Silvana Saker-Sampaio

Universidade Federal do Ceará, Ceará, Ceará, Brazil

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Publications (22)38.86 Total impact

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    ABSTRACT: Natural antioxidants found in marine macroalgae are bioactive compounds known to play an important role in the prevention of diseases associated with aging cells protecting them against the oxidative damage. The purpose of this study was to evaluate the antioxidant and cytotoxic activity of ethanolic extracts of two species of red seaweeds, Amansia multifida and Meristiella echinocarpa. In vitro antioxidant activity was determined by DPPH radical scavenging assay, ferric-reducing antioxidant power (FRAP) assay, ferrous ion chelating (FIC) assay, β-carotene bleaching (BCB) assay and total phenolic content (TPC) quantification. Cytotoxicity was evaluated with the brine shrimp Artemia sp. lethality test. The TPC values observed in the present study indicated that both species A. multifida and M. echinocarpa are rich in phenolic compounds, reaching values of 45.40 and 28.46 mg gallic acid equivalent (GAE) g-1 of ethanolic extract, respectively. DPPH radical scavenging and ferrous ion chelating showed values of 60% and 17%, respectively. Both seaweed extracts inhibited β-carotene oxidation by approximately 40%. None of the algal extracts were potentially cytotoxic. The results have showed that extracts of both species of marine red algae exhibit antioxidant potential and low toxicity. They are sources of natural antioxidant compounds.
    Anais da Academia Brasileira de Ciências 03/2014; 86(1):251-263. · 0.85 Impact Factor
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    ABSTRACT: A novel lectin, HGA-2, was isolated from the sea cucumber Holothuria grisea. The protein was isolated by a single chromatographic step using a column of Guar Gum as affinity. HGA-2 showed an apparent molecular mass of 17kDa and 34kDa under reducing and nonreducing conditions, respectively. The hemagglutinating activity was specific for rabbit erythrocytes, showing no activity for human blood A, B and O. Its hemagglutinating activity was inhibited by carbohydrates containing galactose, with higher affinity for GalNAc and glycoprotein porcine stomach mucin (PSM). HGA-2 was stable at pH 6-10, significantly declining at pH 5 and a temperature of 40°C, with its activity being abolished at 100°C. The HGA-2 protein was found to be Ca(2+)-dependent; it was highly toxic against Artemia nauplii and able to recognize and agglutinate cells of E.coli. Amino acid sequences of tryptic peptides of HGA-2 strongly suggest that HGA-2 is a member of the C-type lectin family.
    International journal of biological macromolecules 01/2014; · 2.37 Impact Factor
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    ABSTRACT: Based on their morphological and physiological features, red algae comprise a complex and variable group of multiple genera, including Hypnea. In particular, the genus Hypnea J.V. Lamouroux (Cystocloniaceae, Rhodophyta) consists of approximately 54 species, including Hypnea cervicornis and H. musciformis. Lectins were described for both species; however, the localization of these proteins is still unclear. Therefore, this work aimed to characterize the morphology and ultrastructure of Hypnea cervicornis and H. musciformis, as well as localize their lectins at the subcellular level. Samples were collected at Praia do Pacheco (Fortaleza-CE) and processed for light, scanning and transmission electron microscopy, in addition to immunocytochemistry. The studied species presented cortical cell layers, subcortical cells and medullary cells. Based on ultrastructural analysis, these species presented vacuolated cortical cells, with a dense cytoplasm containing chloroplasts. The cell wall consisted of concentric microfibrils embedded in an amorphous matrix. Immunochemistry analysis showed the expression of lectins in the cytoplasm and cell walls. While the structure of the studied algae was similar to the description of other species of the genera under different conditions, this is the first record of algae lectin localization.
    Journal of Microscopy and Ultrastructure. 01/2014;
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    ABSTRACT: This study evaluated the effect of derriobtusone A, a flavonoid isolated from Lonchocarpus obtusus, on two important pathogenic bacteria, Staphylococcus aureus and Escherichia coli, as well as its antioxidant activity and toxicity. Planktonic growth assays were performed, and the inhibition of biofilm formation was evaluated. In addition, antioxidant activity was assessed by DPPH radical scavenging assay, ferrous ion chelating assay, ferric-reducing antioxidant power assay, and β -carotene bleaching assay. Toxicity was evaluated by the brine shrimp lethality test. Results showed that derriobtusone A completely inhibited the planktonic growth of S. aureus at 250 and 500 μ g/mL; however, it did not have the same activity on E. coli. Derriobtusone A reduced the biomass and colony-forming unit (cfu) of S. aureus biofilm at concentrations of 250 and 500 μ g/mL. In various concentrations, it reduced the biofilm biomass of E. coli, and, in all concentrations, it weakly reduced the cfu. Derriobtusone A showed highly efficient antioxidant ability in scavenging DPPH radical and inhibiting β -carotene oxidation. The compound showed no lethality to Artemia sp. nauplii. In conclusion, derriobtusone A may be an effective molecule against S. aureus and its biofilm, as well as a potential antioxidant compound with no toxicity.
