Laboratory of Biological Chemistry
Laboratory of Biological Chemistry
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.
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.
Kamada R.,Laboratory of Biological Chemistry |
Tano F.,Laboratory of Biological Chemistry |
Kudoh F.,Laboratory of Biological Chemistry |
Kimura N.,Laboratory of Biological Chemistry |
And 5 more authors.
PLoS ONE | Year: 2016
Nuclear and cytoplasmic morphological changes provide important information about cell differentiation processes, cell functions, and signal responses. There is a strong desire to develop a rapid and simple method for visualizing cytoplasmic and nuclear morphology. Here, we developed a novel and rapid method for probing cellular morphological changes of live cell differentiation process by a fluorescent probe, TAP-4PH, a 1,3a,6a-triazapentalene derivative. TAP-4PH showed high fluorescence in cytoplasmic area, and visualized cytoplasmic and nuclear morphological changes of live cells during differentiation. We demonstrated that TAP-4PH visualized dendritic axon and spine formation in neuronal differentiation, and nuclear structural changes during neutrophilic differentiation. We also showed that the utility of TAP-4PH for visualization of cytoplasmic and nuclear morphologies of various type of live cells. Our visualizing method has no toxicity and no influence on the cellular differentiation and function. The cell morphology can be rapidly observed after addition of TAP-4PH and can continue to be observed in the presence of TAP-4PH in cell culture medium. Moreover, TAP-4PH can be easily removed after observation by washing for subsequent biological assay. Taken together, these results demonstrate that our visualization method is a powerful tool to probe differentiation processes before subsequent biological assay in live cells. © 2016 Kamada et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
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.
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.
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.
PubMed | Laboratory of Biological Chemistry
Type: Journal Article | Journal: Neurochemistry international | Year: 2010
The effects of the 1-methyl-4-phenylpyridinium ion (MPP(+)) and some structurally related compounds on mitochondrial respiration and lactate production in mouse brain synaptosomes were studied with and without tetraphenylboron (TPB(?)), an activator of membrane transport of lipophilic cations. Without TPB(?), both MPP(+) and 4-phenylpyridine (4-PP), at concentrations of 1 mM, weakly inhibited synaptosomal respiration, but paraquat and 4-phenyl-1,2,3,6-tetrahydropyridine (PTP) did not. In the presence of 10 ?M TPB(?), MPP(+), at lower concentrations, significantly inhibited respiration and increased lactate production, but these two effects with 4-PP were not as great as those with MPP(+). Regardless of TPB(?), paraquat did not affect respiration or lactate production, but PTP, with TPB(?), somewhat accelerated both systems. In these experiments, except PTP, the degree of increase in lactate production caused was in close parallel with that of the inhibition of synaptosomal respiration. The present results conclusively indicate that, without TPB(?), MPP(+) scarcely permeates synaptosomal membranes of mouse whole brain. The present results confirm previous findings that nigrostriatal dopamine neurons, which selectively take up MPP(+) by the DA transport system, may be more selectively damaged by concentrated MPP(+) than other neurons that essentially lack a transport system with poor permeability for MPP(+) through their neuronal membranes.