Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 5 de 5
Filtrar
Mais filtros

Base de dados
Tipo de documento
País de afiliação
Intervalo de ano de publicação
1.
Pharm Biol ; 60(1): 1106-1115, 2022 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-35639355

RESUMO

CONTEXT: Obesity, one of the major public health problems worldwide, has attracted increasing attention. Ginsenoside Rb1 is the most abundant active component of Panax ginseng C.A.Mey (Araliaceae) and is reported to have beneficial effects on obesity and diabetes. However, the mechanisms by which Rb1 regulates obesity remain to be explored. OBJECTIVE: This paper intends to further explore the mechanism of Rb1 in regulating obesity. MATERIALS AND METHODS: The C57BL/6 obese mice were divided into two groups: the control (CTR) and Rb1. The CTR group [intraperitoneally (ip) administered with saline] and the Rb1 group (ip administered with Rb1, 40 mg/kg/d) were treated daily for four weeks. In vitro, Rb1 (0, 10, 20, 40 µM) was added to differentiated C2C12 cells and Rb1 (0, 20, 40 µM) was added to 3T3-L1 cells. After 24 h, total RNA and protein from C2C12 cells and 3T3-L1 cells were used to detect myostatin (MSTN) and fibronectin type III domain-containing 5 (FNDC5) expression. RESULTS: Rb1 reduced the body weight and adipocyte size. Improved glucose tolerance and increased basic metabolic activity were also found in Rb1 treated mice. MSTN was downregulated in differentiated C2C12 cells, 3T3-L1 cells and adipose tissues upon Rb1 treatment. FNDC5 was increased after Rb1 treatment. However, MSTN overexpression attenuated Rb1-mediated decrease accumulation of lipid droplets in differentiated 3T3-L1 adipocytes. DISCUSSION & CONCLUSIONS: Rb1 may ameliorate obesity in part through the MSTN/FNDC5 signalling pathway. Our results showed that Rb1 can be used as an effective drug in the treatment of human obesity.


Assuntos
Ginsenosídeos , Miostatina , Obesidade , Panax , Animais , Fibronectinas , Ginsenosídeos/farmacologia , Camundongos , Camundongos Endogâmicos C57BL , Miostatina/genética , Obesidade/tratamento farmacológico , Obesidade/metabolismo
2.
J Sci Food Agric ; 99(3): 1405-1412, 2019 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-30120787

RESUMO

BACKGROUND: Macamides, the main active components contained in maca, have attracted increasing attention due to their various bioactivities. In this study, crude macamide extract (CME) and purified macamide extract (PME) were prepared by enzyme-assisted extraction and macroporous resin separation, and the anti-fatigue effects of CME and PME were evaluated in a forced swimming model. RESULTS: The composition analysis results revealed that both CME and PME mainly contain eight kinds of macamide. Based on the results of a weight-loaded forced swimming test, compared with a control group, CME and and PME groups could prolong exhaustive swimming time, increase levels of liver glycogen (LG) and muscle glycogen (MG), accelerate fatty acid oxidation in serum to provide energy, eliminate the accumulation of blood lactic acid (BLA) and blood urea nitrogen (BUN), and decrease the serum biomarkers for muscle damage, such as lactate dehydrogenase (LDH) and creatine kinase (CK). Histological analysis also indicated that CME and PME attenuated damage to skeletal muscle and the myocardium in mice during exercise. CONCLUSION: Two macamide extracts have a beneficial effect on relieving physical fatigue by attenuating the damage of skeletal muscle and myocardium during exercise, and a better effect was observed in the PME group. © 2018 Society of Chemical Industry.


Assuntos
Amidas/administração & dosagem , Fadiga/tratamento farmacológico , Lepidium/química , Fadiga Muscular/efeitos dos fármacos , Extratos Vegetais/administração & dosagem , Amidas/química , Amidas/isolamento & purificação , Animais , Nitrogênio da Ureia Sanguínea , Peso Corporal/efeitos dos fármacos , Creatina Quinase/metabolismo , Fadiga/metabolismo , Fadiga/fisiopatologia , Glicogênio/metabolismo , Humanos , L-Lactato Desidrogenase/metabolismo , Masculino , Camundongos , Músculo Esquelético/efeitos dos fármacos , Músculo Esquelético/enzimologia , Músculo Esquelético/metabolismo , Extratos Vegetais/química , Extratos Vegetais/isolamento & purificação , Natação
3.
J Proteomics ; 130: 211-20, 2016 Jan 01.
Artigo em Inglês | MEDLINE | ID: mdl-26435418

RESUMO

Hypoxic status alters the energy metabolism and induces cell injury in cardiomyocytes, and it further triggers the occurrence and development of cardiovascular diseases. Our previous studies have shown that salidroside (SAL) exhibits anti-hypoxic activity. However, the mechanisms remain obscure. In the present study, we successfully screened 92 different expression proteins in CoCl2-induced hypoxic conditions, 106 different expression proteins in the SAL-mediated anti-hypoxic group were compared with the hypoxic group using quantitative proteomics strategy, respectively. We confirmed that SAL showed a positive protective function involving the acetyl-CoA metabolic, tricarboxylic acid (TCA) cycle using bioinformatics analysis. We also demonstrated that SAL plays a critical role in restoring the TCA cycle and in protecting cardiomyocytes from oxidative injury via up-regulation expressions of PDHE1-B, ACO2, SUCLG1, SUCLG2 and down-regulation of MDH2. SAL also inhibited H9c2 cell apoptosis by inhibiting the activation of pro-apoptotic molecules caspase 3 and caspase 9 as well as activation of the anti-apoptotic molecular Bcl-2. Additionally, SAL also improved mitochondrial membrane potential (ΔΨm), reduced reactive oxygen species (ROS) and intercellular Ca(2+) concentration ([Ca(2+)]i) accumulation and inhibited the excessive consumption of ATP in H9c2 cells.


