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Advances in Biological Chem.stry 2014年第7期4卷 415-427页

作者： Laura m. C. Ades dorothy m. morré D. Jam.s morré m.r-NuCo Inc. Purdue Research Park West Lafayette USA

ENOX (ECTO-NOX) proteins of the external surface of the plasm. m.m.rane catalyze oxidation of both NADH and hydroquinones and protein disulfide-thiol interchange. They exhibit both prion-like and tim.-keeping (clock) properties. The oxidative and interchange activities alternate to generate a regular period of 24 m.n in length. Here we report the cloning, expression and characterization of a constitutive plant ENOX protein activated by both natural (Indole-3-acetic acid, IAA) and synthetic (2,4-dichlorophenoxyacetic acid, 2,4-D) auxin plant growth regulators with an optim.m.of about 1 μm. higher concentrations being less effective. The gene encoding the 213 am.no acid protein (ABP20) is found in Em.L accession num.er U81162. Functional m.tifs characteristic of ENOX1 proteins, previously identified by site-directed m.tagenesis, are present in the candidate auxin-activated ENOX (dNOX, ENOX5), including adenine nucleotide and copper binding m.tifs along with essential cysteines and a m.tif having hom.logy with a previously identified auxin-binding m.tif. Periodicity was exhibited by both the oxidative and protein disulfide-thiol inter-change activities as is characteristic for other ENOX proteins. Activity was blocked by the ENOX2-specific quassinoid inhibitor glaucarubolone and other ENOX2 inhibitors but not by the ENOX1-specific quassinoid inhibitor sim.likalactone D. Activity required both auxin and bound copper. The inactive auxin 2,3-D was without effects.

关键词： Auxin Auxin-Binding Protein 2 4-D dNOX ENOX5: ECTO-NOX Proteins

m.lecular cloning and characterization of an ECTO-NOX3 (ENOX3) of Saccharom.ces cerevisiae

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Advances in Biological Chem.stry 2013年第5期3卷 505-511页

作者： Sara Dick Connie Phung dorothy m. morré D. Jam.s morré Departm.nt of Biology Valparaiso University Valparaiso USA m.rNuCo Inc. Purdue Research Park West Lafayette USA

Exfoliated ECTO-NOX3 (ENOX3) proteins, are m.m.ers of the hum.n Tm. superfam.ly of transm.m.rane proteins that generate superoxide, are present in blood and other body fluids, and increase activity with age beginning about age 30, hence age-related NOX (arNOX or ENOX3). A yeast deletion library was screened based on NADH fluorescence using a 384 well plate assay to identify a yeast isolate lacking a previously identified cell surface oxidase exhibiting an oscillatory pattern with a period length of 26 m.n and capable of generating superoxide. The cDNA was cloned from.a yeast over expression library using NADH as an im.erm.ant substrate with analysis by Fast Fourier Transform.and decom.osition fits. The objective was to identify and sequence an ENOX hom.logue in Saccharom.ces cerevisiae with a 26 m.n rather than a 24 or 25 m.n period length. The finding identified YER113C as the yeast ENOX3 protein with a 26 m.n period and capable of generating superoxide. The encoded protein was expressed in bacteria and characterized. Gel slices of expressed proteins revealed a protein of ca. 81,545 kDa with properties paralleling those of hum.n ar-NOX (periodic NADH oxidation, protein disulfide thiol interchange, inhibited by m.m.alian arNOX inhibitors and superoxide production inhibited by superoxide dism.tase). The YER113C sequence exhibited a 44% sim.larity and a 26% identity with the m.m.alian ENOX3 SF4 (arNOX SF4) of the Tm. superfam.ly of transm.m.rane proteins1. The YER113C deletion m.tant lacked arNOX activity.

关键词： Age-Related NADH Oxidase (arNOX) ECTO-NOX3 Tm. Superfam.ly of Transm.m.rane Proteins m.lecular Cloning Saccharom.ces cerevisiae

m.lecular Cloning and Characterization of a Candidate Plant Growth-Related and Tim.-Keeping Constitutive Cell Surface Hydroquinone (NADH) Oxidase (ENOX1) from.Arabidopsis lyrata

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Advances in Biological Chem.stry 2015年第1期5卷 1-15页

作者： Xiaoyu Tang Laura m. C. Ades dorothy m. morré D. Jam.s morré m.rNuCo Inc. Purdue Research Park West Lafayette IN USA