    BioMed Research International 01/2014; 2014:248656. · 2.88 Impact Factor
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    ABSTRACT: Two new lectins named Halilectin 1 (H-1) and Halilectin 2 (H-2) were isolated from the marine sponge Haliclona caerulea using a combination of affinity chromatography on stroma fixed onto Sephadex G-25 and cation and anion exchange chromatography. H-1 is a monomeric protein with a molecular mass of 40 kDa estimated using sodium dodecyl sulfate polyacrylamide gel electrophoresis and 15 kDa estimated using a TSK gel. Conversely, H-2 is a homodimeric protein with 15 kDa monomers linked via weak interactions. H-1 more effectively agglutinates trypsinized rabbit erythrocytes, whereas H-2 more effectively agglutinates native rabbit erythrocytes. The hemagglutinating activity of H-1 could be not inhibited by any tested sugars, but H-2 was inhibited by orosomucoid and porcine stomach mucin. Neither lectin was dependent on divalent ions. H-1 was stable at basic pH range and temperatures up to 50 °C, whereas H-2 was stable at acid pH range and temperatures up to 80 °C. The H. caerulea lectins exhibited dose-dependent toxicity against Artemia nauplii. Additionally, 76% of the primary structure of H-2 was determined using tandem mass spectrometry to contain a unique amino acid sequence with no similarity to any members of the animal lectin family. Copyright © 2012 John Wiley & Sons, Ltd.
    Journal of Molecular Recognition 01/2013; 26(1):51-8. · 3.01 Impact Factor
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    ABSTRACT: Lectins are sugar-binding proteins widely distributed in nature with many biological functions. Although many lectins have a remarkable biotechnological potential, some of them can be cytotoxic. Thus, the aim of this study was to assess the toxicity of five lectins, purified from seeds of different species of Canavalia genus. In order to determine the toxicity, assays with Artemia nauplii were performed. In addition, a fluorescence assay was carried out to evaluate the binding of lectins to Artemia nauplii. In order to verify the relationship between the structure of lectins and their cytotoxic effect, structural analysis was carried out to evaluate the volume of the carbohydrate recognition domain (CRD) of each lectin. The results showed that all lectins exhibited different toxicities and bound to a similar area in the digestive tract of Artemia nauplii. Concerning the structural analysis, differences in spatial arrangement and volume of CRD may explain the variation of the toxicity exhibited by each lectin. To this date, this is the first study that establishes a link between toxicity and structure of CRD from Diocleinae lectins.
    BioMed research international. 01/2013; 2013:154542.
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    ABSTRACT: Lectins are a structurally heterogeneous group of proteins that have specific binding sites for carbohydrates and glycoconjugates. Because of their biotechnological potential, lectins are widely used in biomedical research. The present study aimed to evaluate the healing potential of the lectin isolated from the marine red alga Bryothamnion seaforthii (BSL). The lectin was purified using ion exchange chromatography with DEAE cellulose and characterized using tandem mass spectrometry. For healing tests, skin wounds were induced in the dorsal thoracic region of mice. These animals were randomly divided into three groups and subjected to topical treatment for 12 days with BSL, bovine serum albumin and 150 mM NaCl. To evaluate the potential of each treatment, the animals were anesthetized and sacrificed on days 2, 7 and 12, respectively. The parameters evaluated included the wound area, the proportion of wound closure and the histological diagnosis. The wound closure was more effective with BSL (Postoperative Day 7 and 12) than controls. The luminal epithelium was completely restructured; the presence of collagen in the dermis and the strongly active presence of young skin annexes demonstrate the potential of treatment with BSL compared with controls. Our findings suggest that BSL has pro-healing properties and can be a potential medical process in the treatment of acute wounds.
