Recombinant ArtinM activates mast cells

Mast cells are hematopoietically derived cells that play a role in inflammatory processes such as allergy, as well as in the immune response against pathogens by the selective and rapid release of preformed and lipid mediators, and the delayed release of cytokines. The native homotetrameric lectin A...

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Bibliographic Details
Published in:BMC immunology 2016-07, Vol.17 (1), p.22-22, Article 22
Main Authors: Barbosa-Lorenzi, Valéria Cintra, Cecilio, Nerry Tatiana, de Almeida Buranello, Patricia Andressa, Pranchevicius, Maria Cristina, Goldman, Maria Helena S, Pereira-da-Silva, Gabriela, Roque-Barreira, Maria Cristina, Jamur, Maria Célia, Oliver, Constance
Format: Article
Language:English
Subjects:
Animals
Artocarpus - immunology
beta-N-Acetylhexosaminidases - metabolism
Cell Degranulation
Cell Line
Cloning, Molecular
Escherichia coli - genetics
Health aspects
Histamine - metabolism
Immunoglobulin E - metabolism
Immunology
Immunomodulation
Interleukin-4 - metabolism
Lectins
Mannose - metabolism
Mast cells
Mast Cells - immunology
NF-kappa B - metabolism
Physiological aspects
Plant Lectins - immunology
Plant Lectins - isolation & purification
Protein Binding
Rats
Recombinant Proteins - immunology
Recombinant Proteins - isolation & purification
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Summary:Mast cells are hematopoietically derived cells that play a role in inflammatory processes such as allergy, as well as in the immune response against pathogens by the selective and rapid release of preformed and lipid mediators, and the delayed release of cytokines. The native homotetrameric lectin ArtinM, a D-mannose binding lectin purified from Artocarpus heterophyllus seeds, is one of several lectins that are able to activate mast cells. Besides activating mast cells, ArtinM has been shown to affect several biological responses, including immunomodulation and acceleration of wound healing. Because of the potential pharmacological application of ArtinM, a recombinant ArtinM (rArtinM) was produced in Escherichia coli. The current study evaluated the ability of rArtinM to induce mast cell degranulation and activation. The glycan binding specificity of rArtinM was similar to that of jArtinM. rArtinM, via its CRD, was able to degranulate, releasing β-hexosaminidase and TNF-α, and to promote morphological changes on the mast cell surface. Moreover, rArtinM induced the release of the newly-synthesized mediator, IL-4. rArtinM does not have a co-stimulatory effect on the FcεRI degranulation via. The IgE-dependent mast cell activation triggered by rArtinM seems to be dependent on NFkB activation. The lectin rArtinM has the ability to activate and degranulate mast cells via their CRDs. The present study indicates that rArtinM is a suitable substitute for the native form, jArtinM, and that rArtinM may serve as an important and reliable pharmacological agent.
ISSN:1471-2172
1471-2172
DOI:10.1186/s12865-016-0161-0