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1.
Arch Pharm Res ; 38(4): 494-504, 2015 Apr.
Article in English | MEDLINE | ID: mdl-25173360

ABSTRACT

We have recently developed betalain-rich beetroot (Beta vulgaris) dye (betalain) to be used in food products. Betalain (30-300 mg/kg) intraperitoneal (i.p.) treatment diminished carrageenan (100 µg/paw)-induced paw edema and neutrophil migration to the paw skin tissue. Betalain (100 mg/kg) treatment by subcutaneous or per oral routes also inhibited the carrageenan-induced paw edema. Importantly, the post-treatment with betalain (100 mg/kg, i.p.) significantly inhibited carrageenan- and complete Freund's adjuvant (10 µl/paw)-induced paw edema. Betalain (100 mg/kg) also reduced carrageenan (500 µg/cavity)-induced recruitment of total leukocytes, including mononuclear cells and neutrophils, as well as increasing vascular permeability in the peritoneal cavity. Furthermore, betalain significantly reduced carrageenan-induced superoxide anion, tumor necrosis factor-alpha (TNF-α) and interleukin (IL)-1ß levels in the peritoneal fluid, as well as augmenting IL-10 levels. Therefore, this compound presents prominent anti-inflammatory effect on carrageenan-induced paw edema and peritonitis by reducing the production of superoxide anion and the cytokines TNF-α and IL-1ß, in addition to increasing IL-10 levels. These results suggest that betalain shows therapeutic potential that could be utilized in the treatment of inflammation-associated diseases.


Subject(s)
Anti-Inflammatory Agents/therapeutic use , Betalains/therapeutic use , Cytokines/antagonists & inhibitors , Edema/drug therapy , Leukocytes/drug effects , Superoxides/antagonists & inhibitors , Animals , Anti-Inflammatory Agents/pharmacology , Beta vulgaris , Betalains/pharmacology , Cytokines/biosynthesis , Edema/pathology , Leukocytes/metabolism , Male , Mice , Superoxides/metabolism , Treatment Outcome
2.
Arch Biochem Biophys ; 526(1): 22-8, 2012 Oct 01.
Article in English | MEDLINE | ID: mdl-22772065

ABSTRACT

The nucleoid-associated protein H-NS is a major component of the bacterial nucleoid involved in DNA compaction and transcription regulation. The NMR solution structure of the Xylella fastidiosa H-NS C-terminal domain (residues 56-134) is presented here and consists of two beta-strands and two alpha helices, with one loop connecting the two beta-strands and a second loop connecting the second beta strand and the first helix. The amide (1)H and (15)N chemical shift signals for a sample of XfH-NS(56-134) were monitored in the course of a titration series with a 14-bp DNA duplex. Most of the residues involved in contacts to DNA are located around the first and second loops and in the first helix at a positively charged side of the protein surface. The overall structure of the Xylella H-NS C-terminal domain differ significantly from Escherichia coli and Salmonella enterica H-NS proteins, even though the DNA binding motif in loop 2 adopt similar conformation, as well as ß-strand 2 and loop 1. Interestingly, we have also found that the DNA binding site is expanded to include helix 1, which is not seen in the other structures.


Subject(s)
Bacterial Proteins/chemistry , Bacterial Proteins/metabolism , DNA-Binding Proteins/chemistry , DNA-Binding Proteins/metabolism , DNA/metabolism , Xylella , Amino Acid Sequence , DNA/genetics , GC Rich Sequence , Models, Molecular , Molecular Sequence Data , Peptide Fragments/chemistry , Peptide Fragments/metabolism , Protein Binding , Protein Structure, Tertiary , Sequence Alignment , Solutions
3.
Arch Biochem Biophys ; 477(1): 131-8, 2008 Sep 01.
Article in English | MEDLINE | ID: mdl-18593566

ABSTRACT

Human EFHC1 is a member of the EF-hand superfamily of Ca(2+)-binding proteins with three DM10 domains of unclear function. Point mutations in the EFHC1 gene are related to juvenile myoclonic epilepsy, a fairly common idiopathic generalized epilepsy. Here, we report the first structural and thermodynamic analyses of the EFHC1C-terminus (residues 403-640; named EFHC1C), comprising the last DM10 domain and the EF-hand motif. Circular dichroism spectroscopy revealed that the secondary structure of EFHC1C is composed by 34% of alpha-helices and 17% of beta-strands. Size exclusion chromatography and mass spectrometry showed that under oxidizing condition EFHC1C dimerizes through the formation of disulfide bond. Tandem mass spectrometry (MS/MS) analysis of peptides generated by trypsin digestion suggests that the Cys575 is involved in intermolecular S-S bond. In addition, DTNB assay showed that each reduced EFHC1C molecule has one accessible free thiol. Isothermal titration calorimetry (ITC) showed that while the interaction between Ca(2+) and EFHC1C is enthalpically driven (DeltaH=-58.6 to -67 kJ/mol and TDeltaS=-22.5 to -31 kJ/mol) the interaction between Mg(2+) and EFHC1C involves an entropic gain, and is approximately 5 times less enthalpically favorable (DeltaH=-11.7 to -14 kJ/mol and TDeltaS=21.9 to 19 kJ/mol) than for Ca(2+) binding. It was also found that under reducing condition Ca(2+) or Mg(2+) ions bind to EFHC1C in a 1/1 molar ratio, while under oxidizing condition this ratio is reduced, showing that EFHC1C dimerization blocks Ca(2+) and Mg(2+) binding.


Subject(s)
Calcium-Binding Proteins/metabolism , Calcium/metabolism , Magnesium/metabolism , Myoclonic Epilepsy, Juvenile/metabolism , Amino Acid Sequence , Base Sequence , Binding Sites , Blotting, Western , Calcium-Binding Proteins/chemistry , Calcium-Binding Proteins/genetics , Chromatography, Gel , DNA Primers , Dimerization , Humans , Mass Spectrometry , Molecular Sequence Data , Myoclonic Epilepsy, Juvenile/genetics , Protein Binding , Protein Structure, Secondary
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