    Marine Drugs 09/2012; 10(9):1936-54. · 3.98 Impact Factor
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    ABSTRACT: Marine algae are a promising source of beneficial compounds for human use. Among these, pro-vitamin A carotenoids and vitamins B, C, and E stand out. The objective of this study was to investigate seasonal variation of α-tocopherol levels in 5 species of green marine algae of the Caulerpa genus. This research was carried out with both fresh and dry specimens; and, in addition, differences arising as a result of the drying process were examined. Analyses were carried out by high-performance liquid chromatography (HPLC) using an isocratic system and a reversed-phase C-18 column. The distribution of α-tocopherol throughout the year in Caulerpa genus was variable. All samples of both fresh and dried algae contained α-tocopherol, except for the dried C. racemosa from March 2006. The drying process was responsible for losses of α-tocopherol ranging from 21% to 93%.
    Journal of Food Science 06/2011; 76(5):C775-81. · 1.78 Impact Factor
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    ABSTRACT: Many amines are commonly found in food of both animal and vegetable origin, however only a small number is of interest since they produce diverse reactions when ingested and absorbed by humans. Among them, histamine and tyramine can cause intoxication symptoms. Marine algae are consumed widely by the eastern civilizations, and in the West, their consumption is expanding. Brazil does not have this tradition, but the diversity of species found throughout the Brazilian coast line make marine algae potentially useful for human ingestion. For such, it is necessary to perform chemical and biochemical studies. In this study, thirteen species of marine macroalgae were collected from Pacheco beach, on the Atlantic coast of Ceará State, Brazil. Preliminarily, they were analysed for histamine and tyramine using high performance liquid chromatography. These amines were identified by comparing the retention time of standard solutions of histamine dihydrochloride and tyramine hydrochloride with those of the alga extracts. Histamine and/or tyramine have not been found in quantities high enough to cause pharmacological actions in any of the thirteen species of marine macroalgae studied.
    Revista Ciencia Agronomica 06/2011; 42(2):349-353.
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    ABSTRACT: Many amines are commonly found in food of both animal and vegetable origin, however only a small number is of interest since they produce diverse reactions when ingested and absorbed by humans. Among them, histamine and tyramine can cause intoxication symptoms. Marine algae are consumed widely by the eastern civilizations, and in the West, their consumption is expanding. Brazil does not have this tradition, but the diversity of species found throughout the Brazilian coast line make marine algae potentially useful for human ingestion. For such, it is necessary to perform chemical and biochemical studies. In this study, thirteen species of marine macroalgae were collected from Pacheco beach, on the Atlantic coast of Ceará State, Brazil. Preliminarily, they were analysed for histamine and tyramine using high performance liquid chromatography. These amines were identified by comparing the retention time of standard solutions of histamine dihydrochloride and tyramine hydrochloride with those of the alga extracts. Histamine and/or tyramine have not been found in quantities high enough to cause pharmacological actions in any of the thirteen species of marine macroalgae studied.
    Ciência agronômica 01/2011; 42(2):349-353. · 0.71 Impact Factor
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    ABSTRACT: The aim of this work was to evaluate the potential of 32 marine macro algae species, members of Chlorophyta, Rhodophyta and Phaeophyta, as sources of a-carotene, b-carotene and a-tocopherol. Both b-carotene and a-carotene were found in all species of green macroalgae analyzed. The maximum content of a-carotene was detected in algae belonging to Caulerpa genus and the minimum in Codium decorticatum. The amount of b-carotene found was minimum in Caulerpa mexicana and maximum in Ulva fasciata. Among the Rhodophyta species, eleven contain a-carotene, the maximum content was found in Botryocladia occidentalis. b-Carotene was found in all red macroalgae analyzed presenting the lowest and highest values in Gracilaria caudata and Bryothamnion triquetrum, respectively. Species of Phaeophyta contained b-carotene but no a-carotene. The lowest value for b-carotene was found in Dictyopteris delicatula and the highest in Padina gymnospora. In Chlorophyta, the amount of a-tocopherol was maximum in Codium decorticatum and minimum in Caulerpa prolifera. In Rhodophyta, twelve species contained a-tocopherol, the highest value was found in Enantiocladia duperreyi. a-Tocopherol was detected in all Phaeophyta species analyzed. The highest and lowest values were found in Lobophora varigata and Dictyota dichotoma, respectively.
