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1.
PLoS One ; 15(7): e0235792, 2020.
Artigo em Inglês | MEDLINE | ID: mdl-32673347

RESUMO

Discovery of therapeutic avenues to provide the benefits of exercise to patients with enforced sedentary behavior patterns would be of transformative importance to health care. Work in model organisms has demonstrated that benefits of exercise can be provided to stationary animals by daily intermittent stimulation of adrenergic signaling. Here, we examine as a proof of principle whether exposure of human participants to virtual reality (VR) simulation of exercise can alter sympathovagal balance in stationary humans. In this study, 24 participants performed 15 minutes of cycling exercise at standardized resistance, then repeated the exercise with a virtual reality helmet that provided an immersive environment. On a separate day, they each controlled a virtual environment for 15 minutes to simulate exercise without actual cycling exercise. Response to each treatment was assessed by measuring heart rate (HR), norepinephrine, and heart rate variability, and each participant's response to virtual exercise was compared internally to his/her response to the actual cycling. We found that neither post-exercise norepinephrine nor post-exercise HR was significantly increased by VR simulation. However, heart rate variability measured during virtual exercise was comparable to actual cycling in participants that engaged in moderate exercise, but not in those that engaged in high-intensity exercise. These findings suggest that virtual exercise has the potential to mimic some effects of moderate exercise. Further work will be needed to examine the longitudinal effects of chronic exposure to VR-simulated exercise.


Assuntos
Exercício Físico , Realidade Virtual , Pressão Sanguínea , Feminino , Frequência Cardíaca , Humanos , Masculino , Norepinefrina/metabolismo
2.
J Integr Plant Biol ; 62(5): 601-613, 2020 May.
Artigo em Inglês | MEDLINE | ID: mdl-31081586

RESUMO

Polyamines are small aliphatic amines found in almost all organisms, ranging from bacteria to plants and animals. In most plants, putrescine, the metabolic precursor for longer polyamines, such as spermidine and spermine, is produced from arginine, with either agmatine or ornithine as intermediates. Here we show that Arabidopsis thaliana (Arabidopsis) arginine decarboxylase 1 (ADC1), one of the two known arginine decarboxylases in Arabidopsis, not only synthesizes agmatine from arginine, but also converts Nδ -acetylornithine to N-acetylputrescine. Phylogenetic analyses indicate that duplication and neofunctionalization of ADC1 and NATA1, the enzymes that synthesize Nδ -acetylornithine in Arabidopsis, co-occur in a small number of related species in the Brassicaceae. Unlike ADC2, which is localized in the chloroplasts, ADC1 is in the endoplasmic reticulum together with NATA1, an indication that these two enzymes have access to the same substrate pool. Together, these results are consistent with a model whereby NATA1 and ADC1 together provide a pathway for the synthesis of N-acetylputrescine in Arabidopsis.


Assuntos
Proteínas de Arabidopsis/metabolismo , Arabidopsis/metabolismo , Carboxiliases/metabolismo , Acetiltransferases/genética , Acetiltransferases/metabolismo , Arabidopsis/genética , Proteínas de Arabidopsis/genética , Carboxiliases/genética , Retículo Endoplasmático/metabolismo , Regulação da Expressão Gênica de Plantas , Oxigenases/genética , Oxigenases/metabolismo , Filogenia , Putrescina/análogos & derivados , Putrescina/metabolismo
3.
Plant Sci ; 262: 62-73, 2017 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-28716421

RESUMO

Two biosynthetic routes are known for putrescine, an essential plant metabolite. Ornithine decarboxylase (ODC) converts ornithine directly to putrescine, while a second route for putrescine biosynthesis utilizes arginine decarboxylase (ADC) to convert arginine to agmatine, and two additional enzymes, agmatine iminohydrolase (AIH) and N-carbamoyl putrescine aminohydrolase (NLP1) to complete this pathway. Here we show that plants can use ADC and arginase/agmatinase (ARGAH) as a third route for putrescine synthesis. Transformation of Arabidopsis thaliana ADC2, and any of the arginases from A. thaliana (ARGAH1, or ARGHA2) or the soybean gene Glyma.03g028000 (GmARGAH) into a yeast strain deficient in ODC, fully complemented the mutant phenotype. In vitro assays using purified recombinant enzymes of AtADC1 and AtARGAH2 were used to show that these enzymes can function in concert to convert arginine to agmatine and putrescine. Transient expression analysis of the soybean genes (Glyma.06g007500, ADC; Glyma.03g028000 GmARGAH) and the A. thaliana ADC2 and ARGAH genes in leaves of Nicotiana benthamiana, showed that these proteins are localized to the chloroplast. Experimental support for this pathway also comes from the fact that expression of AtARGAH, but not AtAIH or AtNLP1, is co-regulated with AtADC2 in response to drought, oxidative stress, wounding, and methyl jasmonate treatments. Based on the high affinity of ARGAH2 for agmatine, its co-localization with ADC2, and typically low arginine levels in many plant tissues, we propose that these two enzymes can be major contributors to putrescine synthesis in many A. thaliana stress responses.


