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10.1096/fj.13-240309 http://scihub22266oqcxt.onion/10.1096/fj.13-240309 24421402!ä!24421402 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       FASEB+J 2014 ; 28 (4): 1769-79 Nephropedia Template TP {{tp|p=24421402|t=2014. Breaking the chain at the membrane: paraoxonase 2 counteracts lipid peroxidation at the plasma membrane |pdf=|usr=}}{{24421402}} gab.com Text Breaking the chain at the membrane: paraoxonase 2 counteracts lipid peroxidation at the plasma membrane JO: FASEB J http://www.kidney.de/pget.php?&tw=1&pmid=24421402 #FOAvip Lipid peroxidation through electrophilic molecules of extracellular origin is involved in the pathogenesis of many inflammatory conditions. To counteract free radical actions at the plasma membrane, cells host a variety of antioxidative enzymes. Here we analyzed localization, membrane topology, and trafficking of PON2 a member of the paraoxonase family of 3 enzymatically active proteins (PON1-3) found to have antiatherogenic properties. Immunohistochemistry localized PON2 to the villous tip of human intestinal epithelial cells. Employing membrane preparations, surface biotinylation experiments, and mutational analyses in HEK 293T and HeLa cells, we demonstrate that PON2 is a type II transmembrane protein. A hydrophobic stretch in the N terminus was identified as single transmembrane domain of PON2. The enzymatically active domain faced the extracellular compartment, where it suppressed lipid peroxidation (P<0.05) and regulated the glucosylceramide content, as demonstrated by mass spectrometry (P<0.05). PON2 translocation to the plasma membrane was dependent on intracellular calcium responses and could be induced to >10-fold as compared to baseline (P=0.0001) by oxidative stress. Taken together, these data identify the paraoxonase protein PON2 as a type II transmembrane protein, which is dynamically translocated to the plasma membrane in response to oxidative stress to counteract lipid peroxidation. Twit Text FOAVip Breaking the chain at the membrane: paraoxonase 2 counteracts lipid peroxidation at the plasma membrane ????FASEB J http://www.kidney.de/pget.php?&tw=1&pmid=24421402 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24421402 #FOAvip English Wikipedia <ref>{{Cite pmid|24421402}}</ref> Breaking the chain at the membrane: paraoxonase 2 counteracts lipid peroxidation at the plasma membrane #MMPMID24421402 Hagmann H; Kuczkowski A; Ruehl M; Lamkemeyer T; Brodesser S; Horke S; Dryer S; Schermer B; Benzing T; Brinkkoetter PT FASEB J 2014[Apr]; 28 (4): 1769-79 PMID24421402show ga Lipid peroxidation through electrophilic molecules of extracellular origin is involved in the pathogenesis of many inflammatory conditions. To counteract free radical actions at the plasma membrane, cells host a variety of antioxidative enzymes. Here we analyzed localization, membrane topology, and trafficking of PON2 a member of the paraoxonase family of 3 enzymatically active proteins (PON1-3) found to have antiatherogenic properties. Immunohistochemistry localized PON2 to the villous tip of human intestinal epithelial cells. Employing membrane preparations, surface biotinylation experiments, and mutational analyses in HEK 293T and HeLa cells, we demonstrate that PON2 is a type II transmembrane protein. A hydrophobic stretch in the N terminus was identified as single transmembrane domain of PON2. The enzymatically active domain faced the extracellular compartment, where it suppressed lipid peroxidation (P<0.05) and regulated the glucosylceramide content, as demonstrated by mass spectrometry (P<0.05). PON2 translocation to the plasma membrane was dependent on intracellular calcium responses and could be induced to >10-fold as compared to baseline (P=0.0001) by oxidative stress. Taken together, these data identify the paraoxonase protein PON2 as a type II transmembrane protein, which is dynamically translocated to the plasma membrane in response to oxidative stress to counteract lipid peroxidation. |*Lipid Peroxidation[MESH] |Amino Acid Sequence[MESH] |Animals[MESH] |Aryldialkylphosphatase/genetics/*metabolism[MESH] |Calcium/metabolism[MESH] |Cell Membrane/*metabolism[MESH] |Epithelial Cells/enzymology[MESH] |Glucosylceramides/metabolism[MESH] |HEK293 Cells[MESH] |HeLa Cells[MESH] |Humans[MESH] |Immunoblotting[MESH] |Immunohistochemistry[MESH] |Intestines/cytology/enzymology[MESH] |Membrane Proteins/genetics/*metabolism[MESH] |Mice[MESH] |Microscopy, Confocal[MESH] |Molecular Sequence Data[MESH] |Oxidative Stress[MESH] |Protein Transport[MESH]Breaking the chain at the membrane: paraoxonase 2 counteracts lipid pe(epmc).pdf DeepDyve Pubget Overpricing