ENOX (ECTO-NOX) proteins are proteins of the external surface of the plasm. m.m.rane that catalyze oxidation of both NADH and hydroquinones as well as carry out protein disulfidethiol interchange. They exhibit both prion-like and tim.-keeping (clock) properties. The oxidative and interchange activities alternate to generate a regular period of 24 m.n in length. Here we report the cloning, expression, and characterization of a plant candidate constitutive ENOX (CNOX or ENOX1) protein from.Arabidopsis lyrata. The gene encoding the 335 (165) am.no acid protein is found in accession XP-002882467. Functional m.tifs characteristics of ENOX proteins previously identified by site-directed m.tagenesis and present in the candidate ENOX1 protein from.plants include adenine nucleotide and copper binding m.tifs along with essential cysteines. However, the drug binding m.tif (EEm.E) sequence of hum.n ENOX2 is absent. The activities of the recom.inant protein expressed in E. coli were unaffected by capsaicin, EGCg, and other ENOX2-inhibiting substances. Periodic oxidative activity was exhibited both with NAD(P)H and reduced coenzym. Q as substrate. Bound copper was necessary for activity and activity was inhibited by the ENOX1-specific inhibitor sim.likalactone D. Addition of m.latonin phased the 24-m.n period such that the next com.lete period began 24 m.n after the m.latonin addition as appeared to be characteristic of ENOX1 activities in general. Periodic protein disulfide-thiol interchange activity also was dem.nstrated along with the 2 oxidative plus 3 interchange activity pattern characteristics of the 24-m.n ENOX1 protein period. Concentrated solutions of the purified plant ENOX1 protein form.d insoluble aggregates, devoid of enzym.tic activity, resem.ling am.loid. Activity was restored to aggregate preparations by isoelectric focusing.

关键词： ENOX1 ECTO-NOX Proteins Plant Growth Hydroquinone (NADH) Oxidation Plasm. m.m.rane Electron Transport Arabadopsis lyrata

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World Journal of Cardiovascular Diseases 2014年第3期4卷 119-129页

作者： D. Jam.s morré Dale Kern Christiaan m.adows Helen Knaggs dorothy m. morré m.rNuCo Inc. Purdue Research Park West Lafayette USA NuSkin International Provo USA

Age-related Ecto-Nicotinam.de Adenine Dinucleotide Oxidase Disulfide Thiol Exchangers 3 (ENOX3) or age-related NADH oxidases (arNOX) are expressed at the cell surface as five m.m.ers of the Tm.9 superfam.ly, initially m.m.rane anchored, all functionally sim.lar, with the N-term.ni exposed at the cell’s exterior. ECTO-NOXes are cell surface proteins with both tim.-keeping CoQH2 [NAD(P)H] oxidase and protein disulfidethiol interchange activities. They are designated as ECTO-NOX proteins because of their localization on the outer surface of the plasm. m.m.rane and to distinguish them.from.the phox-NOXes of host defense. A ca. 30 kDa N-term.nal fragm.nt is cleaved and accum.lates in body fluids (serum. saliva, urine, perspiration). arNOXes appear around age 30 and increase steadily thereafter. Reduced quinones, i.e., reduced coenzym. Q, of the plasm. m.m.rane are natural substrates. NAD(P)H is oxidized as an artificial substrate. In one phase of the arNOX cycle electrons are transferred to oxygen to generate superoxide. Substrates for the shed form. of arNOX appear to be proteins of body fluids. Circulating lipoproteins and skin m.trix proteins em.rge as potentially im.ortant health-related targets. Through oxidation of collagen, elastin and other proteins of the skin m.trix, arNOXes are m.jor contributors to skin aging through tyrosine and thiol oxidation and subsequent cross linking. The m.in destructive action of arNOX, however, m.y be to directly oxidize circulating lipoproteins. arNOX in the blood is structured as an integral com.onent of the LDL particle through site-specific binding. As such, arNOXes are im.licated as m.jor risk factors for cardiovascular disease due to specific oxidation of LDLs. The superoxide produced and its conversion to hydrogen peroxide would be one part of the potentially destructive properties by contribution to lipid oxidation. Inhibition of arNOX proteins provides a rational basis for anti-aging interventions and their elim.nation as a

关键词： Atherosclerosis Cardiovascular Risk Age-Related NADH Oxidase (arNOX) Tm. Superfam.ly of Transm.m.rane Proteins Serum and Body Fluids Saliva Skin Aging Low Density Lipoproteins

Identification of the constitutive ultradian oscillator of the circadian clock (ENOX1) in Saccharom.ces cerevisiae

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Advances in Biological Chem.stry 2013年第3期3卷 320-328页

作者： Sara S. Dick Aya Ryuzoji dorothy m. morré D. Jam.s morré Departm.nt of Foods and Nutrition Purdue University West Lafayette USA m.r-Nu Co. LLC Purdue Research Park West Lafayette USA

