-
Novel serine proteases encoded by two cytotoxic T lymphocyte-specific genes.
Genes that are expressed exclusively in cytotoxic T cells should encode proteins that are essential for target cell lysis in cell-mediated immune responses. The sequences of two cytotoxic T lymphocyte-specific complementary DNA's (cDNA's) suggest that the two genes encode serine proteases. A full-length cDNA corresponding to one of the genes was isolated and sequenced. The predicted protein resembles serine proteases in that it includes all the residues that form the catalytic triad of the active site of serine proteases. Moreover, it has sequence characteristics thought to occur only in rat mast cell protease type II. These results are in accord with the view that a protease cascade plays a key role in cytotoxic T-cell activation.
PMID: 3518058 [PubMed - indexed for MEDLINE]
-
Cited by 32 PubMed Central articles
-
Residual active granzyme B in cathepsin C-null lymphocytes is sufficient for perforin-dependent target cell apoptosis.
Sutton VR, Waterhouse NJ, Browne KA, Sedelies K, Ciccone A, Anthony D, Koskinen A, Mullbacher A, Trapani JA.
J Cell Biol. 2007 Feb 12; 176(4):425-33. Epub 2007 Feb 5.
[J Cell Biol. 2007]
-
ReviewStructural basis of substrate specificity in the serine proteases.
Perona JJ, Craik CS.
Protein Sci. 1995 Mar; 4(3):337-60.
[Protein Sci. 1995]
-
Structure of a cytotoxic T-lymphocyte-specific gene shows a strong homology to fibrinogen beta and gamma chains.
Koyama T, Hall LR, Haser WG, Tonegawa S, Saito H.
Proc Natl Acad Sci U S A. 1987 Mar; 84(6):1609-13.
[Proc Natl Acad Sci U S A. 1987]
- » See all...