LightNet: a novel lightweight convolutional network for brain tumor segmentation in healthcare.

Diagnosis, treatment planning, surveillance, and the monitoring of clinical trials for brain diseases all benefit greatly from neuroimaging-based tumor segmentation. Recently, Convolutional Neural Networks (CNNs) have demonstrated promising results in enhancing the efficiency of image-based brain tumor segmentation. Most current work on CNNs, however, is devoted to creating increasingly complicated convolution modules to improve performance, which in turn raises the computing cost of the model. This work proposes a simple and effective feed-forward CNN, LightNet (Light Network). Based on multi-path and multi-level, it replaces traditional convolutional methods with light operations, which reduces network parameters and redundant feature maps. In the up-sampling stage, a light channel attention module is added to achieve richer multi-scale and spatial semantic feature information extraction of brain tumor. The performance of the network is evaluated in the Multimodal Brain Tumor Segmentation Challenge (BraTS 2015) dataset, and results are presented here alongside other high-performing CNNs. Results show comparable accuracy with other methods but with increased efficiency, segmentation performance, and reduced redundancy and computational complexity. The result is a high-performing network with a balance between efficiency and accuracy, allowing, for example, better energy performance on mobile devices.

Direct effect of protein kinase A on four putative phosphorylation sites of aquaporin 2 in vitro.

The water channel aquaporin 2 (AQP2) has four phosphorylation sites at Ser256, Ser261, Ser264, and Ser269 in the C-terminus and these sites are important for AQP2 bioactivity. However, the exact role of each phosphorylation site still remains unclear. In this study, we generated unique AQP2 mutants in which we eliminated three phosphorylation sites but maintained only one site at the C-terminal end. The AQP2 phosphorylation of each single site by protein kinase A (PKA) was examined by in vitro translation and 32P incorporation. The ability of AQP2 trafficking to the cell membrane was evaluated by cell surface biotinylation. Among the four phosphorylation sites, AQP2 mutant with only S256 preserved the most ability of AQP2 to cell membrane expression. The AQP2 water permeability was measured in oocyte. Ser256 is the most important site for AQP2 function. Interestingly, Ser261 and Ser264 significantly inhibit AQP2 activity. Ser269 slightly but not statistically reduced AQP2 activity. Our data suggest that the four phosphorylation sites execute differential roles in concert in AQP2 functional regulation. AQP2 activity regulated by phosphorylation at Ser256 can be counterbalanced by phosphorylation at Ser261 and Ser264.

[High performance liquid chromatographic fingerprints of triterpene glycosides from Stichopus japonicus].

The fingerprint chromatograms of triterpene glycosides in Stichopus japonicus were established for its quality control. The samples were prepared by solid phase extraction (SPE). The analysis was performed on a Zorbax SB-C18 column (250 mm x 4.6 mm, 5 microm) with acetonitrile-water (containing 0.1% phosphoric acid) as mobile phase at a flow rate of 1.0 mL/min, and at a column temperature of 30 degrees C. The detection wavelength was set at 205 nm. Ten different original samples were analyzed, and 6 peaks were identified as common fingerprint peaks using the similarity evaluation system for the chromatographic fingerprint of traditional Chinese medicine (TCM) recommended by State Pharmacopoeia Committee of China (Version 2004 A). The similarities of the fingerprints were all greater than 0.97. The method is proved to be stable and repeatable and can be utilized as a quality control for S. japonicus.

Determination of triterpene glycosides in sea cucumber (Stichopus japonicus) and its related products by high-performance liquid chromatography.

A creative and sensitive method has been developed for the determination of triterpene glycosides concentrations in sea cucumber ( Stichopus japonicus) and related products by using d-quinovose (6-deoxyglucose) as the measurement standard by reverse-phase high-performance liquid chromatography (HPLC) and variable-wavelength detection. d-quinovose, which is a unique monosaccharide in holostane triterpene glycosides, was liberated by acid hydrolysis and precolumn derivatized by 1-phenyl-3-methyl-5-pyrazolone (PMP). PMP-quinovose was analyzed by HPLC with 22% acetonitrile in 0.05 M KH2PO4 aquatic solution (pH 5.2) as mobile phase. The calibration curves of d-quinovose were linear within the range of 6.56-164 mg/L (r(2) > 0.995). The contents of triterpene glycosides in various S. japonicus products were determined after appropriate pretreatment methods. The concentration of triterpene glycosides was calculated by the formula C = C(qui) x alpha (alpha = 8.5). The result showed that this method was a simple, rapid, and stable method for the determination of triterpene glycosides in S. japonicus products.