Proteinase 3; a potential target in chronic obstructive pulmonary disease and other chronic inflammatory diseases

Research output: Contribution to journalReview articlepeer-review


Colleges, School and Institutes

External organisations

  • University of Birmingham
  • Institute of Inflammation and Ageing, College of Medical and Dental Sciences, Centre for Translational Inflammation Research, University of Birmingham Research Laboratories, Queen Elizabeth Hospital Birmingham, Mindelsohn Way, Birmingham, B15 2WB, UK.


Chronic Obstructive Pulmonary Disease (COPD) is a common, multifactorial lung disease which results in significant impairment of patients' health and a large impact on society and health care burden. It is believed to be the result of prolonged, destructive neutrophilic inflammation which results in progressive damage to lung structures. During this process, large quantities of neutrophil serine proteinases (NSPs) are released which initiate the damage and contribute towards driving a persistent inflammatory state.Neutrophil elastase has long been considered the key NSP involved in the pathophysiology of COPD. However, in recent years, a significant role for Proteinase 3 (PR3) in disease development has emerged, both in COPD and other chronic inflammatory conditions. Therefore, there is a need to investigate the importance of PR3 in disease development and hence its potential as a therapeutic target. Research into PR3 has largely been confined to its role as an autoantigen, but PR3 is involved in triggering inflammatory pathways, disrupting cellular signalling, degrading key structural proteins, and pathogen response.This review summarises what is presently known about PR3, explores its involvement particularly in the development of COPD, and indicates areas requiring further investigation.


Original languageEnglish
Article number180
JournalRespiratory research
Issue number1
Publication statusPublished - 20 Sep 2018


  • Chronic obstructive pulmonary disease, Inflammation, Lungs, Proteinase 3/myeloblastin, Serine proteinases