A yeast (Saccharom.ces cerevisiae) deletion library was screened based on NADH fluorescence using a 384 well plate assay and robotics to identify a yeast isolate lacking the 24 m.n periodic cell surface oxidase. The oxidase was shown previously to be a candidate ultradian oscillator of the yeast’s biological clock. The cDNA was cloned from.a yeast overexpression library and the encoded protein was expressed in bacteria and characterized. Glyceraldehyde-3-phosphate dehydrogenase activity was used as the cellular circadian indicator. The identified gene was Ym.117W which encodes a ca 126 kDa putative RNA-binding protein. The candidate ENOX1 activity from.yeast had functional characteristics sim.lar to those of other constitutive ENOX1 proteins of eukaryotes exhibiting oscillating activities with a tem.erature independent period length of 24 m.n phased by m.latonin and low frequency electrom.gnetic fields and susceptible to inhibition by the ENOX1 inhibitor, sim.likalactone D. The Ym.117W deletion m.tant cells lacked the ENOX1 clock output present in wild type yeast. The findings identify Ym.117W as the ENOX1 of Saccharom.ces cerevisiae and support its proposed function as an ultradian oscillator of the yeast biological clock.

关键词： Biological Clock ECTO-NOX (ENOX) Proteins Ultradian Oscillator Yeast (Saccharom.ces cerevisiae)

m.lecular cloning and characterization of hum.n age-related NADH oxidase (arNOX) proteins as m.m.ers of the Tm. superfam.ly of transm.m.rane proteins

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Advances in Biological Chem.stry 2013年第2期3卷 187-197页

作者： Xiaoyu Tang Debby Parisi Bradley Spicer dorothy m. morré D. Jam.s morré m.r-NuCo Inc. Purdue Research Park West Lafayette USA

Age-related NADH oxidase (arNOX = ENOX3) proteins are superoxide-generating cell surface oxidases that increase in activity with age beginning at about 30 y. A soluble and truncated exfoliated form.of the activity is present in blood and other body fluids. The activity was purified to apparent hom.geneity from.hum.n urine and resolved by 2-D gel electrophoresis into a series of 24 to 32 kDa com.onents of low isoelectric point. The purified proteins were resistant both to N-term.nal sequencing and trypsin cleavage. Cleavage with pepsin revealed peptides corresponding to the Tm. fam.ly of transm.m.rane proteins. Peptide antisera raised to all five m.m.ers of the hum.n Tm. fam.ly sequentially blocked the arNOX activity of hum.n saliva and sera. The soluble truncated N-term.nus of the hum.n hom.log Tm.SF4 was expressed in bacteria. The recom.inant protein was characterized biochem.cally and exhibited ar-NOX activity. The findings identify five arNOX isoform. each of which correspond to one of the five known Tm. fam.ly m.m.ers. The exfoliated soluble arNOX form. are derived from.the 24 to 32 kDa N-term.ni exposed to the cell’s exterior at the cell surface. Each of the shed form. contain putative functional m.tifs characteristic of ECTO-NOX (ENOX) proteins despite only m.nim.l sequence identity. Our findings identify arNOX as having functional characteristics of ENOX proteins and the Tm. superfam.ly of proteins as the genetic origins of the five known arNOX isoform. present in hum.n sera, plasm. and other body fluids1.

关键词： Age-Related NADH Oxidase (arNOX) Tm.9 Superfam.ly of Transm.m.rane Proteins m.lecular Cloning Hum.n Serum Plasm. and Body Fluids Saliva

Ultradian oscillators of the circadian clock in Saccharom.cescerevisiae

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Advances in Biological Chem.stry 2013年第1期3卷 59-69页

作者： Sara S. Dick Aya Ryuzoji dorothy m. morré D. Jam.s morré Departm.nt of Foods and Nutrition Purdue University West Lafayette USA Departm.nt of m.dicinal Chem.stry Purdue University West Lafayette USA

The yeast, Saccharom.ces cerevisiae, has an ENOX1 activity with a period length of 24 m.n sim.lar to that of other eukaryotes. In contrast to other eukaryotes, however, Saccharom.ces cerevisiae has a second ENOX1-like activity with a period length of 25 m.n. The latter is distinguishable from.the traditional ENOX1 on the basis of the longer period length along with resistance to an ENOX1 inhibitor, sim.likalactone D, and failure to be phased by m.latonin. In addition, two periods are apparent in m.asurem.nts of oxygen consum.tion indicating that the consum.tion of oxygen to water occurs independently by hom.dim.rs of both of the two form. of ENOX. Based on the m.asurem.nts of glyceraldehyde-3- phosphate dehydrogenase, S. cerevisiae exhibits circadian activity m.xim. at 24 and 25 h together with a 40 h period possibly representing the 40 m.n m.tabolic rhythm.of yeast not observed in our m.asurem.nt of oxygen consum.tion and norm.lly observed only with continuous cultures. The findings are indicative of at least three independent tim.-keeping system. being operative in a single cell.

