Biological activities of granzyme K are conserved in the mouse and account for residual Z‐Lys‐SBzl activity in granzyme A‐deficient mice

FEBS Letters

Jenne, Dieter E.²  Tschopp, Jürg¹  Wilharm, Elke² 

[1] Institute of Biochemistry, University of Lausanne, CH-1066 Epalinges, Switzerland;Department of Neuroimmunology, Max-Planck-Institute of Neurobiology, Am Klopferspitz 18A, D-82152 Martinsried, Germany

关键词: Lymphocyte cytotoxicity;    Bikunin;    Granzyme;    DNA fragmentation;    Apoptosis;    Inter-α-trypsin inhibitor;    GzmA;    granzyme A;    GzmK;    granzyme K;    Z-Lys-SBzl;    N α-benzyloxycarbonyl-L-lysine-thiobenzylester;    PCR;    polymerase chain reaction;    Z;    N α-benzyloxycarbonyl;    SBzl;    thiobenzylester;    DTNB;    5;    5′-dithio-bis-(2-nitrobenzoic acid);    CMK;    chloromethyl ketone;    TPCK;    N-tosyl phenylalanine chloromethyl ketone;    TLCK;    N-tosyl lysine chloromethyl ketone;   

DOI  :  10.1016/S0014-5793(99)01200-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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-α-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.

【 授权许可】

Unknown