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Gene Review

Gzma  -  granzyme A

Rattus norvegicus

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High impact information on Gzma

  • The noncytotoxic rat mast cell tumor line RBL was transfected with genes for the cytotoxic lymphocyte granule proteins cytolysin (perforin) and granzyme A, giving transfectants with mRNA and protein expression levels comparable with cloned cytotoxic T lymphocytes [1].
  • These results support the granule-exocytosis model for lymphocyte cytotoxicity and show that effector granzyme A plays a role in target cell DNA breakdown [1].
  • Granzymes are trypsin-like serine proteases mediating apoptotic cell death that are composed of two genetically distinct subfamilies: granzyme A-like proteases resemble trypsin in their active site architecture, while granzyme B-like proteases are quite distinct [2].
  • Granzyme A activates an endoplasmic reticulum-associated caspase-independent nuclease to induce single-stranded DNA nicks [3].
  • Thus, GzmA activates a DNase (GzmA-activated DNase) within the SET complex to produce a novel form of DNA damage during cytotoxic T lymphocyte-mediated death [3].

Biological context of Gzma


Anatomical context of Gzma


Associations of Gzma with chemical compounds


Other interactions of Gzma


Analytical, diagnostic and therapeutic context of Gzma

  • We have previously reported, in a model of heart allograft, the presence of a heavy leukocyte infiltrate, in the allograft which displayed a strong allospecific cytotoxicity when tested in vitro against donor cells, and a strong accumulation of mRNA for granzyme A and perforin in vivo [11].


  1. Cytotoxicity with target DNA breakdown by rat basophilic leukemia cells expressing both cytolysin and granzyme A. Shiver, J.W., Su, L., Henkart, P.A. Cell (1992) [Pubmed]
  2. Characterization of structural determinants of granzyme B reveals potent mediators of extended substrate specificity. Ruggles, S.W., Fletterick, R.J., Craik, C.S. J. Biol. Chem. (2004) [Pubmed]
  3. Granzyme A activates an endoplasmic reticulum-associated caspase-independent nuclease to induce single-stranded DNA nicks. Beresford, P.J., Zhang, D., Oh, D.Y., Fan, Z., Greer, E.L., Russo, M.L., Jaju, M., Lieberman, J. J. Biol. Chem. (2001) [Pubmed]
  4. Purification and identification of a binding protein for pancreatic secretory trypsin inhibitor: a novel role of the inhibitor as an anti-granzyme A. Tsuzuki, S., Kokado, Y., Satomi, S., Yamasaki, Y., Hirayasu, H., Iwanaga, T., Fushiki, T. Biochem. J. (2003) [Pubmed]
  5. Differential expression of granzyme A and granzyme B proteases and their secretion by fresh rat natural killer cells (NK) and lymphokine-activated killer cells with NK phenotype (LAK-NK). Velotti, F., Palmieri, G., D'Ambrosio, D., Piccoli, M., Frati, L., Santoni, A. Eur. J. Immunol. (1992) [Pubmed]
  6. Synergistic roles of granzymes A and B in mediating target cell death by rat basophilic leukemia mast cell tumors also expressing cytolysin/perforin. Nakajima, H., Park, H.L., Henkart, P.A. J. Exp. Med. (1995) [Pubmed]
  7. Expression of human recombinant granzyme A zymogen and its activation by the cysteine proteinase cathepsin C. Kummer, J.A., Kamp, A.M., Citarella, F., Horrevoets, A.J., Hack, C.E. J. Biol. Chem. (1996) [Pubmed]
  8. Granzyme A expression by normal rat natural killer (NK) cells in vivo and by interleukin 2-activated NK cells in vitro. Velotti, F., Palmieri, G., Morrone, S., Piccoli, M., Frati, L., Santoni, A. Eur. J. Immunol. (1989) [Pubmed]
  9. Non-granular proteolytic enzymes of rat interleukin-2-activated natural killer cells. III. Enhancement of A-NKP 1, 2, and 3 proteolytic activities (cleaving after Arg, Phe and Pro) in response to interleukin-2. Kitson, R.P., Miller, C.A., Goldfarb, R.H. Nat. Immun. (1995) [Pubmed]
  10. Decreased IFN-gamma and IL-2 mRNA expression in peripheral tolerance to heart allografts with conserved granzyme A, perforin, and MHC antigens mRNA expression. Bugeon, L., Cuturi, M.C., Paineau, J., Chabannes, D., Soulillou, J.P. Transplant. Proc. (1993) [Pubmed]
  11. Decreased anti-donor major histocompatibility complex class I and increased class II alloantibody response in allograft tolerance in adult rats. Cuturi, M.C., Josien, R., Cantarovich, D., Bugeon, L., Anegon, I., Menoret, S., Smit, H., Douillard, P., Soulillou, J.P. Eur. J. Immunol. (1994) [Pubmed]
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