Lactoferrin Is an Allosteric Enhancer of the Proteolytic Activity of Cathepsin G.
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. H...
| Main Authors: | , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2016-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC4795699?pdf=render |
| _version_ | 1818174578717884416 |
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| author | Steffen Eipper Robin Steiner Adam Lesner Marcin Sienczyk David Palesch Marc-Eric Halatsch Ewa Zaczynska Christopher Heim Marcus D Hartmann Michal Zimecki Christian Rainer Wirtz Timo Burster |
| author_facet | Steffen Eipper Robin Steiner Adam Lesner Marcin Sienczyk David Palesch Marc-Eric Halatsch Ewa Zaczynska Christopher Heim Marcus D Hartmann Michal Zimecki Christian Rainer Wirtz Timo Burster |
| author_sort | Steffen Eipper |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-11T19:46:38Z |
| format | Article |
| id | doaj.art-d3ce30b2596a4d178a0a69b6c596b172 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-11T19:46:38Z |
| publishDate | 2016-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-d3ce30b2596a4d178a0a69b6c596b1722022-12-22T00:52:53ZengPublic Library of Science (PLoS)PLoS ONE1932-62032016-01-01113e015150910.1371/journal.pone.0151509Lactoferrin Is an Allosteric Enhancer of the Proteolytic Activity of Cathepsin G.Steffen EipperRobin SteinerAdam LesnerMarcin SienczykDavid PaleschMarc-Eric HalatschEwa ZaczynskaChristopher HeimMarcus D HartmannMichal ZimeckiChristian Rainer WirtzTimo BursterProtease-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.http://europepmc.org/articles/PMC4795699?pdf=render |
| spellingShingle | Steffen Eipper Robin Steiner Adam Lesner Marcin Sienczyk David Palesch Marc-Eric Halatsch Ewa Zaczynska Christopher Heim Marcus D Hartmann Michal Zimecki Christian Rainer Wirtz Timo Burster Lactoferrin Is an Allosteric Enhancer of the Proteolytic Activity of Cathepsin G. PLoS ONE |
| title | Lactoferrin Is an Allosteric Enhancer of the Proteolytic Activity of Cathepsin G. |
| title_full | Lactoferrin Is an Allosteric Enhancer of the Proteolytic Activity of Cathepsin G. |
| title_fullStr | Lactoferrin Is an Allosteric Enhancer of the Proteolytic Activity of Cathepsin G. |
| title_full_unstemmed | Lactoferrin Is an Allosteric Enhancer of the Proteolytic Activity of Cathepsin G. |
| title_short | Lactoferrin Is an Allosteric Enhancer of the Proteolytic Activity of Cathepsin G. |
| title_sort | lactoferrin is an allosteric enhancer of the proteolytic activity of cathepsin g |
| url | http://europepmc.org/articles/PMC4795699?pdf=render |
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