Cementoin-SLPI fusion protein binds to human monocytes and epithelial cells and shows higher biological activity than SLPI

Secretory Leukocyte Proteinase Inhibitor (SLPI) is an antiinflammatory peptide that blocks the activity of serine proteases, primarily the neutrophil elastase. In an attempt to direct the activity of SLPI on inflamed sites, a chimera consisting of the transglutaminase II substrate domain of trappin...

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Autores principales: Maffía, P.C., Guerrieri, D., Villalonga, X., Caro, F., Gómez, S., Tateosian, N., Bogado, B.P., Sánchez, M.L., Ambrosi, N., Chuluyan, E.
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Acceso en línea:http://hdl.handle.net/20.500.12110/paper_20452322_v8_n1_p_Maffia
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
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spelling todo:paper_20452322_v8_n1_p_Maffia2023-10-03T16:38:26Z Cementoin-SLPI fusion protein binds to human monocytes and epithelial cells and shows higher biological activity than SLPI Maffía, P.C. Guerrieri, D. Villalonga, X. Caro, F. Gómez, S. Tateosian, N. Bogado, B.P. Sánchez, M.L. Ambrosi, N. Chuluyan, E. Secretory Leukocyte Proteinase Inhibitor (SLPI) is an antiinflammatory peptide that blocks the activity of serine proteases, primarily the neutrophil elastase. In an attempt to direct the activity of SLPI on inflamed sites, a chimera consisting of the transglutaminase II substrate domain of trappin 2 (cementoin), and the mature SLPI protein was constructed. Cell attachment and biological activity were compared between SLPI and this chimera. By using whole cell ELISA, fluorescence microscopy and flow cytometry assays we observed that the cementoin-SLPI fusion protein (FP) but not SLPI attached to a human lung epithelial cell line and monocytes. A maximum attachment was achieved 15 min after FP was added to the cell cultures. In an elastase activity assay, we observed that FP retained its antiprotease activity and that at equimolar amount of proteins, FP was more efficient than SLPI in the inhibition. Both, FP and SLPI inhibits IL-2-induced lymphocyte proliferation, however, lower amounts of FP were required to achieve this inhibition. Furthermore, FP binds to mycobacteria and maintained the bactericidal activity observed for SLPI. Overall, these results show that this new chimera is able to attach to the cell surfaces retaining and improving some biological activities described for SLPI. © 2018 The Author(s). JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_20452322_v8_n1_p_Maffia
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
description Secretory Leukocyte Proteinase Inhibitor (SLPI) is an antiinflammatory peptide that blocks the activity of serine proteases, primarily the neutrophil elastase. In an attempt to direct the activity of SLPI on inflamed sites, a chimera consisting of the transglutaminase II substrate domain of trappin 2 (cementoin), and the mature SLPI protein was constructed. Cell attachment and biological activity were compared between SLPI and this chimera. By using whole cell ELISA, fluorescence microscopy and flow cytometry assays we observed that the cementoin-SLPI fusion protein (FP) but not SLPI attached to a human lung epithelial cell line and monocytes. A maximum attachment was achieved 15 min after FP was added to the cell cultures. In an elastase activity assay, we observed that FP retained its antiprotease activity and that at equimolar amount of proteins, FP was more efficient than SLPI in the inhibition. Both, FP and SLPI inhibits IL-2-induced lymphocyte proliferation, however, lower amounts of FP were required to achieve this inhibition. Furthermore, FP binds to mycobacteria and maintained the bactericidal activity observed for SLPI. Overall, these results show that this new chimera is able to attach to the cell surfaces retaining and improving some biological activities described for SLPI. © 2018 The Author(s).
format JOUR
author Maffía, P.C.
Guerrieri, D.
Villalonga, X.
Caro, F.
Gómez, S.
Tateosian, N.
Bogado, B.P.
Sánchez, M.L.
Ambrosi, N.
Chuluyan, E.
spellingShingle Maffía, P.C.
Guerrieri, D.
Villalonga, X.
Caro, F.
Gómez, S.
Tateosian, N.
Bogado, B.P.
Sánchez, M.L.
Ambrosi, N.
Chuluyan, E.
Cementoin-SLPI fusion protein binds to human monocytes and epithelial cells and shows higher biological activity than SLPI
author_facet Maffía, P.C.
Guerrieri, D.
Villalonga, X.
Caro, F.
Gómez, S.
Tateosian, N.
Bogado, B.P.
Sánchez, M.L.
Ambrosi, N.
Chuluyan, E.
author_sort Maffía, P.C.
title Cementoin-SLPI fusion protein binds to human monocytes and epithelial cells and shows higher biological activity than SLPI
title_short Cementoin-SLPI fusion protein binds to human monocytes and epithelial cells and shows higher biological activity than SLPI
title_full Cementoin-SLPI fusion protein binds to human monocytes and epithelial cells and shows higher biological activity than SLPI
title_fullStr Cementoin-SLPI fusion protein binds to human monocytes and epithelial cells and shows higher biological activity than SLPI
title_full_unstemmed Cementoin-SLPI fusion protein binds to human monocytes and epithelial cells and shows higher biological activity than SLPI
title_sort cementoin-slpi fusion protein binds to human monocytes and epithelial cells and shows higher biological activity than slpi
url http://hdl.handle.net/20.500.12110/paper_20452322_v8_n1_p_Maffia
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