sinapaldehyde and coniferaldehyde

sinapaldehyde has been researched along with coniferaldehyde* in 4 studies

Other Studies

4 other study(ies) available for sinapaldehyde and coniferaldehyde

ArticleYear
Whiskey congeners suppress LPS/IFNγ-induced NO production in murine macrophage RAW 264 cells by inducing heme oxygenase-1 expression.
    Journal of agricultural and food chemistry, 2012, Dec-26, Volume: 60, Issue:51

    Whiskey includes many nonvolatile substances (whiskey congeners; Whc) that seep from the oak cask during the maturation process. To date, many functions of Whc have reported, such as antiallergy and antimelanogenesis. This study examined the effect of Whc on LPS/IFNγ-induced nitric oxide (NO) production in murine macrophage RAW 264 cells. Whc suppressed LPS/IFNγ-induced NO production in a concentration-dependent manner. To determine the active compounds in Whc, the effect of 10 major compounds isolated from Whc on LPS/IFNγ-induced NO production was examined. Coniferylaldehyde (CA) and sinapylaldehyde (SiA) strongly suppressed LPS/IFNγ-induced NO production. Pretreatment with Whc, CA, and SiA induced heme oxygenase-1 (HO-1) expression. The expression of HO-1 by Whc, CA, and SiA pretreatment was due to activation of Nrf2/ARE signaling via the elevation of intracellular reactive oxygen species. To investigate the in vivo effects of Whc, Whc was administered to mice with antitype II collagen antibody-induced arthritis, and we the arthritis score and hind paw volume were measured. Administration of Whc remarkably suppressed the arthritis score and hind paw volume. Taken together, these findings suggest that Whc is beneficial for the treatment of inflammatory disease.

    Topics: Acrolein; Alcoholic Beverages; Aldehydes; Animals; Antibodies, Monoclonal; Arthritis, Experimental; Cell Line; Collagen Type II; Enzyme Induction; Heme Oxygenase-1; Interferon-gamma; Lipopolysaccharides; Macrophages; Mice; Nitric Oxide

2012
Induction of heme oxygenase-1 by whisky congeners in human endothelial cells.
    Journal of food science, 2010, Aug-01, Volume: 75, Issue:6

    It is expected that the production of the cytoprotective heme oxygenase-1 (HO-1) protein in endothelial cells would reduce severity of vascular injuries, while phenolic compounds are known to induce HO-1 mRNA and protein in various cells. We investigated the activation of HO-1 by whisky, which contains various phenolic substances. The congeners of whisky stored from 4 to 18 y in oak barrels were shown to induce an increase of HO-1 protein in human umbilical vein endothelial cells, while those of freshly distilled whisky spirit exhibited no activity. To determine the compounds with potent HO-1-inducing activity among the whisky congeners, several chemicals that had been reported to exist in whisky or oak barrels were screened, and coniferyl aldehyde and sinapyl aldehyde showed the activity. Thus, compounds that emerged in whisky during barrel storage induced cytoprotective protein, HO-1, in human endothelial cells.

    Topics: Acrolein; Alcoholic Beverages; Aldehydes; Blotting, Western; Cell Survival; Cells, Cultured; Endothelium, Vascular; Enzyme Induction; Flavonoids; Food Handling; Heme Oxygenase-1; Humans; Phenols; Polyphenols; Time Factors; Wood

2010
Application of laccase-natural mediator systems to sisal pulp: an effective approach to biobleaching or functionalizing pulp fibres?
    Bioresource technology, 2009, Volume: 100, Issue:23

    The effects of laccase-natural mediator systems (LMS) on sisal pulp and their potential for either biobleaching or functionalizing (via radical-coupling) its fibres were investigated. The enzyme treatment (L stage) was followed by extraction with hydrogen peroxide in order to determine whether observable effects could be enhanced by removing LMS-modified lignin. Four different plant phenols [viz. the p-hydroxycinnamic compounds sinapic acid (SNC), ferulic acid (FRC), coniferyl aldehyde (CLD) and sinapyl aldehyde (SLD)] were used as laccase redox mediators and their effects on pulp and effluents compared with those of the synthetic compound 1-hydroxybenzotriazole (HBT). During the L stage performed with HBT, laccase underwent a loss of 99% and 78% of the initial activity, in the absence and presence of pulp, respectively. With natural mediators inactivation was markedly reduced, being the residual activity between 65% and 100% of the initial one, in the presence of pulp. The pulp was found to protect the enzyme against inactivation: the activity was only reduced by 45% in its presence. Under the operating conditions used the natural mediators proved less efficient than HBT in facilitating pulp bleaching; rather, they tended to bind to pulp fibres. This effect could be used to functionalize fibres in order to improve intrinsic properties of pulp or introducing novel ones (e.g. antimicrobial, antioxidant, optical properties, etc.). This paper shows for the first time the application of laccase-mediator systems to sisal pulp.

    Topics: Acrolein; Aldehydes; Anions; Biotechnology; Coumaric Acids; Hydrogen Peroxide; Laccase; Lignin; Oxidation-Reduction; Oxygen; Paper; Phenol; Trees; Wood

2009
Identification and characterisation of Arabidopsis glycosyltransferases capable of glucosylating coniferyl aldehyde and sinapyl aldehyde.
    FEBS letters, 2005, May-23, Volume: 579, Issue:13

    This study describes the substrate recognition profile of UGT72E1, an UDP-glucose:glycosyltransferase of Arabidopsis thaliana that is the third member of a branch of glycosyltransferases, capable of conjugating lignin monomers and related metabolites. The data show that UGT72E1, in contrast to the two closely related UGTs 72E2 and 72E3, is specific for sinapyl and coniferyl aldehydes. The biochemical properties of UGT72E1 are characterised, and are compared with that of UGT72E2, which is capable of glycosylating the aldehydes as well as coniferyl and sinapyl alcohols.

    Topics: Acrolein; Aldehydes; Arabidopsis; Arabidopsis Proteins; Electrophoresis, Polyacrylamide Gel; Glucosyltransferases; Glycosylation; Glycosyltransferases; Kinetics; Recombinant Proteins

2005