ABSTRACT
PURPOSE: To assess the coverage of information about early childhood caries (ECC) available on YouTube videos in three different languages, regarding technical characteristics of videos and interaction metrics. METHODS: Search strategies were developed in English, Spanish, and Portuguese to make a comprehensive collection of videos from YouTube, encompassing 60 samples for each language, regarding all video types. The videos were assessed by a thematic checklist regarding 17 items on ECC. Videos were dichotomized according to the median of the thematic score and the nature of their authorship (health and non-health authors) to compare groups. The statistical analysis was performed using the Statistical Package for Social Science (version 25.0), applying Spearman's rank correlation coefficient and Mann-Whitney U test. P < 0.05 values were considered significant. RESULTS: Among 120 videos meeting inclusion criteria, ECC aetiology and prevention information proved incomplete, with a median score of 5 (Q1-Q3 = 3-7). No correlation emerged between this score and other video characteristics. However, interaction metrics like views, likes, dislikes, and viewing rates displayed significant correlations. Health authors primarily created these videos, yet non-health author channels had more subscribers. Surprisingly, videos focused on the impact of regular sugary food and beverage consumption on ECC progression received the most attention. CONCLUSIONS: Videos that presented information about the aetiology and prevention of ECC invariably focused on partial aspects of the disease. This highlights the need for better-quality educational videos and the importance of dental professionals in guiding patients toward reliable sources of information.
Subject(s)
Dental Caries , Social Media , Humans , Child, Preschool , Dental Caries Susceptibility , Video Recording , Dental Caries/prevention & control , Parents , Reproducibility of ResultsABSTRACT
AIM: To assess the quality and readability of ECC-related Web information available in English, Spanish, and Brazilian Portuguese language. METHODS: This study assessed the quality and readability of information related to ECC in three different languages found on the most popular Internet search engines worldwide. Websites were retrieved from different search engines using specific strategies. DISCERN questionnaire, JAMA benchmark criteria, and language-based readability formulas were used by two independent investigators to evaluate the quality and readability of websites. Also, contents were categorised according to aetiology, prevention, and treatment of ECC. The statistical analysis was performed using Spearman's rank correlation coefficient, hierarchical clustering analysis by Ward's minimum variance method, and Mann-Whitney U test. P values < 0.05 were considered significant. CONCLUSION: ECC-related digital contents were considered simple, accessible and of poor quality, independently of their language and authorship. These findings indicate the importance of professional counseling to empower parents in selecting and consuming adequate information towards the improvement of children's oral health.
Subject(s)
Comprehension , Dental Caries , Child , Child, Preschool , Cross-Sectional Studies , Dental Caries/prevention & control , Dental Caries Susceptibility , Humans , Surveys and QuestionnairesABSTRACT
AIMS: Huntington's disease (HD) is a neurodegenerative disorder characterized by progressive abnormalities in cognitive function, mental state, and motor control. HD is characterized by a failure in brain energy metabolism. It has been proposed that monocarboxylates, such as lactate, support brain activity. During neuronal synaptic activity, ascorbic acid released from glial cells stimulates lactate and inhibits glucose transport. The aim of this study was to evaluate the expression and function of monocarboxylate transporters (MCTs) in two HD models. METHODS: Using immunofluorescence, qPCR, and Western blot analyses, we explored mRNA and protein levels of MCTs in the striatum of R6/2 animals and HdhQ7/111 cells. We also evaluated MCT function in HdhQ7/111 cells using radioactive tracers and the fluorescent lactate sensor Laconic. RESULTS: We found no significant differences in the mRNA or protein levels of neuronal MCTs. Functional analyses revealed that neuronal MCT2 had a high catalytic efficiency in HD cells. Ascorbic acid did not stimulate lactate uptake in HD cells. Ascorbic acid was also unable to inhibit glucose transport in HD cells because they exhibit decreased expression of the neuronal glucose transporter GLUT3. CONCLUSION: We demonstrate that stimulation of lactate uptake by ascorbic acid is a consequence of inhibiting glucose transport. Supporting this, lactate transport stimulation by ascorbic acid in HD cells was completely restored by overexpressing GLUT3. Therefore, alterations in GLUT3 expression could be responsible for inefficient use of lactate in HD neurons, contributing to the metabolic failure observed in HD.
Subject(s)
Glucose Transporter Type 3/metabolism , Huntington Disease/metabolism , Lactic Acid/metabolism , Animals , Cell Line , Corpus Striatum/metabolism , Disease Models, Animal , Female , Humans , Male , Mice, Transgenic , Monocarboxylic Acid Transporters/metabolism , Neurons/metabolism , RNA, Messenger/metabolism , RatsABSTRACT
Failure in energy metabolism and oxidative damage are associated with Huntington's disease (HD). Ascorbic acid released during synaptic activity inhibits use of neuronal glucose, favouring lactate uptake to sustain brain activity. Here, we observe a decreased expression of GLUT3 in STHdhQ111 cells (HD cells) and R6/2 mice (HD mice). Localisation of GLUT3 is decreased at the plasma membrane in HD cells affecting the modulation of glucose uptake by ascorbic acid. An ascorbic acid analogue without antioxidant activity is able to inhibit glucose uptake in HD cells. The impaired modulation of glucose uptake by ascorbic acid is directly related to ROS levels indicating that oxidative stress sequesters the ability of ascorbic acid to modulate glucose utilisation. Therefore, in HD, a decrease in GLUT3 localisation at the plasma membrane would contribute to an altered neuronal glucose uptake during resting periods while redox imbalance should contribute to metabolic failure during synaptic activity.
