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Ma X.-X.,Nankai University | Wang C.-C.,Nankai University | Cai W.-S.,Nankai University | Shao X.-G.,Nankai University | And 2 more authors.
Chinese Chemical Letters | Year: 2016

Urinary albumin is an important diagnostic and prognostic marker for cardiorenal disease. Recent studies have shown that elevation of albumin excretion even in normal concentration range is associated with increased cardiorenal risk. Therefore, accurate measurement of urinary albumin in normal concentration range is necessary for clinical diagnosis. In this work, thiourea-functionalized silica nanoparticles are prepared and used for preconcentration of albumin in urine. The adsorbent with the analyte was then used for near-infrared diffuse reflectance spectroscopy measurement directly and partial least squares model was established for quantitative prediction. Forty samples were taken as calibration set for establishing PLS model and 17 samples were used for validation of the method. The correlation coefficient and the root mean squared error of cross validation is 0.9986 and 0.43, respectively. Residual predictive deviation value of the model is as high as 18.8. The recoveries of the 17 validation samples in the concentration range of 3.39-24.39. mg/L are between 95.9%-113.1%. Therefore, the method may provide a candidate method to quantify albumin excretion in urine. © 2016 Xue-Guang Shao. Source

Liu Y.,Nankai University | Cai W.,Nankai University | Shao X.,Nankai University | Shao X.,Tianjin Key Laboratory of Biosensing and Molecular Recognition | Shao X.,State Key Laboratory of Medicinal Chemical Biology
Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy | Year: 2016

Calibration transfer is essential for practical applications of near infrared (NIR) spectroscopy because the measurements of the spectra may be performed on different instruments and the difference between the instruments must be corrected. For most of calibration transfer methods, standard samples are necessary to construct the transfer model using the spectra of the samples measured on two instruments, named as master and slave instrument, respectively. In this work, a method named as linear model correction (LMC) is proposed for calibration transfer without standard samples. The method is based on the fact that, for the samples with similar physical and chemical properties, the spectra measured on different instruments are linearly correlated. The fact makes the coefficients of the linear models constructed by the spectra measured on different instruments are similar in profile. Therefore, by using the constrained optimization method, the coefficients of the master model can be transferred into that of the slave model with a few spectra measured on slave instrument. Two NIR datasets of corn and plant leaf samples measured with different instruments are used to test the performance of the method. The results show that, for both the datasets, the spectra can be correctly predicted using the transferred partial least squares (PLS) models. Because standard samples are not necessary in the method, it may be more useful in practical uses. © 2016 Elsevier B.V. Source

Yang X.,Nankai University | Xia Y.,Nankai University | Xia Y.,Key Laboratory of Biosensing and Molecular Recognition | Xia Y.,State Key Laboratory of Medicinal Chemical Biology
Microchimica Acta | Year: 2016

Mass spectrometry (MS) is the most powerful tool in phosphoproteomics research. However, phosphopeptides usually are present in low concentrations and their preconcentration therefore is highly desired. We describe a two-step method for the synthesis of a metal organic framework of the type MIL-101(Cr) that is modified with urea (then designated as MIL-101(Cr)-UR2). It possesses large surface area, good solvent stability and high affinity for some phosphates. Due to the presence of modified urea functions, this material allows for selective and effective enrichment of phosphorylated peptides. It was successfully applied to the enrichment of phosphopeptides from non-fat-milk. The method was applied to the detection of phosphopeptides in a tryptic digest of β-casein where is showed a detection sensitivity as low as 10−10 M. [Figure not available: see fulltext.] © 2016 Springer-Verlag Wien Source

Wu F.,Nankai University | Wu F.,Tianjin Key Laboratory of Protein Science | Hu X.,Nankai University | Hu X.,Tianjin Key Laboratory of Protein Science | And 7 more authors.
Protein and Cell | Year: 2014

Formation of the endoplasmic reticulum (ER) network requires homotypic membrane fusion, which involves a class of atlastin (ATL) GTPases. Purified Drosophila ATL is capable of mediating vesicle fusion in vitro, but such activity has not been reported for any other ATLs. Here, we determined the preliminary crystal structure of the cytosolic segment of Drosophila ATL in a GDP-bound state. The structure reveals a GTPase domain dimer with the subsequent three-helix bundles associating with their own GTPase domains and pointing in opposite directions. This conformation is similar to that of human ATL1, to which GDP and high concentrations of inorganic phosphate, but not GDP only, were included. Drosophila ATL restored ER morphology defects in mammalian cells lacking ATLs, and measurements of nucleotide-dependent dimerization and GTPase activity were comparable for Drosophila ATL and human ATL1. However, purified and reconstituted human ATL1 exhibited no in vitro fusion activity. When the cytosolic segment of human ATL1 was connected to the transmembrane (TM) region and C-terminal tail (CT) of Drosophila ATL, the chimera still exhibited no fusion activity, though its GTPase activity was normal. These results suggest that GDP-bound ATLs may adopt multiple conformations and the in vitro fusion activity of ATL cannot be achieved by a simple collection of functional domains. © 2014, The Author(s). Source

Zhang Z.,Nankai University | Zhang Z.,State Key Laboratory of Medicinal Chemical Biology | Li L.-Y.,Nankai University | Li L.-Y.,State Key Laboratory of Medicinal Chemical Biology
Cancer Microenvironment | Year: 2012

Tumor necrosis factor superfamily-15 (TNFSF15; also known as VEGI or TL1A) is a unique cytokine that functions in the modulation of vascular homeostasis and inflammation. TNFSF15 is expressed abundantly in established vasculature but is down-regulated at sites of neovascularization such as in cancers and wounds. TNFSF15 inhibits endothelial cell proliferation and endothelial progenitor cell differentiation. Additionally, TNFSF15 stimulates T cell activation, Th1 cytokine production, and dendritic cell maturation. Some of the functions of TNFSF15 are mediated by death receptor-3. We review the experimental evidences on TNFSF15 activities in angiogenesis, vasculogenesis, inflammation, and immune system mobilization. © 2012 Springer Science+Business Media B.V. Source

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