Proteolytic inactivation of alpha-1-proteinase inhibitor by a neutrophil metalloproteinase.
AUTOR(ES)
Desrochers, P E
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=442601Documentos Relacionados
- Enzymatic reduction of oxidized alpha-1-proteinase inhibitor restores biological activity.
- A lymphokine regulates expression of alpha-1-proteinase inhibitor in human monocytes and macrophages.
- Regulation of alpha 1 proteinase inhibitor function by rabbit alveolar macrophages. Evidence for proteolytic rather than oxidative inactivation.
- A model of decreased functional alpha-1-proteinase inhibitor. Pulmonary pathology of dogs exposed to chloramine T.
- Oxidative regulation of neutrophil elastase-alpha-1-proteinase inhibitor interactions.
