Advertisement

Research Article Free access | 10.1172/JCI113500

Proteolytic inactivation of alpha-1-proteinase inhibitor by a neutrophil metalloproteinase.

P E Desrochers and S J Weiss

Simpson Memorial Research Institute, Department of Internal Medicine, Ann Arbor, Michigan 48109.

Find articles by Desrochers, P. in: PubMed | Google Scholar

Simpson Memorial Research Institute, Department of Internal Medicine, Ann Arbor, Michigan 48109.

Find articles by Weiss, S. in: PubMed | Google Scholar

Published May 1, 1988 - More info

Published in Volume 81, Issue 5 on May 1, 1988
J Clin Invest. 1988;81(5):1646–1650. https://doi.org/10.1172/JCI113500.
© 1988 The American Society for Clinical Investigation
Published May 1, 1988 - Version history
View PDF
Abstract

Human neutrophils triggered with phorbol myristate acetate or opsonized zymosan particles released a metalloproteinase (MP) capable of cleaving and inactivating alpha-1-proteinase inhibitor (alpha-1-PI). Sequence analysis of the amino acids in proteolyzed, native alpha-1-PI revealed a unique single cleavage site between Phe-352 and Leu-353. An analysis of the process regulating the enzyme's activity revealed that the neutrophil MP was released from cells in a latent form whose activation was tightly linked to the generation of hypochlorous acid. These results indicate that human neutrophils use chlorinated oxidants to activate a latent MP that is capable of proteolytically inactivating alpha-1-PI by cleaving the antiproteinase at a unique point in its inhibitory site region.

Images.

Browse pages

Click on an image below to see the page. View PDF of the complete article

Version history
  • Version 1 (May 1, 1988): No description
Advertisement
Advertisement