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da Silva Suéllen Pedrosa,da Costa Clarice Barbosa Lucena,de Freitas Anderson Felipe Soares,da Silva José Dayvid Ferreira,Costa Wêndeo Kennedy,da Silva Wênio Sandoval Filho Lima,Machado Janaina Carla B 한국독성학회 2023 Toxicological Research Vol.39 No.2
The present study aimed to evaluate saline extracts from the leaves (LE) and stem (SE) of Portulaca elatior in relation to their phytochemical composition and photoprotective and antioxidant effects, as well as to evaluate the toxicity of the leaf extract. The extracts were characterized for protein concentration and phenol and flavonoid contents, as well as for thin layer chromatography (TLC) and high-performance liquid chromatography (HPLC) profiles. Total antioxidant capacity and DPPH and ABTS+ scavenging activities were determined. In the photoprotective activity assay, the sun protection factor (SPF) was calculated. The toxicity evaluation of LE included in vitro hemolytic assay and in vivo oral and dermal acute toxicity assays in Swiss mice. LE showed the highest protein, phenol, and flavonoid (8.79 mg/mL, 323.46 mg GAE/g, and 101.96 QE/g, respectively). TLC revealed the presence of flavonoids, reducing sugars, terpenes, and steroids in both extracts. In HPLC profiles, LE contained flavonoids, while SE contained flavonoids and ellagic tannins. The antioxidant activity assays showed the lowest IC50 values (34.15–413.3 μg/mL) for LE, which presented relevant SPF (> 6) at 50 and 100 μg/mL. LE demonstrated low hemolytic capacity, and no signs of intoxication were observed in mice treated orally or topically at 1000 mg/kg. However, at 2000 mg/kg, an increase in the mean corpuscular volume of erythrocytes and a reduction in lymphocytes were observed; animals treated topically with 2000 mg/kg displayed scratching behavior during the first hour of observation and showed edema and erythema that regressed after six days. In conclusion, LE did not present acute oral or dermal toxicity in Swiss mice at a dose of 1000 mg/kg and showed slight toxicity in animals treated with 2000 mg/kg.
Nathalia Del Rio Lyra Graça,Anna Rebeca de Barros Lins Silva Palmeira,Luana Osório Fernandes,Marlus da Silva Pedrosa,Renata Pedrosa Guimarães,Saulo Cabral dos Santos,Anderson Stevens Leonidas Gomes,Cl 대한영상치의학회 2019 Imaging Science in Dentistry Vol.49 No.2
The available methods for veneer evaluation are limited to clinical and radiographic examinations, which may not allow the appropriate identification of failure. In this report, we demonstrate the use of optical coherence tomography (OCT) as a noninvasive diagnostic and follow-up method to evaluate gingival recovery and the adhesive interface in aesthetic oral rehabilitation involving periodontal plastic surgery and ceramic laminate veneers. OCT was efficient for evaluating both soft and hard tissues, as well as the quality of the adhesive interface. In conclusion, OCT was found to be a promising approach for the professional evaluation of aesthetic oral rehabilitation, as it was capable of generating images that enabled the analysis of gingival recovery and the adhesive interface.
Graca, Nathalia Del Rio Lyra,Palmeira, Anna Rebeca de Barros Lins Silva,Fernandes, Luana Osorio,da Silva Pedrosa, Marlus,Guimaraes, Renata Pedrosa,Santos, Saulo Cabral dos,Gomes, Anderson Stevens Leon Korean Academy of Oral and Maxillofacial Radiology 2019 Imaging Science in Dentistry Vol.49 No.2
The available methods for veneer evaluation are limited to clinical and radiographic examinations, which may not allow the appropriate identification of failure. In this report, we demonstrate the use of optical coherence tomography (OCT) as a noninvasive diagnostic and follow-up method to evaluate gingival recovery and the adhesive interface in aesthetic oral rehabilitation involving periodontal plastic surgery and ceramic laminate veneers. OCT was efficient for evaluating both soft and hard tissues, as well as the quality of the adhesive interface. In conclusion, OCT was found to be a promising approach for the professional evaluation of aesthetic oral rehabilitation, as it was capable of generating images that enabled the analysis of gingival recovery and the adhesive interface.
