Serine protease cathepsin G regulates adhesion-dependent neutrophil effector functions by modulating integrin clustering

Sofia Z. Raptis, Steven D. Shapiro, Pamela M. Simmons, Alec M. Cheng, Christine T.N. Pham

Research output: Contribution to journalArticle

57 Scopus citations

Abstract

The polymorphonuclear leukocyte (PMN)-derived serine proteases play a key role in immune complex (IC)-mediated inflammation. However, the mechanisms by which these proteases regulate inflammatory response remain largely undefined. Here, we show that IC-activated cathepsin G- and neutrophil elastase-deficient (CG/NE) PMNs adhered normally to IC-coated surfaces but did not undergo CD11b clustering and failed to initiate cytoskeletal reorganization and cell spreading. As a result, CG/NE-deficient PMNs exhibited severe defects in MIP-2 secretion and reactive oxygen intermediates production. Exogenously added CG, but not proteolytically inactive CG, was sufficient to restore these defects. These findings identify an important role for CG in integrin-dependent PMN effector functions that are separate from and downstream of integrin-dependent adhesion.

Original languageEnglish
Pages (from-to)679-691
Number of pages13
JournalImmunity
Volume22
Issue number6
DOIs
StatePublished - Jun 1 2005

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