    Ciência e Tecnologia de Alimentos 12/2008; 28(4):953-958. · 0.33 Impact Factor
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    ABSTRACT: The agglutinin from the red marine alga Hypnea cervicornis (HCA) was tested in models of nociception and inflammation. The role of carbohydrate-binding sites and the systemic toxicity were assessed. HCA (10(-1), 1, and 10 mg/kg) administered i.v. to mice inhibited writhes induced by acetic acid and, at 10 mg/kg, inhibited the second phase of the formalin test, but did not alter the response latency in the hot-plate test. HCA (1 mg/kg) administered i.v. to rats reduced carrageenan-induced paw edema at 1, 2, and 3 h after challenge, but not edema induced by dextran. The neutrophil migration induced by both N-formyl-methionyl-leucyl-phenylalanine (fMLP) and carrageenan was inhibited by HCA at 10(-1), 1, and 10 mg/kg. The combination of HCA (1 mg/kg) and its ligand mucin reversed the lectin inhibitory effect on carrageenan-induced neutrophil migration and acetic acid-induced writhes. The i.v. treatment of rats with HCA (1 mg/kg) for 7 days did not affect body mass; liver, kidney or heart wet weight; blood leukocyte counts; urea, creatinine or serum transaminase activity; or macroscopy of the organs examined. In short, H. cervicornis agglutinin showed important antinociceptive and anti-inflammatory activity via interaction with the lectin carbohydrate-binding site.
    Archiv für Experimentelle Pathologie und Pharmakologie 05/2008; 377(2):139-48. · 2.15 Impact Factor
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    ABSTRACT: The nutritional concern for marine macroalgae is due to their low caloric value and high content of vitamins, minerals and dietary fibers. Carotenoids consist of a group of natural pigments. Over 700 have been already identified and classified and approximately 50 show vitamin A activity; however, b-carotene exhibits the highest biological activity. Fourteen species of marine macroalgae, belonging to Chlorophyta, Rhodophyta e Phaeophyta, have been analyzed for their provitamin A carotenoid content. The alga extraction was carried out in MeOH-H2O (90:10, v/v), followed by saponification and partitioning in n-hexane. The column Spherisorb S5 ODS 2 (4.6 x 250 mm) was used with MeOH-THF (90:10, v/v), delivered at 2 mL min-1 and detection at 450 nm. Among the studied species, the highest contents of provitamin A carotenoids have been found in green marine macroalgae.
    Ciência agronômica 01/2008; 39(2):257-262. · 0.71 Impact Factor
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    Ciencia E Tecnologia De Alimentos - CIENCIA TECNOL ALIMENT. 01/2008; 28(4).
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    ABSTRACT: The initial colonization of the tooth by streptococci involves their attachment to adsorbed components of the acquired pellicle. Avoiding this adhesion may be successful in preventing caries at early stages. Salivary mucins are glycoproteins that when absorbed onto hydroxyapatite may provide binding sites for certain bacteria. Algal lectins may be especially interesting for oral antiadhesion trials because of their great stability and high specificity for mucins. This work aimed to evaluate the potential of two algal lectins to inhibit the adherence of five streptococci species to the acquired pellicle in vitro. The lectins used were extracted from Bryothamnion triquetrum (BTL) and Bryothamnion seaforthii (BSL). Fluorescence microscopy was applied to visualize the ability of fluorescein isothiocyanate-labelled lectins to attach to the pellicle and revealed a similar capability for both lectins. Streptococcal adherence assays were performed using saliva-coated microtitre plates. BSL inhibited more than 75% of Streptococcus sanguis, Streptococcus mitis, Streptococcus sobrinus and Streptococcus mutans adherence, achieving 92% to the latter. BTL only obtained statistically significant results on S. mitis and S. sobrinus, whose adherence was decreased by 32.5% and 54.4%, respectively. Algal lectins are able to inhibit streptococcal adherence. Our results support the proposed application of lectins in antiadhesion therapeutics.
    Journal of Applied Microbiology 11/2007; 103(4):1001-6. · 2.20 Impact Factor
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    ABSTRACT: The biochemical characterization of a new lectin (Hypnea cervicornis agglutinin or HCA) isolated from the Brazilian red alga H. cervicornis is reported. The haemagglutinating activity of the lectin was only inhibited by the glycoprotein porcine stomach mucin at a minimum inhibitory concentration of 19 microg x mL(-1). No haemagglutination inhibition was detected after the addition of simple sugars. The MALDI-TOF molecular masses of native and reduced and carbamidomethylated HCA were, respectively, 9196.6 Da and 9988.2 Da, indicating that the primary structure of the protein is crosslinked by 7 disulfide bonds. This unusual structural feature among lectins, along with its N-terminal sequence and amino-acid composition, clearly shows that HCA belongs to a protein family distinct from the isolectins Hypnin A1 and A2 isolated from the related Japanese alga Hypnea japonica. On the other hand, HCA displayed a high degree of similarity to the agglutinin from the Brazilian species Hypnea musciformis. Our data indicate the occurrence of structural diversity among lectins of closely related species living in distant ecosystems, i.e., the Pacific coast of Japan and the Atlantic coast of Brazil, and support the hypothesis that the lectin content (lectinome) might serve as a biomarker for taxonomical purposes.
