2024Review
- Immunonutrition: facilitating mucosal immune response in teleost intestine with amino acids through oxidant-antioxidant balance.Frontiers in immunology · 2023Review
- Complement C3a Enhances the Phagocytic Activity of B Cells Through C3aR in a Fish.Frontiers in immunology · 2022Article
- Complement C3 and Activated Fragment C3a Are Involved in Complement Activation and Anti-Bacterial Immunity.Frontiers in immunology · 2022Article
- The Programming of Antioxidant Capacity, Immunity, and Lipid Metabolism in Dojo Loach (Frontiers in physiology · 2021Article
- Transcriptional Profiles of Genes Related to Stress and Immune Response in Rainbow Trout (Frontiers in immunology · 2021Article
- Zebrafish as a Model for Fish Diseases in Aquaculture.Pathogens (Basel, Switzerland) · 2020Review
- Molecular cloning of Gibel carp (Carassius auratus gibelio) complement component C3 and its expression profile after Cyprinid herpesvirus 2 infection.The Journal of veterinary medical science · 2020Article
- Specific Evolution and Gene Family Expansion of Complement 3 and Regulatory Factor H in Fish.Frontiers in immunology · 2020Article
- High-throughput proteomic profiling of the fish liver following bacterial infection.BMC genomics · 2018Article
- Proteome Profiles of Head Kidney and Spleen of Rainbow Trout (Oncorhynchus Mykiss).Proteomics · 2018Article
- Mechanisms of Fish Macrophage Antimicrobial Immunity.Frontiers in immunology · 2018Review
- Phagocytic and Bactericidal Properties of Channel Catfish Peritoneal Macrophages Exposed toFrontiers in microbiology · 2017Article
- Complement component C3 - The "Swiss Army Knife" of innate immunity and host defense.Immunological reviews · 2016Review
- Transcriptome analysis of the effect of Vibrio alginolyticus infection on the innate immunity-related complement pathway in Epinephelus coioides.BMC genomics · 2014Article
- Gene expression and pathologic alterations in juvenile rainbow trout due to chronic dietary TCDD exposure.Aquatic toxicology (Amsterdam, Netherlands) · 2013Article
- Transcriptional responses of resistant and susceptible fish clones to the bacterial pathogen Flavobacterium psychrophilum.PloS one · 2012Article
- Immunotoxic effects of environmental toxicants in fish - how to assess them?Environmental science and pollution research international · 2011Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
In all other species analyzed to date, the functionally active form of complement component C3 exists as the product of a single gene. We have now identified and characterized three functional C3 proteins (C3-1, C3-3, and C3-4) in trout that are the products of at least two distinct C3 genes. All three proteins are composed of an alpha-and a beta-chain and contain a thioester bond in the alpha-chain. However, they differ in their electrophoretic mobility, glycosylation, reactivity with monospecific C3 antibodies, and relative ability to bind to various surfaces (zymosan, Escherichia coli, erythrocytes). A comparison of the partial amino acid sequences of the three proteins showed that the amino acid sequence identity/similarity of C3-3 to C3-4 is 87/91%, while that of C3-3 and C3-4 to C3-1 is 51.5/65.5% and 60/73% respectively. Thus, trout possess multiple forms of functional C3 that represent the products of several distinct genes and differ in their ability to bind covalently to various complement activators.
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