EC Number   |
General Information |
Reference |
|---|
   3.4.21.78 | evolution |
the enzyme belongs to the granzyme serine protease family, key effector molecules expressed by cytotoxic lymphocytes. Peptide substrate specificity profile of mouse and human granzyme A, overview |
732177 |
| 3.4.21.78 | malfunction |
even though granzyme A is expressed by cytotoxic cells from mouse lungs during pulmonary infection, its deficiency in knockout mice does not have an effect in the control of Mycobacterium tuberculosis infection |
-, 755118 |
| 3.4.21.78 | malfunction |
phenotypic characterization of gzmA-/- regulatory T cells (Tregs) efficiently homing to secondary lymphoid organs, GzmA-/- Tregs home efficiently to secondary lymphoid organs, overview. No difference between wild-type and GZMA-/- mice in Treg numbers in spleen and peripheral lymph nodes. Enzyme-deficient gzmA-/- Tregs cannot efficiently protect from GvHD-related inflammation and organ destruction in the intestinal tract with relevant crypt apoptosis detected in the small and large intestine |
755083 |
| 3.4.21.78 | malfunction |
pneumonia is induced in wild-type and GzmA-deficient (GzmA-/-) mice by intranasal inoculation of Streptococcus pneumoniae. In separate experiments, wild-type and GzmA-/- mice are treated with natural killer (NK) cell depleting antibodies. Upon infection, GzmA-/- mice show a better survival and lower bacterial counts in bronchoalveolar lavage fluid (BALF) and distant body sites compared to the wild-type mice. Although NK cells show strong GzmA expression, NK cell depletion does not influence bacterial loads in either wild-type or GzmA-/- mice. GzmA deficiency has little impact on lung pathology during late stage pneumococcal pneumonia |
-, 752445 |
| 3.4.21.78 | metabolism |
CD8 T cells in psoriasis skinlesions display a dominant expression of granzyme A (GzmA) over granzyme B in the absence of perforin expression. Signals recruiting GzmA+ T cells into the skin and triggers of GzmA expression in the context of chronic inflammation, Tc17-polarizing conditions favour development of GzmA+GzmB-Prf-CD8 T-cells in the context of psoriasis |
753512 |
| 3.4.21.78 | physiological function |
granzyme A contributes to the early inflammatory response in the lung. Granzyme A (GzmA) impairs host defense during Streptococcus pneumoniae pneumonia, role of GzmA on the host response during pneumococcal pneumonia, overview |
752445 |
| 3.4.21.78 | physiological function |
granzyme A contributes to the early inflammatory response in the lung. Granzyme A (GzmA) plays an unfavorable role in host defense during pneumococcal pneumonia by a mechanism that does not depend on natural killer cells. GzmA enhances bacterial dissemination and mortality in pneumococcal pneumonia |
-, 752445 |
| 3.4.21.78 | physiological function |
granzyme A is expressed in mouse lungs during Mycobacterium tuberculosis strain H37Rv infection but does not contribute to protection in vivo. Granzyme A does not have a crucial role in vivo in the protective response to tuberculosis |
-, 755118 |
| 3.4.21.78 | physiological function |
granzyme A is required for regulatory T-cell mediated prevention of gastrointestinal graft-versus-host disease. Analysis of the role of granzyme A (GZMA) in a haploidentical murine graft-versus-host disease (GvHD) model using gzmA-/- donor regulatory T cells (Tregs) to clarify the functional relevance of GZMA for Treg-mediated suppression of GvHD. GZMA expressing Tregs protect against GvHD-related tissue damage of the intestine |
755083 |
| 3.4.21.78 | physiological function |
histone H4 is cleaved by granzyme A during staurosporine-induced cell death in B-lymphoid Raji cells. A fast-migrating histone H4 fragment is detected in cells undergoing staurosporine-induced cell death. Treatment with caspase inhibitors (inhibitors of caspase-6 (Z-VEID-FMK) and caspase-9 (Z-LEHD-FMK)) increases both cell death and histone H4 cleavage. The enzyme cleaves the N-terminal tail pf H4. The cleavage of the histone H4 tail by GzmA contributes to the disintegration of chromosomes during the cell death process. The SET complex is normally located in the endoplasmic reticulum, but it translocates to the nucleus in response to reactive oxygen species produced by GzmA-mediated cleavage of NADH dehydrogenase (ubiquinone) Fe-S protein 3. GzmA is mobilized in the nucleus where many of its known substrates reside. In the nucleus, GzmA digests three components of the SET complex: SET, high-mobility group protein B2, and apurinic/apyrimidinic endonuclease. SET is an inhibitor of the SET complex endonuclease NM23-H1. GzmA degrades the linker histone H1 and removes the tails from core histones H2 and H3, opening up the chromatin and making it accessible to nucleases |
753077 |
