Yadav H.,U.S. National Institutes of Health |
Lee J.-H.,U.S. National Institutes of Health |
Lloyd J.,Laboratory of Biological Chemistry |
Walter P.,U.S. National Institutes of Health |
Rane S.G.,U.S. National Institutes of Health
Journal of Biological Chemistry | Year: 2013
Background: The prescription of probiotics as obesity and diabetes therapy is limited because of insufficient efficacy data and lack of understanding of their mechanism of action. Results: The probiotic VSL#3 prevents obesity and diabetes in mice via induction of butyrate and GLP-1. Conclusion: Probiotics modulate the gut flora to elicit beneficial metabolic effects. Significance: Administration of probiotics represents a viable treatment option for obesity and diabetes. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
Kirmizis D.,Aristotle University of Thessaloniki |
Kirmizis D.,Alpha Nephrodynamic Dialysis Unit |
Chatzidimitriou D.,Laboratory of Microbiology |
Chatzopoulou F.,Laboratory of Microbiology |
And 3 more authors.
Clinical Nephrology | Year: 2013
A well-functioning vascular access is the cornerstone for an optimal hemodialysis treatment and an issue of major importance for the outcome of patients on chronic hemodialysis. Over the last few years reports supporting the aspect that mechanisms involved in vascular access malfunction are genetically controlled have been published. Triggered by two cases reported herein, we present a comprehensive review of the literature on an evolving field of particular significance to patients on hemodialysis. © 2013 Dustri-Verlag Dr. K. Feistle.
Tsuruta H.,Kobe University |
Mikami B.,Laboratory of Applied Structural Biology |
Higashi T.,Laboratory of Biological Chemistry |
Aizono Y.,Laboratory of Biological Chemistry
Bioscience, Biotechnology and Biochemistry | Year: 2010
The crystal structure of a cold-active alkaline phosphatase from a psychrophile, Shewanella sp. (SCAP), was solved at 2.2 A. A refined model showed a homo-dimer with six metal-ligand sites. The arrangement of the catalytic residues resembled those of alkaline phosphatases (APs), suggesting that the reaction mechanism of SCAP was fundamentally identical to those of other APs. SCAP had two distinct structural features: (i) a loop with Argl22 that bound to the phosphate moiety of the substrate suffered no constraints from the linkage to other secondary structures, and (ii) Mg3-ligand FBslO9 was considered to undergo repulsive effect with neighboring Trp228. The local flexibility led by these features might be an important factor in the high catalytic efficiency of SCAP at low temperatures.
Kitsati N.,Laboratory of Biological Chemistry |
Fokas D.,Laboratory of Medicinal Chemistry |
Ouzouni M.-D.,Laboratory of Medicinal Chemistry |
Mantzaris M.D.,Laboratory of Biological Chemistry |
And 2 more authors.
Journal of Agricultural and Food Chemistry | Year: 2012
Naturally occurring cinnamic acid derivatives are ubiquitously distributed in the plant kingdom, and it has been proposed that their consumption contributes to the maintenance of human health. However, the molecular mechanisms underlying their health keeping effects remain unknown. In the present investigation, we evaluated the capacity of several cinnamic acid derivatives (trans-cinnamic, p-coumaric, caffeic and ferulic acids, as well as caffeic acid-methyl and -propyl esters) to protect cells from oxidative stress-induced DNA damage. It was observed that effective protection was based on the ability of each compound to (i) reach the intracellular space and (ii) chelate intracellular "labile" iron. These results support the notion that numerous lipophilic iron chelating compounds, present abundantly in plant-derived diet components, may protect cells in conditions of oxidative stress and in this way be important contributors toward maintenance of human health. © 2012 American Chemical Society.
Ujita M.,Laboratory of Biological Chemistry |
Inoue R.,Laboratory of Biological Chemistry |
Yusuke M.,Laboratory of Biological Chemistry |
Katsuno Y.,Laboratory of Biological Chemistry |
Okumura H.,Laboratory of Biological Chemistry
Bioscience, Biotechnology and Biochemistry | Year: 2011
The cytoplasmic domain of the medicinal mushroom Cordyceps militaris β-1,3-glucan synthase catalytic subunit Fks1 was expressed as a fusion protein with an Nterminal hexahistidine tag and glutathione S-transferase in an Escherichia coli cell-free translation system, and was assayed for binding specificity. The recombinant cytoplasmic domain bound specifically to UDP-agarose and lichenan (β-glucan), but not to ADP-agarose, GDPagarose, or other carbohydrates.