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Plasma zinc's alter ego is a low-molecular-weight humoral factor
Ou, Ou,Allen-Redpath, Keith,Urgast, Dagmar,Gordon, Margaret-Jane,Campbell, Gill,Feldmann, Jö,rg,Nixon, Graeme F.,Mayer, Claus-Dieter,Kwun, In-Sook,Beattie, John H. The Federation of American Societies for Experimen 2013 The FASEB Journal Vol.27 No.9
<P>Mild dietary zinc deprivation in humans and rodents has little effect on blood plasma zinc levels, and yet cellular consequences of zinc depletion can be detected in vascular and other tissues. We proposed that a zinc-regulated humoral factor might mediate the effects of zinc deprivation. Using a novel approach, primary rat vascular smooth muscle cells (VSMCs) were treated with plasma from zinc-deficient (<1 mg Zn/kg) or zinc-adequate (35 mg Zn/kg, pair-fed) adult male rats, and zinc levels were manipulated to distinguish direct and indirect effects of plasma zinc. Gene expression changes were analyzed by microarray and qPCR, and incubation of VSMCs with blood plasma from zinc-deficient rats strongly changed the expression of >2500 genes, compared to incubation of cells with zinc-adequate rat plasma. We demonstrated that this effect was caused by a low-molecular-weight (∼2-kDa) zinc-regulated humoral factor but that changes in gene expression were mostly reversed by adding zinc back to zinc-deficient plasma. Strongly regulated genes were overrepresented in pathways associated with immune function and development. We conclude that zinc deficiency induces the production of a low-molecular-weight humoral factor whose influence on VSMC gene expression is blocked by plasma zinc. This factor is therefore under dual control by zinc.—Ou, O., Allen-Redpath, K., Urgast, D., Gordon, M.-J., Campbell, G., Feldmann, J., Nixon, G. F., Mayer, C.-D., Kwun, I.-S., and Beattie, J. H. Plasma zinc's alter ego is a low-molecular-weight humoral factor.</P>
On Using Gait to Enhance Frontal Face Extraction
Sung-Uk Jung,Nixon, M. S. IEEE 2012 IEEE transactions on information forensics and sec Vol.7 No.6
<P>Visual surveillance finds increasing deployment for monitoring urban environments. Operators need to be able to determine identity from surveillance images and often use face recognition for this purpose. In surveillance environments, it is necessary to handle pose variation of the human head, low frame rate, and low resolution input images. We describe the first use of gait to enable face acquisition and recognition, by analysis of 3-D head motion and gait trajectory, with super-resolution analysis. We use region- and distance-based refinement of head pose estimation. We develop a direct mapping to relate the 2-D image with a 3-D model. In gait trajectory analysis, we model the looming effect so as to obtain the correct face region. Based on head position and the gait trajectory, we can reconstruct high-quality frontal face images which are demonstrated to be suitable for face recognition. The contributions of this research include the construction of a 3-D model for pose estimation from planar imagery and the first use of gait information to enhance the face extraction process allowing for deployment in surveillance scenarios.</P>
Huang, Chang-Yi,Nixon, Peter F.,Duggleby, Ronald G. Korean Society for Biochemistry and Molecular Biol 1999 Journal of biochemistry and molecular biology Vol.32 No.1
Pyruvate decarboxylase (PDC) catalyzes the conversion of pyruvate to acetaldehyde as the penultimate step in alcohol fermentation. The enzyme requires two cofactors, thiamin diphosphate (ThDP) and $Mg^{2+}$, for activity. Zymomonas mobilis PDC shows a strong preference for pyruvate although it will use the higher homologues 2-ketobutyrate and 2-ketovalerate to some extent. We have investigated the effect of mutagenesis of valine 111 and leucine 112 on the substrate specificity. V111 was replaced by glycine, alanine, leucine, and isoleucine while L112 was replaced by alanine, valine, and isoleucine. With the exception of L112I, all mutants retain activity towards pyruvate with $k_{cat}$ values ranging from 40% to 139% of wild-type. All mutants show changes from wild-type in the affinity for ThDP, and several (V111A, L112A, and L112V) show decreases in the affinity for $Mg^{2+}$. Two of the mutants, V111G and V111A, show an increase in the $K_m$ for pyruvate. The activity of each mutant towards 2-ketobutyrate and 2-ketovalerate was investigated and some changes from wild-type were found. For the V111 mutants, the most notable of these is a 3.7-fold increase in the ability to use 2-ketovalerate. However, the largest effect is observed for the L112V mutation which increases the ability to use both 2-ketobutyrate (4.3-fold) and 2-ketovalerate (5.7-fold). The results suggest that L112 and, to a lesser extent, V111 are close to the active site and may interact with the alkyl side-chain of the substrate.
