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Thermodynamic and NMR analyses of NADPH binding to lipocalin-type prostaglandin D synthase.

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Thermodynamic and NMR analyses of NADPH binding to lipocalin-type prostaglandin D synthase.

Post  CF on Mon Feb 22, 2016 1:19 am

Biochem Biophys Res Commun. 2015 Dec 4; Epub 2015 Oct 27.
Thermodynamic and NMR analyses of NADPH binding to lipocalin-type prostaglandin D synthase.
Qin S1, Shimamoto S2, Maruno T3, Kobayashi Y3, Kawahara K1, Yoshida T1, Ohkubo T4.

Lipocalin-type prostaglandin D synthase (L-PGDS) is one of the most abundant proteins in human cerebrospinal fluid (CSF) with dual functions as a prostaglandin D2 (PGD2) synthase and a transporter of lipophilic ligands. Recent studies revealed that L-PGDS plays important roles in protecting against various neuronal diseases induced by reactive oxygen species (ROS). However, the molecular mechanisms of such protective actions of L-PGDS remain unknown. In this study, we conducted thermodynamic and nuclear magnetic resonance (NMR) analyses, and demonstrated that L-PGDS binds to nicotinamide coenzymes, including NADPH, NADP(+), and NADH. Although a hydrophilic ligand is not common for L-PGDS, these ligands, especially NADPH showed specific interaction with L-PGDS at the upper pocket of its ligand-binding cavity with an unusually bifurcated shape. The binding affinity of L-PGDS for NADPH was comparable to that previously reported for NADPH oxidases and NADPH in vitro. These results suggested that L-PGDS potentially attenuates the activities of NADPH oxidases through interaction with NADPH. Given that NADPH is the substrate for NADPH oxidases that play key roles in neuronal cell death by generating excessive ROS, these results imply a novel linkage between L-PGDS and ROS.

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Re: Thermodynamic and NMR analyses of NADPH binding to lipocalin-type prostaglandin D synthase.

Post  CF on Mon Feb 22, 2016 1:25 am

If NADPH can be elevated (for example, by reducing 5ar, or perhaps by other means) then would the increased NADPH bind to L-PGDS thereby preventing it from making PGD2?

And is there anything special that should be done to prevent the extra NADPH from producing too much NADPH oxidase?

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Re: Thermodynamic and NMR analyses of NADPH binding to lipocalin-type prostaglandin D synthase.

Post  CausticSymmetry on Mon Feb 22, 2016 3:18 am

CF wrote:If NADPH can be elevated (for example, by reducing 5ar, or perhaps by other means) then would the increased NADPH bind to L-PGDS thereby preventing it from making PGD2?

And is there anything special that should be done to prevent the extra NADPH from producing too much NADPH oxidase?
 
One way is to use a curcumin/resveratrol which can prevent the excessive oxidation rate of NADPH that can occur from copper.

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Re: Thermodynamic and NMR analyses of NADPH binding to lipocalin-type prostaglandin D synthase.

Post  CF on Mon Feb 22, 2016 3:23 am

Thank you, CS.

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Re: Thermodynamic and NMR analyses of NADPH binding to lipocalin-type prostaglandin D synthase.

Post  CF on Mon Feb 22, 2016 3:36 am

Cell. 2010 Nov 24; j.cell.2010.10.002.
Sirt3 mediates reduction of oxidative damage and prevention of age-related hearing loss under caloric restriction.
Someya S1, Yu W, Hallows WC, Xu J, Vann JM, Leeuwenburgh C, Tanokura M, Denu JM, Prolla TA.
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Abstract
Caloric restriction (CR) extends the life span and health span of a variety of species and slows the progression of age-related hearing loss (AHL), a common age-related disorder associated with oxidative stress. Here, we report that CR reduces oxidative DNA damage in multiple tissues and prevents AHL in wild-type mice but fails to modify these phenotypes in mice lacking the mitochondrial deacetylase Sirt3, a member of the sirtuin family. In response to CR, Sirt3 directly deacetylates and activates mitochondrial isocitrate dehydrogenase 2 (Idh2), leading to increased NADPH levels and an increased ratio of reduced-to-oxidized glutathione in mitochondria. In cultured cells, overexpression of Sirt3 and/or Idh2 increases NADPH levels and protects from oxidative stress-induced cell death. Therefore, our findings identify Sirt3 as an essential player in enhancing the mitochondrial glutathione antioxidant defense system during CR and suggest that Sirt3-dependent mitochondrial adaptations may be a central mechanism of aging retardation in mammals.

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Re: Thermodynamic and NMR analyses of NADPH binding to lipocalin-type prostaglandin D synthase.

Post  CF on Mon Feb 22, 2016 3:38 am


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Re: Thermodynamic and NMR analyses of NADPH binding to lipocalin-type prostaglandin D synthase.

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