Disease relevance of GZMK

• Expression of enzymatically active human granzyme 3 in Escherichia coli for analysis of its substrate specificity [1].

High impact information on GZMK

• Using ICE deficient (ICE -/-) mice, embryonic fibroblasts exhibit high levels of resistance to apoptosis by granzyme B or granzyme 3, while B lymphoblasts are granzyme B-resistant, thus identifying an ICE-dependent apoptotic pathway that is activated by CTL granzymes [2].
• We recently cloned a rat granzyme tryptase (RNK-Tryp-2), and used this cDNA to screen human cDNA libraries [3].
• The N-terminal amino acid sequence deduced from HNK-Tryp-2 was identical to that reported for granzyme 3 [3].
• Cloning and expression of a second human natural killer cell granule tryptase, HNK-Tryp-2/granzyme 3 [3].
• However, the closest granzyme 3 homologue is the recently characterized rat tryptase, RNK-Tryp-2 (75% identity) [4].

Biological context of GZMK

• A fifth human granzyme (granzyme 3) has been biochemically purified and its N-terminal amino acid sequence has been reported [3].

Anatomical context of GZMK

• From Northern blots, granzyme 3 appears to be highly expressed in peripheral blood leukocytes, spleen, thymus, and lung tissues [4].

Associations of GZMK with chemical compounds

• Granzyme 3 has the expected features of the chymotrypsin family of serine proteases, and is closely related to other human granzymes (40-45% identity) [4].

References