    Biochemistry and Cell Biology 03/2006; 84(1):49-54. · 2.92 Impact Factor
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    ABSTRACT: HCA and HML represent lectins isolated from the red marine algae Hypnea cervicornis and Hypnea musciformis, respectively. Hemagglutination inhibition assays suggest that HML binds GalNAc/Gal substituted with a neutral sugar through 1-3, 1-4, or 1-2 linkages in O-linked mucin-type glycans, and Fuc(alpha1-6)GlcNAc of N-linked glycoproteins. The specificity of HCA includes the epitopes recognized by HML, although the glycoproteins inhibited distinctly HML and HCA. The agglutinating activity of HCA was inhibited by GalNAc, highlighting the different fine sugar epitope-recognizing specificity of each algal lectin. The primary structures of HCA (9193+/-3 Da) and HML (9357+/-1 Da) were determined by Edman degradation and tandem mass spectrometry of the N-terminally blocked fragments. Both lectins consist of a mixture of a 90-residue polypeptide containing seven intrachain disulfide bonds and two disulfide-bonded subunits generated by cleavage at the bond T50-E51 (HCA) and R50-E51 (HML). The amino acid sequences of HCA and HML display 55% sequence identity (80% similarity) between themselves, but do not show discernible sequence and cysteine spacing pattern similarities with any other known protein structure, indicating that HCA and HML belong to a novel lectin family. Alignment of the amino acid sequence of the two lectins revealed the existence of internal domain duplication, with residues 1-47 and 48-90 corresponding to the N- and C-terminal domains, respectively. The six conserved cysteines in each domain may form three intrachain cysteine linkages, and the unique cysteine residues of the N-terminal (Cys46) and the C-terminal (Cys71) domains may form an intersubunit disulfide bond.
    Protein Science 09/2005; 14(8):2167-76. · 2.74 Impact Factor
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    ABSTRACT: The red marine alga Ptilota plumosa has been shownto contain an anti-human blood group B lectin. We report here a new isolationprocedure by affinity chromatography on Sephadex G-200 and characterisation ofthe isolated lectin. The M r , determined by gelfiltration, was 52,500. SDS-PAGE revealed a single protein band withM r 17,440, indicating the native lectin was atrimer of subunits with the same Mr, as reported for the lectinsfromtwo other Ptilota species, P.filicinaand P. serrata. Analysis of amino acid composition showedslightly more basic than acidic amino acids. This was in contrast to theP. filicina and P. serrata lectinspreviously found to contain a higher proportion of acidic than basic aminoacids. Haemagglutination inhibition tests showed the P.plumosa lectin was inhibited by galactose, glucose and theirderivatives with p-nitrophenyl--D-galactoside moststrongly inhibitory. All glycoproteins tested failed to inhibit the lectin. Theamino acid composition, human blood group-B specificity and lack of inhibitionby glycoproteins indicate the lectin from P. plumosapossesses unique characteristics among marine algal lectins.
    Journal of Applied Phycology 11/2002; 14(6):489-495. · 2.33 Impact Factor
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    ABSTRACT: A lectin from the red marine alga Hypnea musciformis (HML) was purified by extraction with 20 mM PBS, precipitation with 70% saturated ammonium sulphate, ion-exchange DEAE-Cellulose chromatography and RP-HPLC. The 9.3 kDa polypeptide agglutinates erythrocytes from various sources and shows oligomerization tendencies under certain MALDI-TOF / MS conditions. Preliminary N-terminal sequencing and biological assays strongly suggest that the HML may belong to a new class of algae lectins.
    Protein and Peptide Letters 03/2002; 9(2):159-165. · 1.99 Impact Factor

Publication Stats

127 Citations
38.86 Total Impact Points

Institutions

  • 1998–2014
    • Universidade Federal do Ceará
      • • Departamento de Engenharia de Pesca
      • • Departamento de Bioquímica e Biologia Molecular
      • • Centro de Ciências Agrárias (CAA)
      Ceará, Ceará, Brazil
  • 2000
    • Instituto de Biomedicina
      Caracas, Distrito Federal, Venezuela