3.4.21.B4: granzyme K
This is an abbreviated version!
For detailed information about granzyme K, go to the full flat file.
Word Map on EC 3.4.21.B4
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3.4.21.B4
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perforin
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spastic
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paraplegia
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oxysterols
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neurosteroids
- 3.4.21.B4
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perforin
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spastic
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paraplegia
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oxysterols
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neurosteroids
Reaction
endopeptidase activity. Cleaves after Lys and Arg =
Synonyms
fragmentin, Gr3, granzyme 3, granzyme K, granzyme tryptase K, GRK, grzK, Gzm K, GzmK, lymphocyte tryptase 2, RNK-Tryp-2, S01.146, tryptase
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General Information
General Information on EC 3.4.21.B4 - granzyme K
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physiological function
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granzyme K induces pro-inflammatory cytokine release (interleukin-6, interleukin-8 and monocyte chemotactic protein-1) through the activation of protease-activated receptor-1, induces activation of both the ERK1/2 and p38 MAP kinase signaling pathways, and significantly increases fibroblast proliferation
physiological function
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valosin-containing protein cleavage by granzyme K accelerates an endoplasmic reticulum stress leading to caspase-independent cytotoxicity of target tumor cells
physiological function
granzymes are serine proteases released by cytotoxic lymphocytes to induce apoptosis in virus-infected cells and tumor cells. Granzymes also play a role in controlling inflammation. Granzyme K binds to Gram-negative bacteria, e.g. Escherichia coli BL21, Pseudomonas aeruginosa, and Neisseria meningitides, and their cell-wall component lipopolysaccharide. The enzyme synergistically enhances lipopolysaccharide-induced cytokine release in vitro from primary human monocytes and in vivo in a mouse model of lipopolysaccharide challenge. The synergistic effect of the enzyme and lipopolysacchride on monocytes is dependent on cluster of differentiation 14, but the extracellular effects are independent of the enzyme catalytic activity. The enzyme disaggregates lipopolysaccharides from micelles and augments LPS-CD14 complex formation, thereby likely boosting monocyte activation by lipopolysaccharides. The extracellular enzyme is a direct modulator of LPS-TLR4 signaling during the antimicrobial innate immune response, detailed overview
physiological function
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the enzyme has a role in cytotoxic and inflammatory processes
physiological function
the enzyme has a role in cytotoxic and inflammatory processes
physiological function
extracellular granzyme K proteolytically activates protease-activated receptor-1 leading to increased interleukin 6 and monocyte chemotactic protein 1 production in endothelial cells. Granzyme K also increases tumour necrosis factor alpha-induced inflammatory adhesion molecule expression
physiological function
granzyme K expression in testes is testosterone dependent. Granzyme K is located adjacent to germ cells in seminiferous tubules and may be involved in the degradation of microtubules in ectoplasmic specializations
physiological function
GzmK influences wound healing by augmenting inflammation and impeding epithelialization. GzmK-/- mice exhibit improved wound closure, matrix organization, and tensile strength compared with wild-type mice. Reduced proinflammatory IL-6, ICAM-1, VCAM-1, and MCP-1 expressions are observed at 3 days after injury. GzmK induces IL-6 expression in keratinocytes and skin fibroblasts that is dependent on PAR-1 activation. Keratinocytes, but not skin fibroblasts, exposed to GzmK show impaired wound healing in vitro
physiological function
in burn tissue, granzyme K expression is elevated compared with normal skin, with expression predominantly found in macrophages. Granzyme K is expressed and secreted by cultured human classically activated macrophages