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Citations to this article

Proteolytic inactivation of alpha-1-proteinase inhibitor by a neutrophil metalloproteinase.
P E Desrochers, S J Weiss
P E Desrochers, S J Weiss
Published May 1, 1988
Citation Information: J Clin Invest. 1988;81(5):1646-1650. https://doi.org/10.1172/JCI113500.
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Research Article Article has an altmetric score of 6

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

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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.

Authors

P E Desrochers, S J Weiss

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Year: 2023 2018 2017 2013 2011 2008 2007 2006 2005 2004 2002 2001 2000 1997 1996 1995 1994 1993 1992 1991 1990 1989 1986 1985 1983 1981 Total
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