Duggleby, Ronald G.,Huang, Chang-Yi,Nixon,Peter F. The Korea Science and Technology Center 1999 BMB Reports Vol.32 No.1
Pyruvate decarboxylase (PDC) catalyzes the conversion of pyruvate to acetaldehyde as the penultimate step in alcohol fermentation. The enzyme requires two cofactors, thiamin diphosphate (ThDP) and Mg²+ for activity. Zymomonas PDC shows a strong preference for pyruvate although it will use the higher homologues 2-ketobutyrate and 2-ketovalerate to some extent. We have investigated the effect of mutagenesis of valine 111 and leucine 112 on the substrate specificity. V111 was replaced by glycine, alanine, leucine, and isoleucine while L112 was replaced by alanine, valine, and isoleucine. With the exception of L112I, all mutants retains activity towards pyruvate with k cat values ranging from 40% to 139% of wild-type. All mutants show changes from wild-type in the affinity for ThDP, and several (V111A, L112A, and L112V) show decreases in the affinity for Mg²+. Two of the mutants, V111G and V111A, show an increase in the K m for pyruvate. The activity of each mutant towards 2-ketobutyrate and 2-ketovalerate was investigated and some changes from wild-type were found. For the V111 mutants, the most notable of these is a 3.7-fold increase in the ability to use 2-ketovalerate. However, the largest effect is observed for the L112V mutation which increases the ability to use both 2-ketobutyrate (4.3-fold) and 2-ketovalerate (5.7-fold). The results suggest that L112 and, to a lesser extent, V111 are close to the active site and may interact with the alkyl side-chain of the substrate.
Duggleby, Ronald G .,Huang, Chang Yi,Nixon, Peter F . 생화학분자생물학회 1997 BMB Reports Vol.32 No.1
Pyruvate decarboxylase (PDC) catalyzes the conversion of pyruvate to acetaldehyde as the penultimate step in alcohol fermentation. The enzyme requires two cofactors, thiamin diphosphate (ThDP) and Mg^(2+), for activity. Zymomonas mobilis PDC shows a strong preference for pyruvate although it will use the higher homologues 2-ketobutyrate and 2-ketovalerate to some extent. We have investigated the effect of mutagenesis of valine 111 and leucine 112 on the substrate specificity. V111 was replaced by glycine, alanine, leucine, and isoleucine while L112 was replaced by alanine, valine, and isoleucine. With the exception of L1121, all mutants retain activity towards pyruvate with k_cat values ranging from 40% to 139% of wild-type. All mutants show changes from wild-type in the affinity for ThDP, and several (V111A, L112A, and L112V) show decreases in the affinity for Mg ^(2+). Two of the mutants, V111G and V111A, show an increase in the K_m for pyruvate. The activity of each mutant towards 2-ketobutyrate and 2-ketovalerate was investigated and some changes from wild-type were found. For the V111 mutants, the most notable of these is a 3.7-fold increase in the ability to use 2-ketovalerate. However, the largest effect is observed for the L112V mutation which increases the ability to use both 2-ketobutyrate (4.3-fold) and 2-ketovalerate (5.7-fold). The results suggest that L112 and, to a lesser extent, V111 are close to the active site and may interact with the alkyl side-chain of the substrate.