Dear Colleagues,

Several of the hematopoietic cell lineages store massive amounts of serine proteases in cytoplasmic secretory granules. These proteases, which can account for up to 35% of the total cellular protein, are stored in an active form, ready for rapid release upon cell activation. In mammals, these proteases are expressed primarily by mast cells, neutrophils, cytotoxic T cells, and NK cells and they are encoded from four different chromosomal loci. Known functions involve activation of apoptosis in target cells, inducing cytokine production, regulating blood pressure, inactivating snake and scorpion toxins, regulating coagulation, regulating cytokine activity as well as participating in tissue homeostasis. Some of them are very active and have a relatively broad specificity and thereby many potential targets, whereas others are highly specific with only one or a few selected targets. Although much is known about these proteases, very much remains unknown. A few examples of important unsolved questions are: why do mast cells continuously produce such high amounts of these proteases; another is the major target for one of the recently identified highly specific neutrophil proteases (NSP4); and what is the prime function of the most highly conserved members of this subfamily of serine proteases (the granzymes A and K)? This Special Issue will try to address some of these important outstanding questions in the area of hematopoietic serine proteases.

Prof. Lars Hellman
Guest Editor

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• serine protease
• cleavage specificity
• mast cell
• neutrophilic granulocyte
• cytotoxic T cell
• NK cell
• immune regulation
• toxin
• tissue homeostasis
• angiotensin
• cytokines