| First Author | Masson D | Year | 1987 |
| Journal | Cell | Volume | 49 |
| Issue | 5 | Pages | 679-85 |
| PubMed ID | 3555842 | Mgi Jnum | J:39247 |
| Mgi Id | MGI:86629 | Doi | 10.1016/0092-8674(87)90544-7 |
| Citation | Masson D, et al. (1987) A family of serine esterases in lytic granules of cytolytic T lymphocytes. Cell 49(5):679-85 |
| abstractText | Cytoplasmic granules of cytolytic T lymphocytes (CTLs) contain, in addition to the pore-forming protein perforin, a family of highly homologous serine esterases, granzymes A-H. The serine esterase affinity label diisopropyl fluorophosphate reacts strongly with granzymes A and D, to a lesser extent with B, E, F, G, and H, and not at all with C and F. For granzymes A and D, synthetic substrates have been found. Antibodies raised against granzyme B strongly cross-react with A, G, and H, and antibodies to granzyme D recognize C, E, and F. These antigenic relationships correlate with similarities in the N-terminal amino acid sequences. At least 60% homology is observed between the eight proteins, and all are similar to rat mast cell protease 2. Sequence analysis suggests the identity of granzyme A with a protease predicted from a CTL-specific cDNA clone (H factor) and of granzyme B, G, or H with a protein encoded by the CTL-specific cDNA clone CTLA 1/CCP 1. |
