Proteinase 3 has been shown to be important in the pathogenesis of human emphysema. It has also been used in a study to investigate the liberation of the antibacterial and cytotoxic peptide LL-37 by cleavage of human cathelicidin hCAP-183.
Proteinase 3 (PR3) is mapped to human chromosome 19p13.3. Proteinase 3 is present majorly in azurophilic granules and belongs to neutrophil-derived proteases family. PR3 is a peripheral membrane protein and lacks transmembrane domain. It comprises of an unique interfacial binding site (IBS) and two amino acid clusters, one charged and one hydrophobic, for membrane association.
Proteinase 3 (PR-3) is a serine protease expressed in the granules of neutrophils and monocytes. Also known as myeloblastin and p29b, it degrades elastin and is associated with myeloid leukemia and Wegener′s granulomatosis.
