PR3 overexpression 293T lysate (whole cell)

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Proteinase 3 (PR3) also known as PRTN3 is a serine protease with a mass of approximately 29 kDa. It belongs to the human neutrophil elastase (HNE) family and is mainly expressed in neutrophils. Within these immune cells PR3 localizes to azurophilic granules where it participates in early immune responses. The proteolytic activity of PR3 involves cleaving peptide bonds in target proteins contributing to the processing and degradation of various proteins important for immune function.

Biological function summary

Proteinase 3 serves multiple roles including modulating inflammation and immune responses. PR3 functions as part of a complex with azurophilic granules aiding in microbial defense mechanisms. In addition the protease regulates cytokine activation and deactivation which in turn influences cell signaling related to inflammation. Its enzymatic action ensures that PR3 can manage inflammatory processes by breaking down extracellular matrix components thereby allowing white blood cells to access infection sites.

Pathways

Proteinase 3 plays an important role within the serine protease and inflammatory pathways. It interacts with other proteins such as neutrophil elastase with which it shares a pathway to modulate immune responses. PR3 also partners with cathepsin G contributing to processes such as pathogen clearance and tissue remodeling providing a coordinated response during infection and injury. These interactions show PR3's involvement in regulating the balance between inflammation and tissue repair.

PR3 is notably associated with Wegener's granulomatosis also known as granulomatosis with polyangiitis. This autoimmune condition results in systemic vasculitis where anti-proteinase 3 antibodies notably characterize the disease. Additionally PR3 plays a part in chronic obstructive pulmonary disease (COPD) where its proteolytic activity contributes to tissue damage in the lungs. In both conditions PR3 interplays with related proteins like myeloperoxidase further demonstrating its importance in processes leading to these disorders.