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1.
Scand J Med Sci Sports ; 24 Suppl 1: 57-65, 2014 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-24944132

RESUMO

We evaluated the effects of recreational football training combined with calorie-restricted diet (football + diet) vs calorie-restricted diet alone (diet) on aerobic fitness, lipid profile, and insulin resistance indicators in type 2 diabetes (T2D) patients. Forty-four T2D patients aged 48-68 years (27 females, 17 males) were randomly allocated to the football + diet group (FDG; n = 22) or to the diet group (DG; n = 22), of whom 19 FDG and 15 DG subjects completed the study. The football training was performed for 3 × 40 min/week for 12 weeks. Dual-energy X-ray absorptiometry scanning, treadmill testing, and fasting blood samplings were performed pre and post-intervention. After 12 weeks, maximal oxygen uptake (VO2max ) was elevated (P < 0.05) by 10 ± 4% in FDG but not in DG (-3 ± 4%, P < 0.05). After 12 weeks, reductions in blood triglycerides (0.4 ± 0.1 mmol/L), total cholesterol (0.6 ± 0.2 mmol/L), low-density lipoprotein, and very low-density lipoprotein levels were observed only in FDG. Fat mass decreased (P < 0.05) by 3.4 ± 0.4 kg in FDG and 3.7 ± 0.4 kg in DG. The lower (P < 0.05) glucagon and homeostatic model assessment of insulin resistance indicated an improvement in insulin sensitivity in FDG. In conclusion, football combined with restricted diet was effective in enhancing VO2max , reducing total cholesterol and triglycerides, and increasing insulin sensitivity, potentially providing better tools for the prevention of T2D complications than diet alone.


Assuntos
Colesterol/sangue , Diabetes Mellitus Tipo 2/terapia , Terapia por Exercício/métodos , Resistência à Insulina , Aptidão Física , Futebol/fisiologia , Triglicerídeos/sangue , Idoso , Biomarcadores/sangue , Glicemia/metabolismo , Brasil , Restrição Calórica , Terapia Combinada , Diabetes Mellitus Tipo 2/sangue , Diabetes Mellitus Tipo 2/fisiopatologia , Feminino , Frequência Cardíaca , Humanos , Masculino , Pessoa de Meia-Idade , Consumo de Oxigênio , Resultado do Tratamento
2.
Transplant Proc ; 49(4): 813-816, 2017 May.
Artigo em Inglês | MEDLINE | ID: mdl-28457401

RESUMO

BACKGROUND: Aldosterone is involved in the process of renal allograft fibrosis, clinically manifest by proteinuria and allograft dysfunction, with increased risk for cardiovascular death. The treatment with aldosterone antagonists appears to be effective in controlling proteinuria, with a protective effect on progression of renal fibrosis. METHODS: This retrospective, cohort study included kidney transplant recipients from January 1993 to June 2015. Inclusion criteria were persistent proteinuria >0.5 g/d, longer than 6 months, and spironolactone therapy. RESULTS: One hundred forty transplant recipients fulfilled the inclusion criteria and were divided into 3 groups, according to proteinuria levels at the beginning of spironolactone therapy: low (<1 g/24 h), intermediate (1-3 g/24 h), and nephrotic (>3 g/24 h). Groups were comparable in demographic data, with a higher incidence of living related donors in the nephrotic group. In patients with proteinuria ≥1 g/d, we observed a significant reduction in proteinuria after 6 months of therapy that persisted over time. Blood pressure and glomerular filtration rate persisted stable over time. Adverse events were not severe to withdrawal therapy. CONCLUSIONS: Spironolactone can be a safe alternative to control post-transplant proteinuria, especially in patients with mild to moderate allograft dysfunction with proteinuria ≥1 g/day.


Assuntos
Diuréticos/uso terapêutico , Transplante de Rim/efeitos adversos , Proteinúria/tratamento farmacológico , Espironolactona/uso terapêutico , Adulto , Feminino , Humanos , Masculino , Pessoa de Meia-Idade , Proteinúria/etiologia , Estudos Retrospectivos
3.
Biochim Biophys Acta ; 1384(2): 204-8, 1998 May 19.
Artigo em Inglês | MEDLINE | ID: mdl-9659381

RESUMO

The complete amino acid sequence of myotoxin II (godMT-II), a myotoxic phospholipase A2 (PLA2) homologue from the venom of the Central American crotaline snake Cerrophidion (Bothrops) godmani, was determined by direct protein sequencing methods. GodMT-II is a class II PLA2 showing a Lys instead of Asp at position 49. An additional substitution in the calcium binding loop region (Asn instead of Tyr at position 28) suggests the lack of enzymatic activity observed in this toxin is due to loss of its ability to bind the co-factor Ca2+, since the residues involved in forming the catalytic network of PLA2s (His-48, Tyr-52 and Asp-99) are conserved in godMT-II. This myotoxin shows highest sequence homology with other Lys-49 PLA2 s from Bothrops, Agkistrodon and Trimeresurus species, suggesting that they constitute a conserved family of proteins, yet in contrast presents lower homology with Bothrops asper myotoxin III, a catalytically-active PLA2. The C-terminal region of godMT-II, which is rich in cationic and hydrophobic residues, shares high sequence homology to the corresponding region in the myotoxin II from B. asper, which has been proposed to play an important role in the Ca(2+)-independent membrane damaging activity.


Assuntos
Bothrops , Venenos de Crotalídeos/enzimologia , Neurotoxinas/química , Fosfolipases A/química , Sequência de Aminoácidos , Animais , Fosfolipases A2 do Grupo II , Dados de Sequência Molecular , Fosfolipases A2 , Proteínas de Répteis , Alinhamento de Sequência , Homologia de Sequência de Aminoácidos
4.
An Acad Bras Cienc ; 61(4): 405-12, 1989 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-2486896

RESUMO

Hemolytic and phospholipase D activities were found in the saline extract of Enterolobium contortisiliquum seeds. The hemolytic activity is due to a protein which was named enterolobin. This protein was highly purified by extraction with 0.15 M NaCl, precipitation with ammonium sulphate from 0 to 33% of saturation, batch separation by adsorption on DEAE-cellulose and gel filtration chromatography on Sephadex G-100 or G-150. In the batch separation the fraction showing hemolytic activity was not adsorbed by the resin while the fraction with phospholipase activity was. In this manner it was shown that those two activities were due to different proteins. Mouse erythrocytes were less susceptible to hemolysis by enterolobin than human and rabbit erythrocytes. The hemolytic activity was rapidly lost at or above 55 degrees C and in extreme acid (1.6) and basic (10.8) pHs. The following characteristics of purified enterolobin were determined: molecular weights of 55.000 D (by SDS-PAGE), 59.800 D (by gel filtration) and 51.300 D (by HPLC); pI = 7.0; Gln as the N-terminal amino acid residue; high levels of Asp(Asx), Glu(Glx), Ser and Thr residues and low levels of Cys and Met residues. Similarities were noticed between enterolobin and crotin, a hemolytic protein of Croton tiglium seeds.


Assuntos
Hemólise/efeitos dos fármacos , Proteínas de Plantas/isolamento & purificação , Sementes , Aminoácidos/análise , Animais , Brasil , Cromatografia em Gel , Cromatografia Líquida de Alta Pressão , Eletroforese em Gel de Poliacrilamida , Humanos , Focalização Isoelétrica , Camundongos , Peso Molecular , Proteínas de Plantas/análise , Proteínas de Plantas/química , Proteínas de Plantas/farmacologia , Coelhos , Árvores
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