GZMK
GZMK (granzyme K) is a serine protease released by CD8(+) T-cells that initiates the GZMK pathway of the complement system. It is also known as TRYP2 or PRSS, and belongs to the granule-associated serine proteases of immune defence. Browse Assay Genie's current range of GZMK research reagents below, or read on for the biology behind the target.
GZMK is a serine protease that initiates the GZMK pathway of the complement system, a cascade directly activated by CD8(+) T-cells that leads to phagocytosis and breakdown of pathogens and to signalling that strengthens adaptive immunity. The protein is specifically secreted by CD8(+) T-cells and mediates both the recognition and initiation steps of this pathway. It first acts as a pattern recognition receptor, binding heparan sulfate glycosaminoglycans on the pathogen surface to drive opsonisation. It then catalyses cleavage and activation of C2 and C4, the next components of the cascade. GZMK-mediated complement activation is an important contributor to tissue inflammation.
Beyond complement, GZMK can cleave and activate the protease-activated receptors F2R/PAR1 and PAR2/F2RL1, possibly promoting interleukin release. It may also regulate apoptosis by cleaving and activating BID, which promotes cytochrome C release from mitochondria. UniProt records the protein as secreted, at the cell surface and in cytoplasmic granules, and places it in the peptidase S1 family, granzyme subfamily.
The GZMK gene encodes one of a group of related serine proteases found in the cytoplasmic granules of cytotoxic lymphocytes. Cytolytic T lymphocytes and natural killer cells recognise, bind and lyse target cells bearing 'nonself' antigens, typically derived from intracellular pathogens. Unlike other granzymes, this protein lacks consensus sequences for N-glycosylation. Earlier HGNC names for the gene were granzyme 3 and tryptase II, which explains the TRYP2 alias. Mouse and rat both have a Gzmk ortholog.
GZMK starts a complement pathway by binding heparan sulfate and cleaving C2 and C4, making it a focus for studying T-cell-driven complement activation.
GZMK-mediated complement activation contributes to tissue inflammation, and the protease may promote interleukin release through PAR1 and PAR2 cleavage.
As a granule protease of cytotoxic lymphocytes, GZMK helps researchers examine how CD8(+) T-cells and NK cells protect the host.
GZMK may cleave and activate BID, promoting cytochrome C release, which links the protease to the regulation of apoptosis.
GZMK is a serine protease secreted by CD8(+) T-cells. It binds heparan sulfate on pathogen surfaces to drive opsonisation, then cleaves C2 and C4 to initiate the GZMK complement pathway. It can also activate PAR1, PAR2 and BID.
The HGNC name is granzyme K. Aliases include TRYP2 and PRSS, and earlier names were granzyme 3 and tryptase II. These names appear in older literature, so searching them alongside GZMK helps when reviewing past work.
Yes. Mouse and rat each have an ortholog named Gzmk. GZMK belongs to the granzyme subfamily of the peptidase S1 family. Check the datasheet of any product for its validated reactivity.
Other granzymes, complement components, protease-activated receptors and apoptosis regulators linked to GZMK biology.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P49863; product specifications from Assay Genie datasheets.