Pereira, Paula,Pedrosa, Sí,lvia S.,Wymant, Jennifer M.,Sayers, Edward,Correia, Alexandra,Vilanova, Manuel,Jones, Arwyn T.,Gama, Francisco M. American Chemical Society 2015 MOLECULAR PHARMACEUTICS Vol.12 No.6
<P>Glycol chitosan nanogels have been widely used in gene, drug, and contrast agent delivery in an effort to improve disease diagnosis and treatment. Herein, we evaluate the internalization mechanisms and intracellular fate of previously described glycol chitosan nanogels decorated with folate to target the folate receptor. Uptake of the folate-decorated nanogel was impaired by free folate, suggesting competitive inhibition and shared internalization mechanisms via the folate receptor. Nanogel uptake was shown to occur mainly through flotillin-1 and Cdc42-dependent endocytosis. This was determined by inhibition of uptake reduction observed upon siRNA depletion of these two proteins and the pathways that they regulate. The data also suggest the involvement of the actin cytoskeleton in nanogel uptake via macropinocytosis. After 7 h of incubation with HeLa cells, approximately half of the nanogel population was localized in endolysosomal compartments, whereas the remaining 50% of the material was in undefined regions of the cytoplasm. Glycol chitosan nanogels may thus have potential as drug delivery vectors for targeting different intracellular compartments.</P><P><B>Graphic Abstract</B> <IMG SRC='http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/mpohbp/2015/mpohbp.2015.12.issue-6/mp500785t/production/images/medium/mp-2014-00785t_0009.gif'></P><P><A href='http://pubs.acs.org/doi/suppl/10.1021/mp500785t'>ACS Electronic Supporting Info</A></P>
Binding of Lichen Phenolics to Purified Secreted Arginase from the Lichen Evernia prunastri
Legaz, Maria-Estrella,Vicente, Carlos,Pedrosa, Mercedes M. Korean Society for Biochemistry and Molecular Biol 2001 Journal of biochemistry and molecular biology Vol.34 No.3
Secreted arginase from Evernia prunastri thallus has been purified 616-fold from the incubation medium. Purified arginase was resolved as only one peak in a capillary electrophoresis with a pI value of 5.35. The protein contained high amounts of acidic amino acids, such as Asx and Glx, and a relatively high quantity of Ser and Gly. The molecular mass of native, purified arginase was estimated as about 26 kDa by SE-HPLC. Substrate saturated kinetic showed a typical Michaelis-Menten relationship with a K_m value of 3.3 mM L-arginine. Atranorin behaved as a mixed activator of the enzyme (apparent $K_m$ = 0.96 mM); whereas evernic and usnic acid were revealed as non competitive inhibitors (apparent $K_m$ values were 3.16 mM and 3.05 mM, respectively). Kinetics of atranorin binding indicated that saturation was reached from 0.18 ${\mu}mol$ of the total atranorin and the occurrence of multiple sites for the ligand. This agrees with a possible aggregation of several enzyme subunits during the interaction process. A value of binding sites of about 12 was obtained. The binding of evernic acid was saturated from 23 nmol of total phenol. The number of binding sites was about 5. The loss of the binding ability of evernic acid could be interpreted as a single negative cooperatively. Usnic acid behaves in a similar way to evernic acid, although the binding saturation occurs at $0.14\;{\mu}moles$ of the ligand. This binding appears to be unspecific, and has 28 usnic acid binding sites to the protein.