Assuntos
Arginase/metabolismo , Proteínas de Plantas/metabolismo , Putrescina/biossíntese , Arabidopsis/genética , Arabidopsis/metabolismo , Proteínas de Arabidopsis/genética , Proteínas de Arabidopsis/metabolismo , Arginase/genética , Carboxiliases/genética , Carboxiliases/metabolismo , Cloroplastos/genética , Cloroplastos/metabolismo , Ornitina Descarboxilase/genética , Ornitina Descarboxilase/metabolismo , Estresse Oxidativo/genética , Estresse Oxidativo/fisiologia , Proteínas de Plantas/genética , Nicotiana/genética , Nicotiana/metabolismo
4.
Plant Sci ; 258: 146-155, 2017 May.
Artigo em Inglês | MEDLINE | ID: mdl-28330558

RESUMO

Changes in the levels of polyamines are correlated with the activation or repression of developmental response pathways, but the role of polyamine transporters in the regulation of polyamine homeostasis and thus indirectly gene expression, has not been previously addressed. Here we show that the A. thaliana and rice transporters AtPUT5 and OsPUT1 were localized to the ER, while the AtPUT2, AtPUT3, and OsPUT3 were localized to the chloroplast by transient expression in N. benthamiana. A. thaliana plants that were transformed with OsPUT1 under the control the PUT5 promoter were delayed in flowering by 16days. In contrast, put5 mutants flowered four days earlier than WT plants. The delay of flowering was associated with significantly higher levels of spermidine and spermidine conjugates in the leaves prior to flowering. A similar delay in flowering was also noted in transgenic lines with constitutive expression of either OsPUT1 or OsPUT3. All three transgenic lines had larger rosette leaves, thicker flowering stems, and produced more siliques than wild type plants. In contrast, put5 plants had smaller leaves, thinner flowering stems, and produced fewer siliques. Constitutive expression of PUTs was also associated with an extreme delay in both plant senescence and maturation rate of siliques. These experiments provide the first genetic evidence of polyamine transport in the timing of flowering, and indicate the importance of polyamine transporters in the regulation of flowering and senescence pathways.


Assuntos
Flores/crescimento & desenvolvimento , Espermidina/fisiologia , Arabidopsis/crescimento & desenvolvimento , Arabidopsis/metabolismo , Arabidopsis/fisiologia , Transporte Biológico/fisiologia , Proteínas de Transporte/fisiologia , Cloroplastos/metabolismo , Cloroplastos/fisiologia , Flores/fisiologia , Regulação da Expressão Gênica de Plantas/fisiologia , Oryza/crescimento & desenvolvimento , Oryza/metabolismo , Oryza/fisiologia , Transcriptoma
5.
Interdiscip Sci ; 6(4): 279-84, 2014 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-25118648

RESUMO

The PDB file format, is a text format characterizing the three dimensional structures of macro molecules available in the Protein Data Bank (PDB). Determined protein structure are found in coalition with other molecules or ions such as nucleic acids, water, ions, Drug molecules and so on, which therefore can be described in the PDB format and have been deposited in PDB database. PDB is a machine generated file, it's not human readable format, to read this file we need any computational tool to understand it. The objective of our present study is to develop a free online software for retrieval, visualization and reading of annotation of a protein 3D structure which is available in PDB database. Main aim is to create PDB file in human readable format, i.e., the information in PDB file is converted in readable sentences. It displays all possible information from a PDB file including 3D structure of that file. Programming languages and scripting languages like Perl, CSS, Javascript, Ajax, and HTML have been used for the development of PDB Explorer. The PDB Explorer directly parses the PDB file, calling methods for parsed element secondary structure element, atoms, coordinates etc. PDB Explorer is freely available at http://www.pdbexplorer.eminentbio.com/home with no requirement of log-in.


Assuntos
Algoritmos , Bases de Dados de Proteínas , Modelos Moleculares , Anotação de Sequência Molecular , Proteínas/química , Software , Interface Usuário-Computador , Internet , Linguagens de Programação , Estrutura Secundária de Proteína
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