Frutalin, a galactose-binding lectin, induces chemotaxis and rearrangement of actin cytoskeleton in human neutrophils: Involvement of tyrosine kinase and phosphoinositide 3-kinase

Brando-Lima, Aline C.; Saldanha-Gama, Roberta; Henriques, Maria das Graças; Monteiro-Moreira, Ana Cristina de Oliveira; Moreira, Renato de Azevedo; Barja‐Fidalgo, Christina

doi:10.1016/j.taap.2005.02.012

Cited by 23 publications

(10 citation statements)

References 34 publications

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“…FTL has been tested for biomedical applications, particularly because of its notable antitumour properties (Oliveira et al, 2011), potential as a tumour biomarker (Oliveira, Costa et al, 2009), immunomodulatory effects (Brando-Lima et al, 2005, 2006, gastroprotective effects (de Vasconcelos Abdon et al, 2012), cytotoxicity (Oliveira et al, 2011), glycomembrane interaction (Nobre et al, 2010) and chemotaxis (Brando-Lima et al, 2005). We have performed the crystallization and X-ray diffraction analysis of native FTL in order to solve its threedimensional structure.…”

Section: Introductionmentioning

confidence: 99%

Crystallization and preliminary X-ray diffraction studies of frutalin, an α-D-galactose-specific lectin fromArtocarpus incisaseeds

Monteiro-Moreira

Pereira²,

Neto

et al. 2015

Acta Cryst Sect F

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Frutalin is an -d-galactose-specific carbohydrate-binding glycoprotein with antitumour properties and is a powerful tool for tumour biomarker discovery. The crystallization and preliminary X-ray diffraction analysis of this lectin, which was isolated from Artocarpus incisa seeds, are reported here. Frutalin was purified and submitted to mass-spectrometric analysis. Diverse masses at approximately 16 kDa were observed in the deconvoluted spectra, which support the presence of isoforms. The best frutalin crystals were grown within a week in 0.1 M citric acid pH 3.5 which contained 25% PEG 3350 as a precipitant at 293 K, and diffracted to a maximum resolution of 1.81 Å . The monoclinic crystals belonged to space group I2, with unit-cell parameters a = 76.17, b = 74.56, c = 118.98 Å , = 96.56 . A molecular-replacement solution was obtained which indicated the presence of four monomers per asymmetric unit. Crystallographic refinement of the structure is in progress.

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Section: Introductionmentioning

confidence: 99%

Crystallization and preliminary X-ray diffraction studies of frutalin, an α-D-galactose-specific lectin fromArtocarpus incisaseeds

Monteiro-Moreira

Pereira²,

Neto

et al. 2015

Acta Cryst Sect F

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“…Previous studies have shown that frutalin plays an important role in many biomedical applications. This lectin was able to induce mice neutrophil migration in vivo, and to be a potent direct chemotactic for human neutrophils and stimulator of human lymphocytes, both in vitro [8,9]. Considering the potential biological applications of frutalin, it is very important to develop a strategy to increase its production.…”

Section: Introductionmentioning

confidence: 99%

cDNA Cloning and Functional Expression of the α-d-Galactose-Binding Lectin Frutalin in Escherichia coli

et al. 2009

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cDNA clones encoding frutalin, the alpha-D-galactose-binding lectin expressed in breadfruit seeds (Artocarpus incisa), were isolated and sequenced. The deduced amino acid sequences indicated that frutalin may be encoded by a family of genes. The NCBI database searches revealed that the frutalin sequence is highly homologous with jacalin and mornigaG sequences. Frutalin cDNA was re-amplified and cloned into the commercial expression vector pET-25b(+) for frutalin production in Escherichia coli. An experimental factorial design was employed to maximise the soluble expression of the recombinant lectin. The results indicated that temperature, time of induction, concentration of IPTG and the interaction between the concentration of IPTG and the time of induction had the most significant effects on the soluble expression level of recombinant frutalin. The optimal culture conditions were as follows: induction with 1 mM IPTG at 22 degrees C for 20 h, yielding 16 mg/l of soluble recombinant frutalin. SDS-PAGE and Western blot analysis revealed that recombinant frutalin was successfully expressed by bacteria with the expected molecular weight (17 kDa). These analyses also showed that recombinant frutalin was mainly produced as insoluble protein. Recombinant frutalin produced by bacteria revealed agglutination properties and carbohydrate-binding specificity similar to the native breadfruit lectin.

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“…Results are representative of two similar experiments. duction [22,21] and IL-2R activation [28], it is conceivable that having once activated TCR, frutalin could trigger the PI3K/Akt pathway which might modulate IL-2 and IL-2R gene transcription and also IL-2 responses through IL-2R.…”

Section: Discussionmentioning

confidence: 99%

“…More recently, we have demonstrated that interaction of frutalin with human neutrophils induced chemotaxis and triggered the oxidative burst. These effects were accompanied by profound alterations in the dynamics of the actin cytoskeleton dynamic and activation of the PTK and PI3K pathways [21].…”

Section: Introductionmentioning

confidence: 99%

Involvement of phosphatidylinositol-3 kinase–Akt and nuclear factor kappa-B pathways in the effect of frutalin on human lymphocyte

Brando-Lima¹,

Saldanha-Gama²,

Pereira³

et al. 2006

International Immunopharmacology

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Frutalin, a galactose-binding lectin, induces chemotaxis and rearrangement of actin cytoskeleton in human neutrophils: Involvement of tyrosine kinase and phosphoinositide 3-kinase

Cited by 23 publications

References 34 publications

Crystallization and preliminary X-ray diffraction studies of frutalin, an α-D-galactose-specific lectin fromArtocarpus incisaseeds

Crystallization and preliminary X-ray diffraction studies of frutalin, an α-D-galactose-specific lectin fromArtocarpus incisaseeds

cDNA Cloning and Functional Expression of the α-d-Galactose-Binding Lectin Frutalin in Escherichia coli

Involvement of phosphatidylinositol-3 kinase–Akt and nuclear factor kappa-B pathways in the effect of frutalin on human lymphocyte

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