Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 4 de 4
Filtrar
Mais filtros










Base de dados
Intervalo de ano de publicação
1.
Med Eng Phys ; 98: 50-56, 2021 12.
Artigo em Inglês | MEDLINE | ID: mdl-34848038

RESUMO

Medical professionals have complained of extreme discomfort and fatigue from continuous wearing of N95 respirators (N95) overlaid with surgical masks (SM) and face shields (FS) during COVID-19 pandemic. However, there are no reports on the effect of face coverings on transdermal CO2 (TrCO2) levels (a measure of blood CO2) during moderate activity. In this study, real-time monitoring of TrCO2, heart rate and skin surface temperature was conducted for six subjects aged 20-59 years with and without wearing personal protective equipment (PPE). We initially studied the effect of wearing PPE (N95+SM+FS) at rest. Then, the effect of moderate stepping/walking activity (120 steps per minute for 60 min) while wearing PPE was evaluated. In addition, we investigated the effect of exercising intensity with different masks. We observed a significant difference (p < 0.0001) in TrCO2 levels between without and with PPE during moderate exercise, but not while resting. TrCO2 levels were correlated to exercise intensity independently with masking condition and breathability of masks. For the first time, we present data showing that a properly fitting N95 worn along with SM and FS consistently leads to elevated TrCO2 under moderate exertion, which could contribute to fatigue over long-term use.


Assuntos
COVID-19 , Dióxido de Carbono , Humanos , Máscaras , Pandemias , SARS-CoV-2
2.
Front Bioeng Biotechnol ; 9: 672594, 2021.
Artigo em Inglês | MEDLINE | ID: mdl-34113606

RESUMO

The prevalence of the two most common neurodegenerative diseases, Parkinson's disease (PD) and Alzheimer's Disease (AD), are expected to rise alongside the progressive aging of society. Both PD and AD are classified as proteinopathies with misfolded proteins α-synuclein, amyloid-ß, and tau. Emerging evidence suggests that these misfolded aggregates are prion-like proteins that induce pathological cell-to-cell spreading, which is a major driver in pathogenesis. Additional factors that can further affect pathology spreading include oxidative stress, mitochondrial damage, inflammation, and cell death. Nanomaterials present advantages over traditional chemical or biological therapeutic approaches at targeting these specific mechanisms. They can have intrinsic properties that lead to a decrease in oxidative stress or an ability to bind and disaggregate fibrils. Additionally, nanomaterials enhance transportation across the blood-brain barrier, are easily functionalized, increase drug half-lives, protect cargo from immune detection, and provide a physical structure that can support cell growth. This review highlights emergent nanomaterials with these advantages that target oxidative stress, the fibrillization process, inflammation, and aid in regenerative medicine for both PD and AD.

3.
Science ; 353(6307)2016 09 30.
Artigo em Inglês | MEDLINE | ID: mdl-27708076

RESUMO

Emerging evidence indicates that the pathogenesis of Parkinson's disease (PD) may be due to cell-to-cell transmission of misfolded preformed fibrils (PFF) of α-synuclein (α-syn). The mechanism by which α-syn PFF spreads from neuron to neuron is not known. Here, we show that LAG3 (lymphocyte-activation gene 3) binds α-syn PFF with high affinity (dissociation constant = 77 nanomolar), whereas the α-syn monomer exhibited minimal binding. α-Syn-biotin PFF binding to LAG3 initiated α-syn PFF endocytosis, transmission, and toxicity. Lack of LAG3 substantially delayed α-syn PFF-induced loss of dopamine neurons, as well as biochemical and behavioral deficits in vivo. The identification of LAG3 as a receptor that binds α-syn PFF provides a target for developing therapeutics designed to slow the progression of PD and related α-synucleinopathies.


Assuntos
Antígenos CD/metabolismo , Doença de Parkinson/metabolismo , alfa-Sinucleína/metabolismo , Animais , Neurônios Dopaminérgicos/metabolismo , Endocitose , Humanos , Camundongos , Camundongos Transgênicos , Ligação Proteica , Transporte Proteico , alfa-Sinucleína/genética , Proteína do Gene 3 de Ativação de Linfócitos
4.
Microb Pathog ; 52(3): 149-56, 2012 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-22197999

RESUMO

Recent work has demonstrated that the spectrin cytoskeleton is a host cell target, exploited during intestinal bacterial disease. Here we show that the highly virulent intestinal pathogen enterohaemorrhagic Escherichia coli (EHEC) is also reliant upon the spectrin cytoskeleton during key pathogenic events. Immunofluorescent microscopy demonstrated that the core components of the spectrin cytoskeleton (spectrin, adducin, and protein 4.1 [p4.1]) are recruited to sites of EHEC attachment and localized at pedestal structures along with the EHEC pedestal specific proteins IRSp53 and IRTKS. Further studies involving siRNA-mediated knockdowns of spectrin, adducin, or p4.1 revealed that those proteins are needed for efficient docking of EHEC to host cells, are involved in recruiting IRSp53 to the pedestal and are necessary for pedestal formation. These findings identify the spectrin cytoskeleton as a major host cell cytoskeletal network involved in critical EHEC pathogenic events.


Assuntos
Aderência Bacteriana , Proteínas de Ligação a Calmodulina/metabolismo , Escherichia coli Êntero-Hemorrágica/patogenicidade , Interações Hospedeiro-Patógeno , Proteínas de Membrana/metabolismo , Espectrina/metabolismo , Proteínas de Ligação a Calmodulina/antagonistas & inibidores , Inativação Gênica , Células HeLa , Humanos , Proteínas de Membrana/antagonistas & inibidores , Proteínas dos Microfilamentos/metabolismo , Proteínas do Tecido Nervoso/metabolismo , Ligação Proteica , RNA Interferente Pequeno/genética , RNA Interferente Pequeno/metabolismo , Espectrina/antagonistas & inibidores
SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA
...