Binding of Lichen Phenolics to Purified Secreted Arginase from the Lichen Evernia prunastri
(Maria Estrella Legaz),(Carlos Vicente),(Mercedes M . Pedrosa) 생화학분자생물학회 2001 BMB Reports Vol.34 No.3
Secreted arginase from Evernia prunnstri thallus has been purified 616-fold from the incubation medium. Purified arginase was resolved as only one peak in a capillary electrophoresis with a pI value of 5.35. The protein contained high amounts of acidic amino acids, such as Asx and Glx, and a relatively high quantity of Ser and Gly. The molecular mass of native, purified arginase was estimated as about 26 kDa by SE-HPLC. Substrate saturated kinetic showed a typical Michaelis-Menten relationship with a K_m value of 3.3 mM L-arginine. Atranorin behaved as a mixed activator of the enzyme (apparent K_m = 0.96 mM); whereas evernic and usnic acid were revealed as non competitive inhibitors (apparent K_m values were 3.16 mM and 3.05 mM, respectively). Kinetics of atranorin binding indicated that saturation was reached from 0.18 μmol of the total atranorin and the occurrence of multiple sites for the ligand. This agrees with a possible aggregation of several enzyme subunits during the interaction process. A value of binding sites of about 12 was obtained. The binding of evernic acid was saturated from 23 nmol of total phenol. The number of binding sites was about 5. The loss of the binding ability of evernic acid could be interpreted as a single negative cooperatively. Usnic acid behaves in a similar way to evernic acid, although the binding saturation occurs at 0.14 μmoles of the ligand. This binding appears to be unspecific, and has 28 usnic acid binding sites to the protein.
Evaluation of Biological and Biochemical Quality of Whey Protein
Fabiano Kenji Haraguchi,Maria Lucia Pedrosa,Heberth de Paula,Rinaldo Cardoso dos Santos,Marcelo Eustaquio Silva 한국식품영양과학회 2010 Journal of medicinal food Vol.13 No.6
Nutritional and biochemical properties of noncommercial whey protein have been described since 1950. However, comparisons between commercial whey protein for human consumption and casein are rarely found. The aim of this study was to compare biological quality of a commercial whey protein with casein and its effect on biochemical parameters of rats. Thirty-two weanling Fisher rats were divided into three groups and given the following diets: casein group, standard diet (AOAC); whey protein group, modified AOAC diet with whey protein instead of casein; and casein:whey group, modified AOAC diet with 70%:30% casein:whey. A protein-free group was used for determination of endogenous nitrogen losses. Net protein ratio, protein efficiency ratio, and true digestibility were determined, and blood was collected for biochemical analysis. When compared with casein, whey protein showed significant differences for all biological parameters evaluated, as well as for albumin, total protein, total cholesterol, and glucose concentrations. Replacing 30% of casein with whey protein did not affect these parameters. A positive relation among whey protein, high-density lipoprotein-cholesterol, and paraoxonase activity was found. Hepatic or renal dysfunctions were not observed. In conclusion, in comparison with casein, commercial whey protein had higher values of biological parameters, and biochemical evaluation revealed it improved glycemic homeostasis, lipid status, and paraoxonase activity in rats.
( Jorge Frias ),( Duarte Toubarro ),( Alexandra Fraga ),( Claudia Botelho ),( Jose Teixeira ),( Jorge Pedrosa ),( Nelson Simoes ) 한국미생물생명공학회(구 한국산업미생물학회) 2021 Journal of microbiology and biotechnology Vol.31 No.2
Fibrinolytic enzymes with a direct mechanism of action and safer properties are currently requested for thrombolytic therapy. This paper reports on a new enzyme capable of degrading blood clots directly without impairing blood coagulation. This enzyme is also non-cytotoxic and constitutes an alternative to other thrombolytic enzymes known to cause undesired side effects. Twenty-four Bacillus isolates were screened for production of fibrinolytic enzymes using a fibrin agar plate. Based on produced activity, isolate S127e was selected and identified as B. subtilis using the 16S rDNA gene sequence. This strain is of biotechnological interest for producing high fibrinolytic yield and consequently has potential in the industrial field. The purified fibrinolytic enzyme has a molecular mass of 27.3 kDa, a predicted pI of 6.6, and a maximal affinity for Ala-Ala-Pro-Phe. This enzyme was almost completely inhibited by chymostatin with optimal activity at 48℃ and pH 7. Specific subtilisin features were found in the gene sequence, indicating that this enzyme belongs to the BPN group of the S8 subtilisin family and was assigned as AprE127. This subtilisin increased thromboplastin time by 3.7% (37.6 to 39 s) and prothrombin time by 3.2% (12.6 to 13 s), both within normal ranges. In a whole blood euglobulin assay, this enzyme did not impair coagulation but reduced lysis time significantly. Moreover, in an in vitro assay, AprE127 completely dissolved a thrombus of about 1 cc within 50 min and, in vivo, reduced a thrombus prompted in a rat tail by 11.4% in 24 h compared to non-treated animals.