PUBLICATION
            Indentification and molecular characterization of the interleukin-10 receptor 1 of the zebrafish (Danio rerio) and the goldfish (Carassius auratus L.)
- Authors
 - Grayfer, L., and Belosevic, M.
 - ID
 - ZDB-PUB-110920-1
 - Date
 - 2012
 - Source
 - Developmental and comparative immunology 36(2): 408-17 (Journal)
 - Registered Authors
 - Keywords
 - interleukin-10 receptor, IL10R1, interleukin-10 receptor, alpha chain, bony fish, goldfish, inflammation, gene expression, macrophages, STAT3, JAK1
 - MeSH Terms
 - 
    
        
        
            
                
- Animals
 - Amino Acid Sequence
 - Sequence Analysis, DNA
 - Random Amplified Polymorphic DNA Technique
 - Cloning, Molecular/methods
 - Goldfish/genetics
 - Goldfish/immunology*
 - Sequence Alignment
 - Female
 - Recombinant Proteins/immunology
 - Molecular Sequence Data
 - Base Sequence
 - Zebrafish/genetics
 - Zebrafish/immunology*
 - Male
 - Interleukin-10 Receptor alpha Subunit/genetics*
 - Interleukin-10 Receptor alpha Subunit/immunology*
 - Phylogeny
 - RNA/chemistry
 - RNA/genetics
 - Evolution, Molecular
 
 - PubMed
 - 21906622 Full text @ Dev. Comp. Immunol.
 
            Citation
        
        
            Grayfer, L., and Belosevic, M. (2012) Indentification and molecular characterization of the interleukin-10 receptor 1 of the zebrafish (Danio rerio) and the goldfish (Carassius auratus L.). Developmental and comparative immunology. 36(2):408-17.
        
    
                
                    
                        Abstract
                    
                    
                
                
            
        
        
    
        
            
            
 
    
    
        
    
    
    
        
                This is the first report of the identification and molecular characterization of an interleukin-10 receptor 1 in bony fish. By gene synteny analysis, we identified the zebrafish interleukin-10 receptor 1 (IL10R1) and using this IL10R1 sequence, we cloned the goldfish IL10R1 cDNA transcript. The identified fish IL10R1 protein sequences had a putative JAK1 binding site, only one of the two STAT3 binding sites, that are present in all other vertebrates IL10R1 proteins as well as C-terminal serine rich areas, believed to be responsible for the anti-inflammatory properties of IL10R1. Phylogenetically, the fish IL10R1 proteins grouped independently of the amphibian, avian and mammalian IL10R1s. Quantitative gene expression analysis of the IL10R1 of zebrafish and goldfish revealed highest mRNA levels in the spleen tissues. High mRNA levels were also observed in the zebrafish muscle in contrast to low mRNA levels in the muscle of the goldfish. Moderate IL10R1 mRNA levels were seen in most other tissues examined and lowest gene expression was in the liver of both fish species. Goldfish monocytes stimulated with a recombinant goldfish interleukin-10 (rgIL-10) or with heat killed fish pathogens, Aeromonas salmonicida or Trypanosoma carassii, exhibited significantly reduced mRNA levels of the IL10R1. Furthermore, we produced a recombinant form of the goldfish IL10R1 (rgIL10R1) and using in vitro binding studies, demonstrated that the dimerized rgIL-10 specifically interacted with rgIL10R1. Our results suggest that interleukin-10 system has been highly conserved throughout evolution.
            
    
        
        
    
    
    
                
                    
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                        Sequence Targeting Reagents
                    
                    
                
                
            
        
        
    
        
            
            
        
        
    
    
    
                
                    
                        Fish
                    
                    
                
                
            
        
        
    
        
            
            
        
        
    
    
    
                
                    
                        Orthology
                    
                    
                
                
            
        
        
    
        
            
            
        
        
    
    
    
                
                    
                        Engineered Foreign Genes
                    
                    
                
                
            
        
        
    
        
            
            
        
        
    
    
    
                
                    
                        Mapping