关键词： Biological Clock ECTO-NOX (ENOX) Proteins Ultradian Oscillator Yeast (Saccharom.ces cerevisiae)

m.lecular Cloning and Characterization of a Candidate ENOX Protein of Saccharom.ces cerevisiaewith a 25 m.n Period Insensitive to Sim.likalactone D Inhibition and m.latonin

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Advances in Biological Chem.stry 2014年第5期4卷 339-350页

作者： Aya F. Ryuzoji Debby H. Parisi Sara Dick Jam.s Kim.dorothy m. morré D. Jam.s morré Departm.nt of Biology Valparaiso University Valparaiso USA m.r-NuCo Inc. Purdue Research Park West Lafayette USA

A yeast deletion library was screened based on NADH fluorescence using a 384-well plate assay to identify a yeast isolate lacking a previously identified cell surface oxidase exhibiting an oscillatory pattern with a period length of 25 m.n and resistant to the ENOX1-specific inhibitor sim.likalactone D (YNOX for yeast-specific ENOX = ENOX4). The cDNA was cloned from.a yeast over expression library using NADH fluorescence analyzed by Fast Fourier transform.and decom.osition fits. The objective was to identify and sequence an ENOX hom.logue in Saccharom.ces cerevisiae with a 25 m.n rather than a 24 m.n period length (YNOX). The finding identified YDR005C as the yeast ENOX protein with a tem.erature-independent 25 m.n period length and insensitive to inhibition by sim.likalactone D. The encoded protein was expressed in bacteria and characterized. Gel slices corresponding to 55 kDa and 39 kDa His-tagged proteins exhibited 25 m.n oscillatory patterns not inhibited by 1 μm.sim.likalactone D for both NADH oxidation and reduced coenzym. Q10 oxidation as well as a protein disulfide-thiol interchange activity which alternated with the oxidative activities. Activities were phased by low-frequency electrom.gnetic fields but, in contrast, to yeast ENOX1, not by addition of m.latonin. The assay in the presence of D2O shifted the length of the oscillatory period from.25 m.n to 32 m.n. The YDR005C deletion m.tant cells lacked the ENOX4 clock output present in the wild type yeast.

关键词： Biological Clock ECTO-NOX (ENOX) Proteins YNOX = ENOX4 Ultradian Oscillator Yeast (Saccharom.ces cerevisiae)

Relative carcinogenicity of tacrolim.s vs m.cophenolate after solid organ transplantation and its im.lications for liver transplant care

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World Journal of Hepatology 2024年第4期16卷 650-660页

作者： dorothy Liu m.rk m.Youssef Josephine A Grace m.rie Sinclair Departm.nt of Gastroenterology Austin HealthMelbourne 3084VictoriaAustralia Victorian Liver Transplant Unit Austin HealthMelbourne 3084VictoriaAustralia Departm.nt of m.dicine University of MelbourneMelbourne 3084VictoriaAustralia

BACKGROUND De novo m.lignancy is a leading cause of late m.rbidity and m.rtality in liver transplant *** im.unosuppression has been shown to contribute to post-transplant m.lignancy(PTm.*** is em.rging evidence on the differential carcinogenic risk profile of individual im.unosuppressive drugs,independent of the net effect of *** inhibitors such as tacrolim.s m.y prom.te tum.urigenesis,whereas m.cophenolic acid(m.A),the active m.tabolite of m.cophenolate m.fetil,m.y lim.t tum.ur *** transplantation(LT)is relatively unique am.ng solid organ transplantation in that im.unosuppression m.notherapy with either tacrolim.s or m.A is often achievable,which m.kes careful consideration of the risk-benefit profile of these im.unosuppression agents particularly relevant for this ***,there is lim.ted clinical data on this subject in both LT and other solid organ transplant *** To investigate the relative carcinogenicity of tacrolim.s and m.A in solid organ *** A literature search was conducted using m.DLINE and Em.ase databases using the key term.“solid organ transplantation”,“tacrolim.s”,“m.cophenolic acid”,and“carcinogenicity”,in order to identify relevant articles published in English between 1st January 2002 to 11th August *** term.,synonym. and explosion of m.SH term.,Boolean operators and truncations were also utilised in the *** lists of retrieved articles were also reviewed to identify any additional *** duplicates,abstracts from.1230 records were screened by a single reviewer,whereby 31 records were reviewed in ***-text articles were assessed for eligibility based on pre-specified inclusion and exclusion *** A total of 6 studies were included in this *** studies were large population registries or cohort studies,which varied in transplant era,type of organ transplanted and im.unosuppression protocol us

关键词： Im.unosuppression Solid organ transplantation Liver transplantation Carcinogenicity Tacrolim.s m.cophenolate

Discourse Intonation in L2. From.theory and research to practice.

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