کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5916470 | 1163744 | 2015 | 13 صفحه PDF | دانلود رایگان |
- Catfish Lck and CD2 were identified and are specifically expressed by T cells.
- Binding experiments with Lck and T cell co-receptors indicate that CD2, CD4-1, and CD4-2 bind to Lck.
- In contrast, catfish CD8α and CD8β do not reproducibly bind to Lck.
The binding of the lymphocyte specific protein tyrosine kinase (Lck) to T cell co-receptors is required for T cell development and activation. In mammals, Lck initiates signal transduction by binding to CD4 and CD8 co-receptors and phosphorylating ITAMs in the cytoplasmic tail of the CD3 molecules and the ζ chains. In addition, Lck can also bind to the adhesion molecule CD2 and trigger T cell activation. In this study, Lck and CD2 homologs were identified and characterized in channel catfish, Ictalurus punctatus. Lck and CD2 mRNAs were specifically expressed by clonal T cell lines, including both CD4+ and CD4âCD8â CTL lines, and in mixed lymphocyte cultures (MLC). Western blot analyses using anti-trout Lck and anti-human p-Lck antibodies demonstrated that Lck protein is expressed in catfish clonal CTL and is phosphorylated at a conserved tyrosine residue. Because of the lack of CD8+ CTL lines as well as the absence of CD8 message in MLC, we performed magnetic bead binding assays to correlate CD2, CD4, and CD8 co-receptor expression with Lck binding ability. Recombinant Lck reproducibly bound to CD2, CD4-1, and CD4-2, but not to CD8α or CD8β. These data provide one possible explanation for the apparent low numbers of CD8+ CTL and the presence of CD4+ and CD4âCD8âCD2+ CTL in catfish.
Journal: Molecular Immunology - Volume 66, Issue 2, August 2015, Pages 126-138