The Dietary Nutrient Trimethylamine N-Oxide Affects the Phospholipid Vesicle Membrane: Probable Route to Adverse Intake

Author(s):  
Sourav Nandi ◽  
Arghajit Pyne ◽  
Souvik Layek ◽  
Chirag Arora ◽  
Nilmoni Sarkar
RSC Advances ◽  
2016 ◽  
Vol 6 (50) ◽  
pp. 44456-44458 ◽  
Author(s):  
M. Poznik ◽  
B. König

Co-embedding of an amphiphilic non-chiral hydrolysis catalyst with amphiphilic chiral additives into the membrane of a phospholipid vesicle induces different rates of ester hydrolysis for enantiomeric amino acid esters.


2005 ◽  
Vol 283 (9) ◽  
pp. 987-993 ◽  
Author(s):  
Kazuma Yasuhara ◽  
Akio Ohta ◽  
Yoshihiro Asakura ◽  
Taishi Kodama ◽  
Tsuyoshi Asakawa ◽  
...  

2009 ◽  
Vol 58 (12) ◽  
pp. 607-615 ◽  
Author(s):  
Akio Ohta ◽  
Yuya Miyazato ◽  
Hiroyasu Sasaki ◽  
Kazuma Yasuhara ◽  
Tsuyoshi Asakawa

Langmuir ◽  
2020 ◽  
Vol 36 (9) ◽  
pp. 2459-2473
Author(s):  
Sourav Nandi ◽  
Arghajit Pyne ◽  
Meghna Ghosh ◽  
Pavel Banerjee ◽  
Biswajoy Ghosh ◽  
...  

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Sonja Christiane Bäßler ◽  
Ákos Kenéz ◽  
Theresa Scheu ◽  
Christian Koch ◽  
Ulrich Meyer ◽  
...  

AbstractMetabolic consequences of an energy and protein rich diet can compromise metabolic health of cattle by promoting a pro-inflammatory phenotype. Laminitis is a common clinical sign, but affected metabolic pathways, underlying pathophysiology and causative relationships of a systemic pro-inflammatory phenotype are unclear. Therefore, the aim of this study was to elucidate changes in metabolome profiles of 20 months old Holstein bulls fed a high energy and protein diet and to identify novel metabolites and affected pathways, associated with diet-related laminitis. In a randomized controlled feeding trial using bulls fed a high energy and protein diet (HEP; metabolizable energy [ME] intake 169.0 ± 1.4 MJ/day; crude protein [CP] intake 2.3 ± 0.02 kg/day; calculated means ± SEM; n = 15) versus a low energy and protein diet (LEP; ME intake 92.9 ± 1.3 MJ/day; CP intake 1.0 ± 0.01 kg/day; n = 15), wide ranging effects of HEP diet on metabolism were demonstrated with a targeted metabolomics approach using the AbsoluteIDQ p180 kit (Biocrates Life Sciences). Multivariate statistics revealed that lower concentrations of phosphatidylcholines and sphingomyelins and higher concentrations of lyso-phosphatidylcholines, branched chain amino acids and aromatic amino acids were associated with an inflammatory state of diet-related laminitis in Holstein bulls fed a HEP diet. The latter two metabolites share similarities with changes in metabolism of obese humans, indicating a conserved pathophysiological role. The observed alterations in the metabolome provide further explanation on the underlying metabolic consequences of excessive dietary nutrient intake.


1987 ◽  
Vol 60 (11) ◽  
pp. 3849-3853 ◽  
Author(s):  
Mitsuhiro Takasaki ◽  
Noboru Takisawa ◽  
Keishiro Shirahama

2013 ◽  
Vol 453 (1) ◽  
pp. 37-47 ◽  
Author(s):  
Stefan Mahrhold ◽  
Jasmin Strotmeier ◽  
Consuelo Garcia-Rodriguez ◽  
Jianlong Lou ◽  
James D. Marks ◽  
...  

The highly specific binding and uptake of BoNTs (botulinum neurotoxins; A–G) into peripheral cholinergic motoneurons turns them into the most poisonous substances known. Interaction with gangliosides accumulates the neurotoxins on the plasma membrane and binding to a synaptic vesicle membrane protein leads to neurotoxin endocytosis. SV2 (synaptic vesicle glycoprotein 2) mediates the uptake of BoNT/A and /E, whereas Syt (synaptotagmin) is responsible for the endocytosis of BoNT/B and /G. The Syt-binding site of the former was identified by co-crystallization and mutational analyses. In the present study we report the identification of the SV2-binding interface of BoNT/E. Mutations interfering with SV2 binding were located at a site that corresponds to the Syt-binding site of BoNT/B and at an extended surface area located on the back of the conserved ganglioside-binding site, comprising the N- and C-terminal half of the BoNT/E-binding domain. Mutations impairing the affinity also reduced the neurotoxicity of full-length BoNT/E at mouse phrenic nerve hemidiaphragm preparations demonstrating the crucial role of the identified binding interface. Furthermore, we show that a monoclonal antibody neutralizes BoNT/E activity because it directly interferes with the BoNT/E–SV2 interaction. The results of the present study suggest a novel mode of binding for BoNTs that exploit SV2 as a cell surface receptor.


Nutrients ◽  
2017 ◽  
Vol 9 (3) ◽  
pp. 221 ◽  
Author(s):  
Yan Zhang ◽  
Hong Zhou ◽  
Anthony Perkins ◽  
Yan Wang ◽  
Jing Sun

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