title: Recombinant ArtinM activates mast cells.
abstract: 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.
authors.affiliation: Department of Cell and Molecular Biology and Pathogenic Bioagents, Ribeirão Preto Medical School, University of São Paulo, Ribeirão Preto, SP, Brazil.|Present address: Department of Biochemistry, Weill Cornell Medical College of Cornell University, New York, NY, USA.
authors.forename: Valéria Cintra
authors.initials: VC
authors.lastname: Barbosa-Lorenzi
authors.affiliation: Department of Cell and Molecular Biology and Pathogenic Bioagents, Ribeirão Preto Medical School, University of São Paulo, Ribeirão Preto, SP, Brazil.
authors.forename: Nerry Tatiana
authors.initials: NT
authors.lastname: Cecilio
authors.affiliation: Department of Cell and Molecular Biology and Pathogenic Bioagents, Ribeirão Preto Medical School, University of São Paulo, Ribeirão Preto, SP, Brazil.|Present address: Department of Biological Sciences, Universidade Federal do Triangulo Mineiro, Uberaba, MG, Brazil.
authors.forename: Patricia Andressa
authors.initials: PA
authors.lastname: de Almeida Buranello
authors.affiliation: Department of Cell and Molecular Biology and Pathogenic Bioagents, Ribeirão Preto Medical School, University of São Paulo, Ribeirão Preto, SP, Brazil.|Present address: Department of Genetics and Evolution, Universidade Federal de São Carlos, São Carlos, SP, Brazil.
authors.forename: Maria Cristina
authors.initials: MC
authors.lastname: Pranchevicius
authors.affiliation: Department of Biology, Faculdade de Filosofia Ciências e Letras de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto, SP, Brazil.
authors.forename: Maria Helena S
authors.initials: MH
authors.lastname: Goldman
authors.affiliation: Department of Maternal-Infant Nursing and Public Health, Escola de Enfermagem de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto, SP, Brazil.
authors.forename: Gabriela
authors.initials: G
authors.lastname: Pereira-da-Silva
authors.affiliation: Department of Cell and Molecular Biology and Pathogenic Bioagents, Ribeirão Preto Medical School, University of São Paulo, Ribeirão Preto, SP, Brazil.
authors.forename: Maria Cristina
authors.initials: MC
authors.lastname: Roque-Barreira
authors.affiliation: Department of Cell and Molecular Biology and Pathogenic Bioagents, Ribeirão Preto Medical School, University of São Paulo, Ribeirão Preto, SP, Brazil.
authors.forename: Maria Célia
authors.initials: MC
authors.lastname: Jamur
authors.affiliation: Department of Cell and Molecular Biology and Pathogenic Bioagents, Ribeirão Preto Medical School, University of São Paulo, Ribeirão Preto, SP, Brazil. coliver@fmrp.usp.br.
authors.forename: Constance
authors.identifier: 0000-0002-8633-4612
authors.initials: C
authors.lastname: Oliver
mesh_terms: D000818:Animals; D031622:Artocarpus / Q000276:immunology; D015550:Cell Degranulation; D002460:Cell Line; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics; D006632:Histamine / Q000378:metabolism; D007073:Immunoglobulin E / Q000378:metabolism; D056747:Immunomodulation; D015847:Interleukin-4 / Q000378:metabolism; D008358:Mannose / Q000378:metabolism; D008407:Mast Cells / Q000276:immunology*; D016328:NF-kappa B / Q000378:metabolism; D037121:Plant Lectins / Q000276:immunology* / Q000302:isolation & purification; D011485:Protein Binding; D051381:Rats; D011994:Recombinant Proteins / Q000276:immunology* / Q000302:isolation & purification; D001619:beta-N-Acetylhexosaminidases / Q000378:metabolism
chemical_list: D016328:NF-kappa B; D037121:Plant Lectins; D011994:Recombinant Proteins; D015847:Interleukin-4; D007073:Immunoglobulin E; D006632:Histamine; D001619:beta-N-Acetylhexosaminidases; D008358:Mannose
keywords: ArtinM; Degranulation; Lectin; Mast cells; rArtinM