Lactoferrin Is an Allosteric Enhancer of the Proteolytic Activity of Cathepsin G
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Date
2016-03-17
Authors
Eipper, Steffen
Steiner, Robin
Lesner, Adam
Sienczyk, Marcin
Palesch, David
Halatsch, Marc- Eric
Zaczynska, Ewa
Heim, Christopher
Hartmann, Marcus D.
Zimecki, Michal
Journal Title
Journal ISSN
Volume Title
Publisher
PLOS ONE
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 granulocytederived
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.
Description
Keywords
lactoferrin, cathepsin G
Citation
Eipper S, Steiner R, Lesner A, Sienczyk M, Palesch D, Halatsch M-E, et al. (2016) Lactoferrin Is an Allosteric Enhancer of the Proteolytic Activity of Cathepsin G. PLoS ONE 11(3): e0151509. doi:10.1371/journal.pone.0151509