Assuntos
Cobalto/química , Glucosídeos/química , Miócitos Cardíacos/metabolismo , Fenóis/química , Proteômica/métodos , Ácidos Tricarboxílicos/química , Trifosfato de Adenosina/química , Apoptose , Cálcio/química , Caspase 3/metabolismo , Caspase 9/metabolismo , Linhagem Celular , Cromatografia Líquida , Ciclo do Ácido Cítrico , Biologia Computacional , Hipóxia/patologia , Potenciais da Membrana , Oxigênio/química , Extratos Vegetais/química , Proteoma , Proteínas Proto-Oncogênicas c-bcl-2/metabolismo , Espécies Reativas de Oxigênio/metabolismo , Rhodiola/química , Espectrometria de Massas em Tandem
4.
PLoS One ; 7(4): e34894, 2012.
Artigo em Inglês | MEDLINE | ID: mdl-22485190

RESUMO

The structural homeostasis of the cochlear hair cell membrane is critical for all aspects of sensory transduction, but the regulation of its maintenance is not well understood. In this report, we analyzed the cochlear hair cells of mice with specific deletion of myosin light chain kinase (MLCK) in inner hair cells. MLCK-deficient mice showed impaired hearing, with a 5- to 14-dB rise in the auditory brainstem response (ABR) thresholds to clicks and tones of different frequencies and a significant decrease in the amplitude of the ABR waves. The mutant inner hair cells produced several ball-like structures around the hair bundles in vivo, indicating impaired membrane stability. Inner hair cells isolated from the knockout mice consistently displayed less resistance to hypoosmotic solution and less membrane F-actin. Myosin light-chain phosphorylation was also reduced in the mutated inner hair cells. Our results suggest that MLCK is necessary for maintaining the membrane stability of inner hair cells.


Assuntos
Membrana Celular/enzimologia , Células Ciliadas Auditivas Internas/enzimologia , Homeostase , Quinase de Cadeia Leve de Miosina/fisiologia , Citoesqueleto de Actina/metabolismo , Actinas/metabolismo , Animais , Membrana Celular/metabolismo , Epitélio/enzimologia , Epitélio/metabolismo , Potenciais Evocados Auditivos do Tronco Encefálico , Expressão Gênica , Células Ciliadas Auditivas Internas/metabolismo , Células Ciliadas Auditivas Internas/ultraestrutura , Camundongos , Camundongos da Linhagem 129 , Camundongos Endogâmicos C57BL , Camundongos Knockout , Cadeias Leves de Miosina/metabolismo , Miosina VIIa , Quinase de Cadeia Leve de Miosina/deficiência , Quinase de Cadeia Leve de Miosina/genética , Miosinas/metabolismo , Órgão Espiral/citologia , Pressão Osmótica , Fosforilação , Processamento de Proteína Pós-Traducional , Deleção de Sequência , ATPase Trocadora de Sódio-Potássio/genética , ATPase Trocadora de Sódio-Potássio/metabolismo
5.
Zhongguo Yi Xue Ke Xue Yuan Xue Bao ; 24(2): 149-55, 2002 Apr.
Artigo em Chinês | MEDLINE | ID: mdl-12905792

RESUMO

OBJECTIVE: To acquire cDNA sequence of lecithin-cholesterol acyltransferase (LCAT) from tree shrew and analyze the sequence structure. METHODS: The first strand cDNA was acquired by reverse transcription using mRNA from tree shrew liver as template. By the method of SMART RACE PCR, tree shrew LCAT cDNA was acquired and deduced its amino acids sequence. The sequence and structure of tree shrew LCAT cDNA and amino acid were analyzed and predicted by the molecular software. RESULTS: Tree shrew LCAT cDNA is composed of 1,340 bp, including 2 bp 5' untranslated region (5' UTR), 1,320 bp open reading frame (ORF) which encodes protein precursor of 440 amino acids (24 amino acids signal peptide and 416 amino acids mature peptide), and 18 bp 3' untranslated region (3'UTR). The stop codon is TAA and there is a poly (A) signal sequence AATAAA and a 25 bp poly (A) tail. Tree shrew LCAT cDNA sequence has been accepted by GenBank as a new gene, accession number AF272861 and its homology with human and baboon was 90% and 89%, respectively. CONCLUSION: The sequence of LCAT cDNA in tree shrew has high identity with that of human and other experimental animal species.


Assuntos
Fosfatidilcolina-Esterol O-Aciltransferase/química , Fosfatidilcolina-Esterol O-Aciltransferase/genética , Sequência de Aminoácidos , Animais , Sequência de Bases , DNA Complementar/genética , Fígado/enzimologia , Dados de Sequência Molecular , Fases de Leitura Aberta/genética , Análise de Sequência de Proteína , Tupaiidae
SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA