Lack of requirement for SHP-1 in both Fas- mediated and perforin-mediated cell death induced by CTL.
The Fas (CD95)-transmitted cell death signal has been reported to involve a protein tyrosine phosphatase, SHP-1. We analyzed the role of SHP-1 in the Fas-dependent as well as the perforin-dependent pathways of CTL- mediated killing using target cells prepared from SHP-1-deficient motheaten mice. Con A blast targets prepared from both a motheaten mouse and a phenotype-normal littermate were equally sensitive to the cytolysis and DNA fragmentation induced by both perforin-deficient Fas-dependent CTL and Fas ligand-deficient perforin-positive CTL. Fas- induced DNA degradation detected by the terminal deoxynucleotide transferase reaction was also observed in the killing of motheaten thymocytes by a Fas-based CTL as well as by anti-Fas mAb. These data cast doubt on the involvement of SHP-1 in Fas-induced lymphoid cell death.[1]References
- Lack of requirement for SHP-1 in both Fas-mediated and perforin-mediated cell death induced by CTL. Takayama, H., Lee, M.H., Shirota-Someya, Y. J. Immunol. (1996) [Pubmed]
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