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1.
Clin Chim Acta ; 455: 87-92, 2016 Apr 01.
Artigo em Inglês | MEDLINE | ID: mdl-26826396

RESUMO

BACKGROUND: TGF-ß1 regulates bone metabolism and mediates bone turnover during postmenopause. Sclerostin negatively regulates Wnt signaling pathway and also has an important role in postmenopausal bone loss. Little is known about the relationship between serum TGF-ß1 and sclerostin during menopause. METHODS: We compared serum levels of TGF-ß1 and sclerostin in pre- and postmenopausal women and assessed the potential correlations of these levels with each other and with serum levels of bone turnover markers and bone mineral density. RESULTS: A total of 176 women (58 premenopausal, 62 early postmenopausal, and 56 late postmenopausal) were included in this study. Serum TGF-ß1 level was significantly higher in early postmenopausal women compared with premenopausal (32.0±7.19 vs. 26.55±6.67 ng/ml, p=0.01) and late postmenopausal (32.0±7.19 vs. 28.65±7.70 pg/ml, p=0.031) women, and no significant differences in serum sclerostin levels were observed among the 3 groups. There was a significant negative correlation between TGF-ß1 and sclerostin in early postmenopausal women, but not in other groups of women. Based on multiple regression analysis, only TGF-ß1 (ß=-0.362; p=0.007) was an independent predictor of sclerostin during early postmenopause. CONCLUSIONS: Our findings suggest that serum TGF-ß1 level increases during postmenopause and declines in old age. Sclerostin production is inhibited by TGF-ß1 during early postmenopause.


Assuntos
Proteínas Morfogenéticas Ósseas/sangue , Pós-Menopausa , Fator de Crescimento Transformador beta1/sangue , Proteínas Adaptadoras de Transdução de Sinal , Estudos de Coortes , Estudos Transversais , Feminino , Marcadores Genéticos , Humanos , Pessoa de Meia-Idade
2.
Anal Chem ; 87(17): 9078-83, 2015 Sep 01.
Artigo em Inglês | MEDLINE | ID: mdl-26235567

RESUMO

While serology represents the forefront technique for cancer diagnosis, current clinical methods for the detection of serum biomarkers have flaws in terms of the need of complicated manipulations, long analytical time, and high cost. Here, we develop a supramolecular glycoprobe for the quick serological detection of a cancer biomarker. The probe formed by agglutination between self-assembled glyco-gold nanoparticles and a lectin shows subtle optical variations upon the competitive recognition of a glycoprotein biomarker secreted by cancer cells, tumor-bearing mice, as well as clinical cancer patients, with no response to a series of controls including the serum of hepatitis patients. This research provides an insight into the development of effective tools for serological diagnosis of cancer.


Assuntos
Biomarcadores Tumorais/sangue , Glicoproteínas/química , Ouro/química , Neoplasias Hepáticas/sangue , Nanopartículas Metálicas/química , Animais , Feminino , Células HeLa , Células Hep G2 , Humanos , Neoplasias Hepáticas/diagnóstico , Neoplasias Hepáticas Experimentais/sangue , Neoplasias Hepáticas Experimentais/diagnóstico , Camundongos , Camundongos Endogâmicos BALB C , Camundongos Nus , Estrutura Molecular , Tamanho da Partícula , Propriedades de Superfície , Células Tumorais Cultivadas
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