Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 5 de 5
Filter
Add more filters










Language
Publication year range
1.
Biol Res ; 57(1): 22, 2024 May 04.
Article in English | MEDLINE | ID: mdl-38704609

ABSTRACT

BACKGROUND: Chromatin dynamics is deeply involved in processes that require access to DNA, such as transcriptional regulation. Among the factors involved in chromatin dynamics at gene regulatory regions are general regulatory factors (GRFs). These factors contribute to establishment and maintenance of nucleosome-depleted regions (NDRs). These regions are populated by nucleosomes through histone deposition and nucleosome sliding, the latter catalyzed by a number of ATP-dependent chromatin remodeling complexes, including ISW1a. It has been observed that GRFs can act as barriers against nucleosome sliding towards NDRs. However, the relative ability of the different GRFs to hinder sliding activity is currently unknown. RESULTS: Considering this, we performed a comparative analysis for the main GRFs, with focus in their ability to modulate nucleosome sliding mediated by ISW1a. Among the GRFs tested in nucleosome remodeling assays, Rap1 was the only factor displaying the ability to hinder the activity of ISW1a. This effect requires location of the Rap1 cognate sequence on linker that becomes entry DNA in the nucleosome remodeling process. In addition, Rap1 was able to hinder nucleosome assembly in octamer transfer assays. Concurrently, Rap1 displayed the highest affinity for and longest dwell time from its target sequence, compared to the other GRFs tested. Consistently, through bioinformatics analyses of publicly available genome-wide data, we found that nucleosome occupancy and histone deposition in vivo are inversely correlated with the affinity of Rap1 for its target sequences in the genome. CONCLUSIONS: Our findings point to DNA binding affinity, residence time and location at particular translational positions relative to the nucleosome core as the key features of GRFs underlying their roles played in nucleosome sliding and assembly.


Subject(s)
Chromatin Assembly and Disassembly , DNA-Binding Proteins , Nucleosomes , Nucleosomes/metabolism , Nucleosomes/genetics , Chromatin Assembly and Disassembly/physiology , Adenosine Triphosphatases/metabolism , Adenosine Triphosphatases/genetics , Saccharomyces cerevisiae Proteins/metabolism , Saccharomyces cerevisiae Proteins/genetics , Transcription Factors/metabolism , Transcription Factors/genetics , Saccharomyces cerevisiae/genetics , Saccharomyces cerevisiae/metabolism , Histones/metabolism
2.
Molecules ; 28(17)2023 Aug 31.
Article in English | MEDLINE | ID: mdl-37687197

ABSTRACT

The catalytic oxidation of phenethoxybenzene as a lignin model compound with a ß-O-4 bond was conducted using the Keggin-type polyoxometalate nanocatalyst (TBA)5[PMo10V2O40]. The optimization of the process's operational conditions was carried out using response surface methodology. The statistically significant variables in the process were determined using a fractional factorial design. Based on this selection, a central circumscribed composite experimental design was used to maximize the phenethoxybenzene conversion, varying temperature, reaction time, and catalyst load. The optimal conditions that maximized the phenethoxybenzene conversion were 137 °C, 3.5 h, and 200 mg of catalyst. In addition, under the optimized conditions, the Kraft lignin catalytic depolymerization was carried out to validate the effectiveness of the process. The depolymerization degree was assessed by gel permeation chromatography from which a significant decrease in the molar mass distribution Mw from 7.34 kDa to 1.97 kDa and a reduction in the polydispersity index PDI from 6 to 3 were observed. Furthermore, the successful cleavage of the ß-O-4 bond in the Kraft lignin was verified by gas chromatography-mass spectrometry analysis of the reaction products. These results offer a sustainable alternative to efficiently converting lignin into valuable products.

3.
Nutr Hosp ; 39(6): 1389-1396, 2022 Dec 20.
Article in English | MEDLINE | ID: mdl-36327126

ABSTRACT

Introduction: Irisin is an adipomyokine involved in white adipose tissue browning, therefore, could be a key protein in metabolic health. However, exercise effects on irisin in subjects with overweight and/or obesity are conflicting. Therefore, this systematic review aims to search and analyse the literature available on this topic. From three databases: PubMed, ScienceDirect, and Medline, clinical studies published between 2010 and 2021 were considered. From 134 found, 14 studies were included. Only six reported plasma increases after exercise (~1.2 to 3-fold from pre-exercise levels). In addition, only 1 reported significant increases in skeletal muscle irisin mRNA levels (~2-fold). Also, irisin was measured from subcutaneous adipose tissue and saliva, where a ~2-fold increase in its protein levels was found in the latter. Exercise seems to increase the circulatory concentrations of irisin in subjects with overweight or obesity. However, this response is highly variable, therefore, a more integrative approach is urgently needed.


