NDLI: Olfactomedin 4 inhibits cathepsin C-mediated protease activities, thereby modulating neutrophil killing of Staphylococcus aureus and Escherichia coli in mice.

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Olfactomedin 4 inhibits cathepsin C-mediated protease activities, thereby modulating neutrophil killing of Staphylococcus aureus and Escherichia coli in mice.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Yan, Ming Coleman, William G. Rodgers, Griffin P. Liu, Yueqin McLeish, Kenneth R. Liu, Wenli
Description	Country affiliation: United States Author Affiliation: Liu W ( Molecular and Clinical Hematology Branch, National Heart, Lung, and Blood Institute, Bethesda, MD 20892, USA.)
Abstract	Neutrophils kill bacteria generally through oxidative and nonoxidative mechanisms. Whereas much research has focused on the enzymes essential for neutrophil killing, little is known about the regulatory molecules responsible for such killing. In this study, we investigated the role of olfactomedin 4 (OLFM4), an olfactomedin-related glycoprotein, in neutrophil bactericidal capability and host innate immunity. Neutrophils from OLFM4â »/â » mice have increased intracellular killing of Staphylococcus aureus and Escherichia coli in vitro. The OLFM4â »/â » mice have enhanced in vivo bacterial clearance and are more resistant to sepsis when challenged with S. aureus or E. coli by i.p. injection. OLFM4 was found to interact with cathepsin C, a cysteine protease that plays an important role in bacterial killing and immune regulation. We demonstrated that OLFM4 inhibited cathepsin C activity in vitro and in vivo. The cathepsin C activity in neutrophils from OLFM4â »/â » mice was significantly higher than that in neutrophils from wild-type littermate mice. The activities of three serine proteases (neutrophil elastase, cathepsin G, and proteinase 3), which require cathepsin C activity for processing and maturity, were also significantly higher in OLFM4â »/â » neutrophils. The bacterial killing and clearance capabilities observed in OLFM4â »/â » mice that were enhanced relative to wild-type mice were significantly compromised by the additional loss of cathepsin C in mice with OLFM4 and cathepsin C double deficiency. These results indicate that OLFM4 is an important negative regulator of neutrophil bactericidal activity by restricting cathepsin C activity and its downstream granule-associated serine proteases.
ISSN	00221767
e-ISSN	15506606
DOI	10.4049/jimmunol.1103179
Journal	The Journal of Immunology
Issue Number	5
Volume Number	189
Language	English
Publisher	The American Association of Immunologists
Publisher Date	2012-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Cathepsin C Antagonists & Inhibitors Escherichia Coli Infections Immunology Granulocyte Colony-stimulating Factor Physiology Neutrophil Activation Protease Inhibitors Metabolism Staphylococcal Infections Animals Enzymology Pathology Deficiency Hek293 Cells Hela Cells Mice Mice, Inbred C57bl Mice, Knockout Research Support, N.i.h., Extramural Research Support, N.i.h., Intramural Discipline Immunology
Content Type	Text
Resource Type	Article
Subject	Immunology and Allergy Immunology

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