Disease relevance of Caffeate

• We report crystallographic analyses of unliganded Rhodobacter sphaeroides tyrosine ammonia-lyase (RsTAL) and RsTAL bound to p-coumarate and caffeate [1].
• Inhibition of tumor metastasis by sodium caffeate and its effect on angiogenesis [2].
• Chemiosmotic energy conservation with Na(+) as the coupling ion during hydrogen-dependent caffeate reduction by Acetobacterium woodii [3].
• In an appropriate genetic background, it was possible to select for an Acinetobacter strain that had lost the ability to grow with caffeate, a commonly occurring hydroxycinnamate [4].
• In conclusion, we demonstrate that a novel potent antioxidant, octyl caffeate, significantly ameliorates circulatory failure of endotoxemia in vivo by a mechanism involving suppression of iNOS expression through inactivation of mitogen-activated protein kinases in RASMCs [5].

High impact information on Caffeate

• Poplars expressing cinnamyl alcohol dehydrogenase (CAD) or caffeate/5-hydroxy-ferulate O-methyltransferase (COMT) antisense transgenes were grown for four years at two sites, in France and England. The trees remained healthy throughout the trial [6].
• 5-Hydroxyconiferyl aldehyde also inhibited the caffeate and 5-hydroxyferulate methylation activities of xylem proteins from various angiosperm tree species [7].
• When the hcaA mutation was combined with a mutation in the repressor HcaR, exposure of the doubly mutated Acinetobacter cells to caffeate, p-coumarate, or ferulate at 10(-6) M totally inhibited the growth of cells [8].
• On the other hand, octyl caffeate (10 and 50 microM) significantly suppressed activation of c-Jun-N-terminal kinase and extracellular signal-regulated kinase [5].
• In addition, we found that octyl caffeate did not significantly affect IkappaBalpha degradation stimulated by LPS/IFN-gamma in RASMCs [5].

Chemical compound and disease context of Caffeate

• Cell suspensions of Acetobacterium woodii prepared from cultures grown on fructose plus caffeate catalyzed caffeate reduction with electrons derived from molecular hydrogen [3].

Biological context of Caffeate

• Octyl caffeate (0.1-1.0 microM) exerted a concentration-dependent inhibition of iron-catalyzed lipid peroxidation in rat brain homogenates [5].
• The sodium ionophore ETH2120, but not protonophores, stimulated hydrogen-dependent caffeate reduction by 280%, indicating that caffeate reduction is coupled to the buildup of a membrane potential generated by primary Na(+) extrusion [3].
• Caffeic acid, methyl caffeate, rosmarinic acid, and luteolin 7-O-glucuronide-6"-methyl ester were isolated as active constituents from the extract of the typical strain of P. frutescens, and their IC50 values for PDGF-induced mesangial cell proliferation were estimated as 26 microM, 2.6 microM, 1.8 microM, and 4.1 microM, respectively [9].
• Both copper and iron enhanced the radical intensity of ascorbates, but slightly reduced the radical intensity of gallate and caffeate, suggesting that radical intensity is not the sole determinant of apoptosis induction [10].
• Copper also stimulated the gallate or caffeate-induced apoptotic cell death, whereas iron was inhibitory [10].

Anatomical context of Caffeate

• The result suggests that dehydrodicaffeates are formed in the cell walls from two molecules of caffeate, probably formed through C-C, and C-O-C coupling processes [11].
• Sodium caffeate induces endothelial cell apoptosis and inhibits VEGF expression in cancer cells [12].

Associations of Caffeate with other chemical compounds

• The enzyme has a pI of 6.5, and maximum activity is observed at pH 6.7 and 60 degrees C. Specific activities for methyl ferulate, methyl p-coumarate, methyl sinapate, and methyl caffeate are 21.6, 35.3, 12.9, and 30.4 micro mol/min/mg, respectively [13].
• The ATPase inhibitor N,N'-dicyclohexylcarbodiimide (DCCD) abolished ATP synthesis, and at the same time, hydrogen-dependent caffeate reduction was inhibited [3].

Gene context of Caffeate

• These results suggest that ROS generated through activation of NADPH oxidase may play an essential role in the apoptosis induced by CA and FA in HepG2 cells [14].

References