Introducción: La irisina es una adipomioquina relacionada a la transformación del tejido adiposo blanco a marrón, por tanto, podría ser una proteína clave para la salud metabólica. Sin embargo, los efectos del ejercicio sobre la irisina en personas con sobrepeso u obesidad son poco claros. Por lo anterior, esta revisión sistemática apunta a buscar y analizar la literatura disponible en este tema. Desde tres bases de datos: PubMed, ScienceDirect y Medline se buscaron estudios clínicos publicados entre el 2010 y 2021. De 134 estudios encontrados, 14 fueron incluidos. Solo 6 reportaron incrementos plasmáticos de irisina después del ejercicio (~1.2 a 3-veces respecto a niveles preejercicio). Además, solo 1 estudio describió incrementos significativos en el ARNm de irisina en el músculo esquelético (~2 veces sobre niveles preejercicio). La irisina también se medió desde tejido adiposo subcutáneo y saliva, encontrándose una elevación de (~2 veces sobre niveles preejercicio) en esta última. El ejercicio físico incrementaría las concentraciones circulatorias de irisina en personas con sobrepeso u obesidad. Sin embargo, esta respuesta es muy variable, por lo que se requiere una mirada más integrativa a la hora de estudiar este fenómeno.


Subject(s)
Exercise Therapy , Exercise , Fibronectins , Overweight , Humans , Exercise/physiology , Muscle, Skeletal/metabolism , Obesity/therapy , Overweight/metabolism
4.
Nutr. hosp ; 39(6): 1389-1396, nov.-dic. 2022. ilus, tab
Article in English | IBECS | ID: ibc-214848

ABSTRACT

Irisin is an adipomyokine involved in white adipose tissue browning, therefore, could be a key protein in metabolic health. However, exercise effects on irisin in subjects with overweight and/or obesity are conflicting. Therefore, this systematic review aims to search and analyse the literature available on this topic. From three databases: PubMed, ScienceDirect, and Medline, clinical studies published between 2010 and 2021 were considered. From 134 found, 14 studies were included. Only six reported plasma increases after exercise (~1.2 to 3-fold from pre-exercise levels). In addition, only 1 reported significant increases in skeletal muscle irisin mRNA levels (~2-fold). Also, irisin was measured from subcutaneous adipose tissue and saliva, where a ~2-fold increase in its protein levels was found in the latter. Exercise seems to increase the circulatory concentrations of irisin in subjects with overweight or obesity. However, this response is highly variable, therefore, a more integrative approach is urgently needed. (AU)


La irisina es una adipomioquina relacionada a la transformación del tejido adiposo blanco a marrón, por tanto, podría ser una proteína clave para la salud metabólica. Sin embargo, los efectos del ejercicio sobre la irisina en personas con sobrepeso u obesidad son poco claros. Por lo anterior, esta revisión sistemática apunta a buscar y analizar la literatura disponible en este tema. Desde tres bases de datos: PubMed, ScienceDirect y Medline se buscaron estudios clínicos publicados entre el 2010 y 2021. De 134 estudios encontrados, 14 fueron incluidos. Solo 6 reportaron incrementos plasmáticos de irisina después del ejercicio (~1.2 a 3-veces respecto a niveles preejercicio). Además, solo 1 estudio describió incrementos significativos en el ARNm de irisina en el músculo esquelético (~2 veces sobre niveles preejercicio). La irisina también se medió desde tejido adiposo subcutáneo y saliva, encontrándose una elevación de (~2 veces sobre niveles preejercicio) en esta última. El ejercicio físico incrementaría las concentraciones circulatorias de irisina en personas con sobrepeso u obesidad. Sin embargo, esta respuesta es muy variable, por lo que se requiere una mirada más integrativa a la hora de estudiar este fenómeno. (AU)


Subject(s)
Humans , Exercise Therapy , Overweight/metabolism , Obesity/therapy , Fibronectins , Muscle, Skeletal/metabolism
5.
Front Pharmacol ; 11: 900, 2020.
Article in English | MEDLINE | ID: mdl-32636743

ABSTRACT

The neurulation process is regulated by a large amount of genetic and environmental factors that determine the establishment, folding, and fusion of the neural plate to form the neural tube, which develops into the main structure of the central nervous system. A recently described factor involved in this process is glutamate. Through NMDA ionotropic receptor, glutamate modifies intracellular Ca2+ dynamics allowing the oriented cell migration and proliferation, essentials processes in neurulation. Glutamate synthesis depends on the mitochondrial enzyme known as glutaminase 1 (GLS1) that is widely expressed in brain and kidney. The participation of GLS 1 in prenatal neurogenic processes and in the adult brain has been experimentally established, however, its participation in early stages of embryonic development has not been described. The present investigation describes for the first time the presence and functionality of GLS1 in Xenopus laevis embryos during neurulation. Although protein expression levels remains constant, the catalytic activity of GLS1 increases significantly (~66%) between early (stage 12) and middle to late (stages 14-19) neurulation process. Additionally, the use of 6-diazo-5-oxo-L-norleucine (L-DON, competitive inhibitor of glutamine-depend enzymes), reduced significantly the GLS1 specific activity during neurulation (~36%) and induce the occurrence of neural tube defects involving its possible participation in the neural tube closure in Xenopus laevis embryos.

SELECTION OF CITATIONS
SEARCH DETAIL
...