Granzymes are a family of serine proteases that play a crucial role in the immune system. They are primarily found in the granules of cytotoxic T lymphocytes (CTLs) and natural killer (NK) cells. These enzymes are released during the immune response to target and induce apoptosis in infected or malignant cells .
Granzyme-H (GzmH) is one of the five human granzymes, alongside Granzyme A, B, K, and M. It is a chymotrypsin-like serine protease predominantly expressed in NK cells . GzmH has unique substrate specificity and plays a significant role in the innate immune response against tumors and viral infections .
The recombinant form of Granzyme-H, produced in sf9 insect cells, is utilized for research and therapeutic purposes. The sf9 cell line, derived from the fall armyworm (Spodoptera frugiperda), is commonly used in biotechnology for the production of recombinant proteins. This system allows for the expression of human proteins with post-translational modifications similar to those in mammalian cells .
The structure of Granzyme-H has been studied to understand its substrate specificity and mechanism of action. The enzyme contains a unique RKR motif that helps define its binding regions, indicating a preference for acidic residues at specific sites . This structural information is crucial for designing inhibitors that can selectively block the enzymatic and cytotoxic activity of GzmH .
Given its role in immune responses, Granzyme-H has potential therapeutic applications. Understanding its structure and function can aid in the development of targeted therapies for cancer and viral infections. Additionally, recombinant Granzyme-H can be used in research to further explore its biological activities and potential clinical applications .