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Lactoferrin Is an Allosteric Enhancer of the Proteolytic Activity of Cathepsin G.

ABSTRACT: Protease-mediated degradation of proteins is critical in a plethora of physiological processes. Neutrophils secrete serine proteases including cathepsin G (CatG), neutrophile elastase (NE), and proteinase 3 (PR3) together with lactoferrin (LF) as a first cellular immune response against pathogens. Here, we demonstrate that LF increases the catalytic activity of CatG at physiological concentration, with its highest enhancing capacity under acidic (pH 5.0) conditions, and broadens the substrate selectivity of CatG. On a functional level, the enzymatic activity of CatG was increased in the presence of LF in granulocyte-derived supernatant. Furthermore, LF enhanced CatG-induced activation of platelets as determined by cell surface expression of CD62P. Consequently, LF-mediated enhancement of CatG activity might promote innate immunity during acute inflammation.

SUBMITTER: Eipper S

PROVIDER: S-EPMC4795699 | biostudies-literature | 2016

REPOSITORIES: biostudies-literature

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Lactoferrin Is an Allosteric Enhancer of the Proteolytic Activity of Cathepsin G.

Eipper Steffen S Steiner Robin R Lesner Adam A Sienczyk Marcin M Palesch David D Halatsch Marc-Eric ME Zaczynska Ewa E Heim Christopher C Hartmann Marcus D MD Zimecki Michal M Wirtz Christian Rainer CR Burster Timo T

PloS one 20160317 3

Protease-mediated degradation of proteins is critical in a plethora of physiological processes. Neutrophils secrete serine proteases including cathepsin G (CatG), neutrophile elastase (NE), and proteinase 3 (PR3) together with lactoferrin (LF) as a first cellular immune response against pathogens. Here, we demonstrate that LF increases the catalytic activity of CatG at physiological concentration, with its highest enhancing capacity under acidic (pH 5.0) conditions, and broadens the substrate se ...[more]

PMID: 26986619

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