TY - JOUR
TI - Platelet-activating factor detection, metabolism, and inhibitors in the ethanologenic bacterium Zymomonas mobilis
AU - Tsoupras, A.B.
AU - Demopoulos, C.A.
AU - Pappas, K.M.
JO - Lipid - Fett (now called European Journal of Lipid Science and Technology)
PY - 2012
VL - 114
TODO - 2
SP - 123-133
PB - 
SN - 0931-5985, 1521-4133
TODO - 10.1002/ejlt.201000489
TODO - Alphaproteobacteria;  Bacteria (microorganisms);  Oryctolagus cuniculus;  Proteobacteria;  Zymomonas mobilis
TODO - Platelet-activating factor (PAF) is a signaling phospholipid with a significant physiological role in multicellular and unicellular organisms, including fermentative organisms such as yeast. Zymomonas mobilis is an ethanologenic α-proteobacterium currently studied for bioethanol production. In order to examine the presence of PAF and/or PAF inhibitors in Z. mobilis, a new one-step high performance liquid chromatography (HPLC) separation procedure of total lipids was performed, using a C8 reversed-phase semi-preparative column. According to this method and to bioassays based on washed rabbit platelet aggregation, two lipid molecules with PAF-like activity and same retention times as those of standard PAF were detected; electron-spray ionization MS and MS/MS analysis revealed that they share similar structure with 16:0 and 18:0 PAF. Furthermore, other lipids extracted from Z. mobilis were found to exhibit a potent anti-PAF activity. Enzyme activities indicative of key PAF biosynthetic enzymes, such as dithiothreitol-insensitive cholinephosphotransferase (PAF-CPT) and lyso-PAF acetyltransferase were detected in Z. mobilis homogenates. As for PAF degradation, activity similar to that of PAF acetylhydrolase was also discovered. Overall, the presence of PAF, PAF-specific inhibitors, and enzyme activities relating to PAF metabolism, suggests that PAF may play an intrinsic role in this biotechnological organism. © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
ER -