Release and Degradation of Angiotensin I and Angiotensin II from Angiotensinogen by Neutrophil Serine Proteinases

• Published in: Archives of biochemistry and biophysics 2002-01, Vol.397 (1), p.77-83
• Main Authors: Ramaha, Ahmed, Patston, Philip A.
• Format: Article
• Language: English
• Subjects: angiotensin; Angiotensin I - chemistry; Angiotensin I - metabolism; Angiotensin II - chemistry; Angiotensin II - metabolism; angiotensinogen; Angiotensinogen - chemistry; Binding Sites; Cathepsin G; Cathepsins - metabolism; Dose-Response Relationship, Drug; elastase; Electrophoresis, Polyacrylamide Gel; Humans; Inflammation; Models, Biological; Myeloblastin; neutrophil; Neutrophils - enzymology; Pancreatic Elastase - metabolism; Protein Binding; proteinase 3; proteolysis; Serine Endopeptidases - chemistry; Serine Endopeptidases - metabolism; serpin; Time Factors; Wound Healing
• ISSN: 0003-9861; 1096-0384
• DOI: 10.1006/abbi.2001.2687

Cathepsin G, elastase, and proteinase 3 are serine proteinases released by activated neutrophils. Cathepsin G can cleave angiotensinogen to release angiotensin II, but this activity has not been previously reported for elastase or proteinase 3. In this study we show that elastase and proteinase 3 can release angiotensin I from angiotensinogen and release angiotensin II from angiotensin I and angiotensinogen. The relative order of potency in releasing angiotensin II by the three proteinases at equivalent concentrations is cathepsin G > elastase > proteinase 3. When all three proteinases are used together, the release of angiotensin II is greater than the sum of the release when each proteinase is used individually. Cathepsin G and elastase can also degrade angiotensin II, reactions which might be important in regulating the activity of angiotensin II. The release and degradation of angiotensin II by the neutrophil proteinases are reactions which could play a role in the local inflammatory response and wound healing.