Subject(s)
Disease Models, Animal , Energy Metabolism/drug effects , Glucose Transporter Type 3/metabolism , Huntington Disease/pathology , Neurons/pathology , Oxidative Stress , Animals , Antioxidants/pharmacology , Ascorbic Acid/pharmacology , Blotting, Western , Cell Membrane/metabolism , Cells, Cultured , Female , Fluorescent Antibody Technique , Glucose/metabolism , Glucose Transporter Type 3/genetics , Huntington Disease/genetics , Huntington Disease/metabolism , Male , Mice , Neurons/drug effects , Neurons/metabolism , Oxidation-Reduction , RNA, Messenger/genetics , Rats , Rats, Wistar , Real-Time Polymerase Chain Reaction , Reverse Transcriptase Polymerase Chain ReactionABSTRACT
Huntington's disease has been associated with a failure in energy metabolism and oxidative damage. Ascorbic acid is a powerful antioxidant highly concentrated in the brain where it acts as a messenger, modulating neuronal metabolism. Using an electrophysiological approach in R6/2 HD slices, we observe an abnormal ascorbic acid flux from astrocytes to neurons, which is responsible for alterations in neuronal metabolic substrate preferences. Here using striatal neurons derived from knock-in mice expressing mutant huntingtin (STHdhQ cells), we study ascorbic acid transport. When extracellular ascorbic acid concentration increases, as occurs during synaptic activity, ascorbic acid transporter 2 (SVCT2) translocates to the plasma membrane, ensuring optimal ascorbic acid uptake for neurons. In contrast, SVCT2 from cells that mimic HD symptoms (dubbed HD cells) fails to reach the plasma membrane under the same conditions. We reason that an early impairment of ascorbic acid uptake in HD neurons could lead to early metabolic failure promoting neuronal death.
Subject(s)
Ascorbic Acid/metabolism , Energy Metabolism , Huntington Disease/metabolism , Huntington Disease/pathology , Animals , Astrocytes/metabolism , Astrocytes/pathology , Cell Line , Cell Membrane/genetics , Cell Membrane/metabolism , Disease Models, Animal , Female , Huntingtin Protein , Huntington Disease/genetics , Male , Mice , Mice, Transgenic , Nerve Tissue Proteins/genetics , Nerve Tissue Proteins/metabolism , Neuroglia/metabolism , Neuroglia/pathology , Neurons/metabolism , Neurons/pathology , Protein Transport , Rats, Wistar , Sodium-Coupled Vitamin C Transporters/genetics , Sodium-Coupled Vitamin C Transporters/metabolismABSTRACT
Glycogen is the main source of glucose for many biological events. However, this molecule may have other functions, including those that have deleterious effects on cells. The rate-limiting enzyme in glycogen synthesis is glycogen synthase (GS). It is encoded by two genes, GYS1, expressed in muscle (muscle glycogen synthase, MGS) and other tissues, and GYS2, primarily expressed in liver (liver glycogen synthase, LGS). Expression of GS and its activity have been widely studied in many tissues. To date, it is not clear which GS isoform is responsible for glycogen synthesis and the role of glycogen in testis. Using RT-PCR, Western blot and immunofluorescence, we have detected expression of MGS but not LGS in mice testis during development. We have also evaluated GS activity and glycogen storage at different days after birth and we show that both GS activity and levels of glycogen are higher during the first days of development. Using RT-PCR, we have also shown that malin and laforin are expressed in testis, key enzymes for regulation of GS activity. These proteins form an active complex that regulates MGS by poly-ubiquitination in both Sertoli cell and male germ cell lines. In addition, PTG overexpression in male germ cell line triggered apoptosis by caspase3 activation, proposing a proapoptotic role of glycogen in testis. These findings suggest that GS activity and glycogen synthesis in testis could be regulated and a disruption of this process may be responsible for the apoptosis and degeneration of seminiferous tubules and possible cause of infertility.
Subject(s)
Germ Cells/cytology , Germ Cells/metabolism , Glycogen Synthase/metabolism , Glycogen/metabolism , Protein Isoforms/metabolism , Testis/cytology , Testis/metabolism , Animals , Apoptosis/genetics , Apoptosis/physiology , Glycogen Synthase/genetics , Immunoblotting , Male , Mice , Mice, Transgenic , Protein Isoforms/genetics , Reverse Transcriptase Polymerase Chain Reaction , Seminiferous Tubules/cytology , Seminiferous Tubules/metabolism , Testis/enzymologyABSTRACT
Intracellular ascorbic acid is able to modulate neuronal glucose utilization between resting and activity periods. We have previously demonstrated that intracellular ascorbic acid inhibits deoxyglucose transport in primary cultures of cortical and hippocampal neurons and in HEK293 cells. The same effect was not seen in astrocytes. Since this observation was valid only for cells expressing glucose transporter 3 (GLUT3), we evaluated the importance of this transporter on the inhibitory effect of ascorbic acid on glucose transport. Intracellular ascorbic acid was able to inhibit (3)H-deoxyglucose transport only in astrocytes expressing GLUT3-EGFP. In C6 glioma cells and primary cultures of cortical neurons, which natively express GLUT3, the same inhibitory effect on (3)H-deoxyglucose transport and fluorescent hexose 2-[N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino]-2-deoxyglucose (2-NBDG) was observed. Finally, knocking down the native expression of GLUT3 in primary cultured neurons and C6 cells using shRNA was sufficient to abolish the ascorbic acid-dependent inhibitory effect on uptake of glucose analogs. Uptake assays using real-time confocal microscopy demonstrated that ascorbic acid effect abrogation on 2-NBDG uptake in cultured neurons. Therefore, ascorbic acid would seem to function as a metabolic switch inhibiting glucose transport in neurons under glutamatergic synaptic activity through direct or indirect inhibition of GLUT3.
