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1.
Food Funct ; 7(2): 953-63, 2016 Feb.
Article in English | MEDLINE | ID: mdl-26738438

ABSTRACT

OBJECTIVE: epicardial adipose tissue (EAT) from patients with coronary artery disease (CAD) contains higher levels of inflammatory proteins and lower adiponectin levels than subcutaneous adipose tissue (SAT), enhancing the progression of atherosclerosis. Since products from sea cucumber have anti-inflammatory properties, we investigated its effect on EAT, SAT and endothelial cells. METHODS: stromal cells or explants from EAT and SAT were obtained from patients with cardiovascular disease. Extracts were obtained after hydrolysis by food-grade enzymes at different times. Proteins were identified by LC-MALDI mass spectrometry. Adipogenesis and adiponectin induction were determined on stromal cells in the presence/absence of extracts. The bioavailability of the extracts was tested on a Caco-2 cell culture model in vitro. The bioavailable fraction was probed on endothelial cells and EAT or SAT explants. Vascular cell adhesion protein (VCAM-1), intercellular adhesion molecule (ICAM-1), IL-6 and adiponectin were determined by real time polymerase chain reaction (RT-PCR). RESULTS: our results showed that H. forskali and P. tremulus extracts contained compounds with anti-oxidant and anti-inflammatory properties. The bioavailable fraction of P. tremulus reduced VCAM-1 (p < 0.01) and IL-6 (p < 0.05) expression levels in endothelial cells while bioavailable compounds from H. forskali decreased ICAM-1 expression in SAT (p < 0.05). No effect was observed on EAT. CONCLUSION: these results suggest that sea cucumber extracts might be used for the prevention of endothelial cells and SAT inflammation.


Subject(s)
Anti-Inflammatory Agents/pharmacology , Endothelial Cells/drug effects , Pericardium/drug effects , Sea Cucumbers/chemistry , Subcutaneous Fat/drug effects , Adipogenesis/drug effects , Adiponectin/blood , Angiotensin-Converting Enzyme Inhibitors/pharmacology , Animals , Antioxidants/pharmacology , Caco-2 Cells , Cell Proliferation/drug effects , Cell Survival/drug effects , Coronary Artery Disease/drug therapy , Endothelial Cells/metabolism , Humans , Inflammation/drug therapy , Interleukin-6/metabolism , Pericardium/metabolism , Proteomics , Subcutaneous Fat/metabolism , Vascular Cell Adhesion Molecule-1/metabolism
2.
Biotechnol Lett ; 32(12): 1893-6, 2010 Dec.
Article in English | MEDLINE | ID: mdl-20703805

ABSTRACT

A new, thermostable superoxide dismutase (SOD) from Bacillus licheniformis M20, isolated from Bulgarian mineral springs, was purified 11-fold with 11% recovery of activity. From native PAGE and SDS-PAGE, the enzyme was composed of two subunits of 21.5 kDa each. The SOD was inhibited only by NaN(3), which suggested that this SOD is of the manganese superoxide dismutase type. The purified enzyme had maximum activity at pH 8 and 55°C. The half-life of the SOD was 10 min at 95°C.


Subject(s)
Bacillus/enzymology , Hot Springs/microbiology , Superoxide Dismutase/isolation & purification , Superoxide Dismutase/metabolism , Bacillus/isolation & purification , Bulgaria , Electrophoresis, Polyacrylamide Gel , Enzyme Inhibitors/metabolism , Enzyme Stability , Half-Life , Hot Temperature , Hydrogen-Ion Concentration , Molecular Weight , Protein Subunits/chemistry , Protein Subunits/isolation & purification , Sodium Azide/metabolism , Superoxide Dismutase/chemistry
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