Your browser doesn't support javascript.
Mostrar: 20 | 50 | 100
Resultados 1 - 2 de 2
Mais filtros

Base de dados
Intervalo de ano de publicação
Int J Biol Macromol ; 82: 22-30, 2016 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-26433176


Recent advances in glycobiology have revealed the essential role of lectins in deciphering the glycocodes at the cell surface to generate important biological signaling responses. ArtinM, a d-mannose-binding lectin isolated from the seeds of jackfruit (Artocarpus heterophyllus), is composed of 16 kDa subunits that are associated to form a homotetramer. Native ArtinM (n-ArtinM) exerts immunomodulatory and regenerative effects, but the potential pharmaceutical applicability of the lectin is highly limited by the fact that its production is expensive, laborious, and impossible to be scaled up. This led us to characterize a recombinant form of the lectin obtained by expression in Saccharomyces cerevisiae (y-ArtinM). In the present study, we demonstrated that y-ArtinM is similar to n-ArtinM in subunit arrangement, oligomerization and carbohydrate binding specificity. We showed that y-ArtinM can exert n-ArtinM biological activities such as erythrocyte agglutination, stimulation of neutrophil migration and degranulation, mast cell degranulation, and induction of interleukin-12 and interleukin-10 production by macrophages. In summary, the expression of ArtinM in yeast resulted in successful production of an active, recombinant form of ArtinM that is potentially useful for pharmaceutical application.

Carboidratos/química , Lectinas de Ligação a Manose/química , Estrutura Molecular , Proteínas Recombinantes , Animais , Degranulação Celular/efeitos dos fármacos , Degranulação Celular/imunologia , Movimento Celular/efeitos dos fármacos , Movimento Celular/imunologia , Citocinas/biossíntese , Hemaglutinação , Humanos , Macrófagos/efeitos dos fármacos , Macrófagos/imunologia , Macrófagos/metabolismo , Masculino , Lectinas de Ligação a Manose/metabolismo , Lectinas de Ligação a Manose/farmacologia , Mastócitos/efeitos dos fármacos , Mastócitos/imunologia , Mastócitos/metabolismo , Camundongos , Neutrófilos/efeitos dos fármacos , Neutrófilos/imunologia , Neutrófilos/metabolismo , Polissacarídeos/química , Ligação Proteica , Receptor 2 Toll-Like , Leveduras/genética , Leveduras/metabolismo
Biochem Biophys Res Commun ; 416(3-4): 318-24, 2011 Dec 16.
Artigo em Inglês | MEDLINE | ID: mdl-22108054


Mast cells are inflammatory cells that respond to signals of innate and adaptive immunity with immediate and delayed release of mediators. ArtinM, a lectin from Artocarpus integrifolia with immunomodulatory activities, is able to induce mast cell activation, but the mechanisms remain unknown. This study sought to further investigate the effects of the lectin on mast cells. We showed that ArtinM binds to mast cells, possibly to the high affinity receptor for immunoglobulin E (IgE) - FcεRI - and/or to IgE bound to FcεRI. Binding of the lectin resulted in protein tyrosine phosphorylation and release of the pre- and newly-formed mediators, ß-hexosaminidase and LTB(4) by mast cells, activities that were potentiated in the presence of IgE. ArtinM also induced the activation of the transcription factors NFκB and NFAT, resulting in expression of some of their target genes such as IL-4 and TNF-α. In view of the established significance of mast cells in many immunological and inflammatory reactions, a better understanding of the mechanisms involved in mast cell activation by ArtinM is crucial to the pharmacological application of the lectin.

Artocarpus/química , Mastócitos/imunologia , Lectinas de Plantas/imunologia , Receptores de IgE/imunologia , Animais , Linhagem Celular , Expressão Gênica , Imunoglobulina E/imunologia , Mastócitos/efeitos dos fármacos , NF-kappa B/agonistas , Fatores de Transcrição NFATC/agonistas , Fosforilação , Lectinas de Plantas/metabolismo , Lectinas de Plantas/farmacologia , Ratos , Tirosina/metabolismo