| First Author | Wilharm E | Year | 1999 |
| Journal | FEBS Lett | Volume | 459 |
| Issue | 1 | Pages | 139-42 |
| PubMed ID | 10508933 | Mgi Jnum | J:57970 |
| Mgi Id | MGI:1346256 | Doi | 10.1016/s0014-5793(99)01200-4 |
| Citation | Wilharm E, et al. (1999) Biological activities of granzyme K are conserved in the mouse and account for residual Z-Lys-SBzl activity in granzyme A-deficient mice. FEBS Lett 459(1):139-42 |
| abstractText | Tryptase-like activities of T and NK cells contribute to the induction of target cell apoptosis, but only granzyme A (GzmA) has been shown to exhibit Z-Lys-SBzl esterase activity in murine T cells. GzmA-deficient mice exhibit residual Z-Lys-SBzl hydrolyzing activity and almost normal levels of lymphocyte-mediated cytotoxicity. Here we report the cloning and biochemical characterization of recombinant mouse granzyme K (GzmK). The purified murine protein shows Z-Lys-SBzl hydrolyzing activity and is inhibited by bikunin, the light chain of inter-alpha-trypsin inhibitor, like the human homolog. We conclude that GzmK expressed by GzmA-deficient T cells accounts for the remaining Z-Lys-SBzl activity. Functional similarities between GzmA and GzmK may explain the subtle immunological deficits observed in GzmA-deficient mice. |
