Lactoferrin and yolkin-derived proteins increase the proteolytic capacity of the serine protease cathepsin G important for an immune response

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Abstract

Neutrophils secrete serine proteases, including cathepsin G (CatG), as a first cellular immune response against pathogens. CatG secreted at the site of inflammation has several functions, for instance, degrades pathogen-derived proteins, processes chemokines and cytokines, and plays an important role in antigen processing in the adaptive immune response.
We found that lactoferrin (LF) and yolkin, which is a polypeptide complex naturally occurring in hen’s egg yolk, enhanced the proteolytic activity of CatG. The data provided show that both LF and yolkin change the substrate selectivity of CatG, while combination of LF and yolkin inhibits the proteolytic activity of CatG. In addition, CatG, LF, and yolkin effectively reduce the cell viability of glioblastoma cell line in a proteolytically independent manner. Furthermore, LF upregulates cell surface major histocompatibility complex class I (MHC I) molecules on immune- and glioblastoma cells important for an immune response. In conclusion, we describe novel biochemical properties of LF and yolkin.
Original languageEnglish
Title of host publication2nd International Conference Biotechnology: Research and Industrial Application. Faculty of Biotechnology and Food Science Wroclaw, Poland. Oral presentation
Publication statusPublished - 2018

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